Structured Review

Abbott Laboratories ritonavir
Ninety-five percent prediction intervals (P2.5–P97.5) determined from simulated data of <t>atazanavir/ritonavir</t> administered at (a) 300/100 mg once daily, (b) 200/100 mg once daily and (c) 150/100 mg once daily. Observed data are superimposed for the three evaluated regimens.
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1) Product Images from "Population pharmacokinetics of ritonavir-boosted atazanavir in HIV-infected patients and healthy volunteers"

Article Title: Population pharmacokinetics of ritonavir-boosted atazanavir in HIV-infected patients and healthy volunteers

Journal: Journal of Antimicrobial Chemotherapy

doi: 10.1093/jac/dkp102

Ninety-five percent prediction intervals (P2.5–P97.5) determined from simulated data of atazanavir/ritonavir administered at (a) 300/100 mg once daily, (b) 200/100 mg once daily and (c) 150/100 mg once daily. Observed data are superimposed for the three evaluated regimens.
Figure Legend Snippet: Ninety-five percent prediction intervals (P2.5–P97.5) determined from simulated data of atazanavir/ritonavir administered at (a) 300/100 mg once daily, (b) 200/100 mg once daily and (c) 150/100 mg once daily. Observed data are superimposed for the three evaluated regimens.

Techniques Used:

2) Product Images from "Effect of omeprazole on the plasma concentrations of indinavir when administered alone and in combination with ritonavir"

Article Title: Effect of omeprazole on the plasma concentrations of indinavir when administered alone and in combination with ritonavir

Journal: American journal of health-system pharmacy : AJHP : official journal of the American Society of Health-System Pharmacists

doi: 10.2146/ajhp070226

Mean plasma indinavir concentration versus time profiles in study participants receiving indinavir plus placebo, indinavir plus omeprazole 20 mg, indinavir plus omeprazole 40 mg, and indinavir plus ritonavir and omeprazole 40 mg. Vertical bars indicate
Figure Legend Snippet: Mean plasma indinavir concentration versus time profiles in study participants receiving indinavir plus placebo, indinavir plus omeprazole 20 mg, indinavir plus omeprazole 40 mg, and indinavir plus ritonavir and omeprazole 40 mg. Vertical bars indicate

Techniques Used: Concentration Assay

3) Product Images from "Effects of the Human Immunodeficiency Virus-Protease Inhibitor, Ritonavir, on Basal and Catecholamine-Stimulated Lipolysis"

Article Title: Effects of the Human Immunodeficiency Virus-Protease Inhibitor, Ritonavir, on Basal and Catecholamine-Stimulated Lipolysis

Journal: The Journal of clinical endocrinology and metabolism

doi: 10.1210/jc.2004-2194

Activation of ERK 1 and 2 in 3T3-L1 adipocytes treated with ritonavir for 14 d. Samples from 2-h incubations were collected after 1-h preincubation with the ERK inhibitor PD 98059 [dissolved in 0.1% dimethylsulfoxide (DMSO)] or 0.1% DMSO. A, Representative Western blot; B, glycerol release; C, NEFA release; n = 14–15 from three independent experiments. †, P
Figure Legend Snippet: Activation of ERK 1 and 2 in 3T3-L1 adipocytes treated with ritonavir for 14 d. Samples from 2-h incubations were collected after 1-h preincubation with the ERK inhibitor PD 98059 [dissolved in 0.1% dimethylsulfoxide (DMSO)] or 0.1% DMSO. A, Representative Western blot; B, glycerol release; C, NEFA release; n = 14–15 from three independent experiments. †, P

Techniques Used: Activation Assay, Western Blot

Total cellular triglyceride (A) and AP-2 protein expression (B and C) in 3T3-L1 adipocytes treated with ritonavir (Rit) or control medium (0.1% ethanol) for 14 d. Cells were grown in 100-mm dishes. AP-2 protein expression by Western blot was measured in whole-cell lysates collected at 6, 10, and 14 d after initiation of differentiation (as described in Materials and Methods ). A, n = 5–6 from two independent experiments. B and C, n = 6 from two independent experiments.
Figure Legend Snippet: Total cellular triglyceride (A) and AP-2 protein expression (B and C) in 3T3-L1 adipocytes treated with ritonavir (Rit) or control medium (0.1% ethanol) for 14 d. Cells were grown in 100-mm dishes. AP-2 protein expression by Western blot was measured in whole-cell lysates collected at 6, 10, and 14 d after initiation of differentiation (as described in Materials and Methods ). A, n = 5–6 from two independent experiments. B and C, n = 6 from two independent experiments.

Techniques Used: Expressing, Western Blot

4) Product Images from "HIV-1 Genotypic Resistance Patterns Predict Response to Saquinavir-Ritonavir Therapy in Patients in Whom Previous Protease Inhibitor Therapy Had Failed"

Article Title: HIV-1 Genotypic Resistance Patterns Predict Response to Saquinavir-Ritonavir Therapy in Patients in Whom Previous Protease Inhibitor Therapy Had Failed

Journal: Annals of internal medicine

doi:

Virologic response to saquinavir plus ritonavir through week 26 based on response by week 12 See the Methods section for further explanation. Triangles represent nonresponders; diamonds represent partial responders; circles represent complete responders.
Figure Legend Snippet: Virologic response to saquinavir plus ritonavir through week 26 based on response by week 12 See the Methods section for further explanation. Triangles represent nonresponders; diamonds represent partial responders; circles represent complete responders.

Techniques Used:

5) Product Images from "Recent Progress in the Development of HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS"

Article Title: Recent Progress in the Development of HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS

Journal: Journal of medicinal chemistry

doi: 10.1021/acs.jmedchem.5b01697

Structures of ritonavir and cobicistat
Figure Legend Snippet: Structures of ritonavir and cobicistat

Techniques Used:

6) Product Images from "Absent reduction by HIV protease inhibitors of Candida albicans adhesion to endothelial cells"

Article Title: Absent reduction by HIV protease inhibitors of Candida albicans adhesion to endothelial cells

Journal:

doi: 10.1111/j.1439-0507.2006.01353.x

Adherence of Candida albicans CBS 5982 to EAhy 926 cells (a–c) or human umbilical vein endothelial cells (d–f) in the presence of Ritonavir (RTV, left), Indinavir (IDV, centre) or Saquinavir (SQV, right). The bottom boxes show the results
Figure Legend Snippet: Adherence of Candida albicans CBS 5982 to EAhy 926 cells (a–c) or human umbilical vein endothelial cells (d–f) in the presence of Ritonavir (RTV, left), Indinavir (IDV, centre) or Saquinavir (SQV, right). The bottom boxes show the results

Techniques Used:

7) Product Images from "The Acute Effects of HIV Protease Inhibitors on Insulin Suppression of Glucose Production in Healthy HIV-negative Men"

Article Title: The Acute Effects of HIV Protease Inhibitors on Insulin Suppression of Glucose Production in Healthy HIV-negative Men

Journal: Journal of acquired immune deficiency syndromes (1999)

doi: 10.1097/QAI.0b013e3181b03214

Effect of (A) indinavir vs. placebo, (B) ritonavir vs. placebo, and (C) amprenavir vs. placebo on endogenous glucose production during the hyperinsulinemic, euglycemic clamp. Values are mean ± SEM.
Figure Legend Snippet: Effect of (A) indinavir vs. placebo, (B) ritonavir vs. placebo, and (C) amprenavir vs. placebo on endogenous glucose production during the hyperinsulinemic, euglycemic clamp. Values are mean ± SEM.

Techniques Used:

8) Product Images from "Outcomes by Sex Following Treatment Initiation With Atazanavir Plus Ritonavir or Efavirenz With Abacavir/Lamivudine or Tenofovir/Emtricitabine"

Article Title: Outcomes by Sex Following Treatment Initiation With Atazanavir Plus Ritonavir or Efavirenz With Abacavir/Lamivudine or Tenofovir/Emtricitabine

Journal: Clinical Infectious Diseases: An Official Publication of the Infectious Diseases Society of America

doi: 10.1093/cid/cit747

Time to virologic failure ( A ), safety ( B ), and tolerability ( C ) endpoints by sex. Abbreviations: ABC/3TC, abacabir/lamivudine; ATV/r, atazanavir/ritonavir; EFV, efavirenz; TDF/FTC, tenofovir/emtricitabine.
Figure Legend Snippet: Time to virologic failure ( A ), safety ( B ), and tolerability ( C ) endpoints by sex. Abbreviations: ABC/3TC, abacabir/lamivudine; ATV/r, atazanavir/ritonavir; EFV, efavirenz; TDF/FTC, tenofovir/emtricitabine.

Techniques Used:

9) Product Images from "Effect of a Modified Saquinavir/Ritonavir Dosing Regimen with Lower Dose Lead-In Phase on QTc Interval, Pharmacokinetics, Antiviral Activity and Safety in Treatment-Naïve HIV-1-Infected Patients"

Article Title: Effect of a Modified Saquinavir/Ritonavir Dosing Regimen with Lower Dose Lead-In Phase on QTc Interval, Pharmacokinetics, Antiviral Activity and Safety in Treatment-Naïve HIV-1-Infected Patients

Journal: Drugs in R & D

doi: 10.1007/s40268-015-0087-7

Mean plasma concentration–time profiles following administration of the modified saquinavir/ritonavir regimen for a saquinavir and b ritonavir
Figure Legend Snippet: Mean plasma concentration–time profiles following administration of the modified saquinavir/ritonavir regimen for a saquinavir and b ritonavir

Techniques Used: Concentration Assay, Modification

10) Product Images from "EFFECT OF ULTRA-HIGH PRESSURE HOMOGENIZATION ON THE INTERACTION BETWEEN BOVINE CASEIN MICELLES AND RITONAVIR"

Article Title: EFFECT OF ULTRA-HIGH PRESSURE HOMOGENIZATION ON THE INTERACTION BETWEEN BOVINE CASEIN MICELLES AND RITONAVIR

Journal: Pharmaceutical research

doi: 10.1007/s11095-014-1518-9

Stability of ritonavir-casein micellar systems and improvement of ritonavir dispersibility after interaction with caseins
Figure Legend Snippet: Stability of ritonavir-casein micellar systems and improvement of ritonavir dispersibility after interaction with caseins

Techniques Used:

HPLC chromatogram of ritonavir (RIT) recovered from skim milk. Peak marked as * corresponds to proteins that remained after the extraction process
Figure Legend Snippet: HPLC chromatogram of ritonavir (RIT) recovered from skim milk. Peak marked as * corresponds to proteins that remained after the extraction process

Techniques Used: High Performance Liquid Chromatography

Intrinsic fluorescence emission spectra of pure ritonavir (RIT) and skim milk (SM) controls and RIT-SM systems obtained at 0.1, 300 and 500 MPa
Figure Legend Snippet: Intrinsic fluorescence emission spectra of pure ritonavir (RIT) and skim milk (SM) controls and RIT-SM systems obtained at 0.1, 300 and 500 MPa

Techniques Used: Fluorescence

DSC thermograms of pure ritonavir (RIT), non-homogenized skim milk (SM) and RIT-SM mixtures with different RIT content (0.4 – 15%, w/w)
Figure Legend Snippet: DSC thermograms of pure ritonavir (RIT), non-homogenized skim milk (SM) and RIT-SM mixtures with different RIT content (0.4 – 15%, w/w)

Techniques Used:

11) Product Images from "Ultra-Fast Analysis of Plasma and Intracellular Levels of HIV Protease Inhibitors in Children: A Clinical Application of MALDI Mass Spectrometry"

Article Title: Ultra-Fast Analysis of Plasma and Intracellular Levels of HIV Protease Inhibitors in Children: A Clinical Application of MALDI Mass Spectrometry

Journal: PLoS ONE

doi: 10.1371/journal.pone.0011409

Lopinavir and ritonavir concentrations in an HIV infected child determined by HPLC-UV and by MALDI-triple quadrupole MS. Pharmacokinetic curve of lopinavir and ritonavir in one HIV infected child determined by HPLC-UV (triangles for lopinavir and crosses for ritonavir), MALDI-triple quadrupole MS (diamonds for lopinavir and circles for ritonavir), and MALDI-triple quadrupole MS when ten additional drugs (10 µM per drug) were spiked to the patient's samples (squares for lopinavir and pluses for ritonavir).
Figure Legend Snippet: Lopinavir and ritonavir concentrations in an HIV infected child determined by HPLC-UV and by MALDI-triple quadrupole MS. Pharmacokinetic curve of lopinavir and ritonavir in one HIV infected child determined by HPLC-UV (triangles for lopinavir and crosses for ritonavir), MALDI-triple quadrupole MS (diamonds for lopinavir and circles for ritonavir), and MALDI-triple quadrupole MS when ten additional drugs (10 µM per drug) were spiked to the patient's samples (squares for lopinavir and pluses for ritonavir).

Techniques Used: Infection, High Performance Liquid Chromatography, Mass Spectrometry

12) Product Images from "Unexpected Hepatotoxicity of Rifampin and Saquinavir/Ritonavir in Healthy Male Volunteers"

Article Title: Unexpected Hepatotoxicity of Rifampin and Saquinavir/Ritonavir in Healthy Male Volunteers

Journal: Archives of Drug Information

doi: 10.1111/j.1753-5174.2009.00017.x

Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) elevations for all nine participants in study arm 2 who commenced rifampin (600 mg once daily) + saquinavir/ritonavir (1000/100 mg twice daily) after 14 days of rifampin alone. Falling levels are post-discontinuation. Numbers indicated are participant identifiers. (a) ALT; (b) AST.
Figure Legend Snippet: Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) elevations for all nine participants in study arm 2 who commenced rifampin (600 mg once daily) + saquinavir/ritonavir (1000/100 mg twice daily) after 14 days of rifampin alone. Falling levels are post-discontinuation. Numbers indicated are participant identifiers. (a) ALT; (b) AST.

Techniques Used: AST Assay

Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) levels for two participants in study arm 1 who developed significant (grades 2 and 3) elevations in ALT following concomitant dosing of rifampin (600 mg once daily) with saquinavir/ritonavir (1000/100 mg twice daily). Participants took saquinavir/ritonavir alone for days 1 to 14. Falling levels are postdiscontinuation. Numbers indicated are participant identifiers.
Figure Legend Snippet: Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) levels for two participants in study arm 1 who developed significant (grades 2 and 3) elevations in ALT following concomitant dosing of rifampin (600 mg once daily) with saquinavir/ritonavir (1000/100 mg twice daily). Participants took saquinavir/ritonavir alone for days 1 to 14. Falling levels are postdiscontinuation. Numbers indicated are participant identifiers.

Techniques Used: AST Assay

13) Product Images from "The HIV protease inhibitor ritonavir blocks osteoclastogenesis and function by impairing RANKL-induced signaling"

Article Title: The HIV protease inhibitor ritonavir blocks osteoclastogenesis and function by impairing RANKL-induced signaling

Journal: Journal of Clinical Investigation

doi: 10.1172/JCI200415797

Ritonavir inhibits RANKL-induced NF-κB activation. ( A ) Bone marrow macrophages pretreated with ritonavir (20 μg/ml) or vehicle for 1 hour were stimulated with RANKL for the indicated time points, and protein lysates were prepared for IκBα immunoblot. Ritonavir pretreatment impairs RANKL-induced degradation of IκBα. ( B ) Bone marrow macrophages pretreated with ritonavir (20 μg/ml) for the indicated time were stimulated with RANKL for 15 minutes and evaluated for NF-κB activation. Ritonavir inhibits NF-κB activation as assessed by EMSA after 1 hour and after 18 hours of pretreatment (Pretx). Numbers below lanes indicate relative band intensity. ( C ) Cell lysates prepared as in A and immunoblotted for phospho-IκBα (p-IκBα) and IκBα reveal similar levels of phospho-IκBα intensity, irrespective of ritonavir pretreatment, despite the failure of ritonavir pretreatment to decrease total IκBα levels. β-Actin immunoblots confirm similar amounts of cell extracts were analyzed.
Figure Legend Snippet: Ritonavir inhibits RANKL-induced NF-κB activation. ( A ) Bone marrow macrophages pretreated with ritonavir (20 μg/ml) or vehicle for 1 hour were stimulated with RANKL for the indicated time points, and protein lysates were prepared for IκBα immunoblot. Ritonavir pretreatment impairs RANKL-induced degradation of IκBα. ( B ) Bone marrow macrophages pretreated with ritonavir (20 μg/ml) for the indicated time were stimulated with RANKL for 15 minutes and evaluated for NF-κB activation. Ritonavir inhibits NF-κB activation as assessed by EMSA after 1 hour and after 18 hours of pretreatment (Pretx). Numbers below lanes indicate relative band intensity. ( C ) Cell lysates prepared as in A and immunoblotted for phospho-IκBα (p-IκBα) and IκBα reveal similar levels of phospho-IκBα intensity, irrespective of ritonavir pretreatment, despite the failure of ritonavir pretreatment to decrease total IκBα levels. β-Actin immunoblots confirm similar amounts of cell extracts were analyzed.

Techniques Used: Activation Assay, Western Blot

RANKL-induced recruitment of c-Src and TRAF6 to lipid raft component is inhibited by ritonavir treatment. Preosteoclasts generated after 3 days of culture with RANKL and M-CSF were starved for 3 hours, followed by pretreatment with either vehicle or ritonavir (1 hour). Cells were then stimulated with RANKL for 5 minutes, followed by lipid raft isolation. Note the continued recruitment of TRAF2 to lipid rafts with ritonavir treatment, indicating that the inhibition is specific to TRAF6 and c-Src.
Figure Legend Snippet: RANKL-induced recruitment of c-Src and TRAF6 to lipid raft component is inhibited by ritonavir treatment. Preosteoclasts generated after 3 days of culture with RANKL and M-CSF were starved for 3 hours, followed by pretreatment with either vehicle or ritonavir (1 hour). Cells were then stimulated with RANKL for 5 minutes, followed by lipid raft isolation. Note the continued recruitment of TRAF2 to lipid rafts with ritonavir treatment, indicating that the inhibition is specific to TRAF6 and c-Src.

Techniques Used: Generated, Isolation, Inhibition

Introduction of PI3K-CA restores RANKL-induced phosphorylation of Akt and osteoclast actin ring formation in the presence of ritonavir. ( A ) Retroviral transduction of either vector or PI3K-CA (p110a-CA) into bone marrow macrophages was followed by 3 days of culture in selection media, M-CSF, and RANKL. After starvation (3 hours) and pretreatment (1 hour) with either vehicle or ritonavir, cells were stimulated with RANKL for 15 minutes. Immunoblots reveal restoration of RANKL-induced Akt phosphorylation when PI3K-CA is introduced. As expected, total PI3K is enhanced as a result of transduction (p110α blot). TRAF6 Western blots act as a loading control. ( B ) Percentage of osteoclasts with intact actin rings after ritonavir exposure is quantitated. ( C ) Osteoclasts, retrovirally transduced with either vector or PI3K-CA, were generated on glass coverslips. After 4 days, cells were exposed to various doses of ritonavir for 2 hours, then processed for immunofluorescence microscopy for β-actin. Dose-dependent disruption of the characteristic actin ring of the osteoclast cytoskeleton is observed in vector but not PI3K-CA–transduced cells.
Figure Legend Snippet: Introduction of PI3K-CA restores RANKL-induced phosphorylation of Akt and osteoclast actin ring formation in the presence of ritonavir. ( A ) Retroviral transduction of either vector or PI3K-CA (p110a-CA) into bone marrow macrophages was followed by 3 days of culture in selection media, M-CSF, and RANKL. After starvation (3 hours) and pretreatment (1 hour) with either vehicle or ritonavir, cells were stimulated with RANKL for 15 minutes. Immunoblots reveal restoration of RANKL-induced Akt phosphorylation when PI3K-CA is introduced. As expected, total PI3K is enhanced as a result of transduction (p110α blot). TRAF6 Western blots act as a loading control. ( B ) Percentage of osteoclasts with intact actin rings after ritonavir exposure is quantitated. ( C ) Osteoclasts, retrovirally transduced with either vector or PI3K-CA, were generated on glass coverslips. After 4 days, cells were exposed to various doses of ritonavir for 2 hours, then processed for immunofluorescence microscopy for β-actin. Dose-dependent disruption of the characteristic actin ring of the osteoclast cytoskeleton is observed in vector but not PI3K-CA–transduced cells.

Techniques Used: Transduction, Plasmid Preparation, Selection, Western Blot, Activated Clotting Time Assay, Generated, Immunofluorescence, Microscopy

Osteoclast function is impaired by ritonavir. ( A ) Osteoclasts, generated on whale dentine slices for 3 days by treatment with RANKL and M-CSF, were exposed to control medium, ritonavir (10 μg/ml), or indinavir (10 μg/ml) for an additional 2 days. TRAP-stained dentine slices show no change in osteoclast number with exposure to PIs (top panels). Following cell removal, Coomassie blue staining of dentine slices show decreased bone pits with ritonavir treatment (bottom panels). Magnification, ×100. ( B ) Ritonavir, but not indinavir, decreases pit number (per 0.36 mm 2 ), percentage of pit area, and pit depth (in micrometers) by half (each P
Figure Legend Snippet: Osteoclast function is impaired by ritonavir. ( A ) Osteoclasts, generated on whale dentine slices for 3 days by treatment with RANKL and M-CSF, were exposed to control medium, ritonavir (10 μg/ml), or indinavir (10 μg/ml) for an additional 2 days. TRAP-stained dentine slices show no change in osteoclast number with exposure to PIs (top panels). Following cell removal, Coomassie blue staining of dentine slices show decreased bone pits with ritonavir treatment (bottom panels). Magnification, ×100. ( B ) Ritonavir, but not indinavir, decreases pit number (per 0.36 mm 2 ), percentage of pit area, and pit depth (in micrometers) by half (each P

Techniques Used: Generated, Staining

Ritonavir blocks PTH-induced osteoclast formation in vivo. ( A ) Osteoclast number was determined from TRAP-stained histologic sections of calvariae from mice stimulated with PTH or vehicle and intraperitoneally injected with ritonavir or vehicle. Ritonavir abrogates the osteoclast increase stimulated by PTH ( n = 3 mice per group; P
Figure Legend Snippet: Ritonavir blocks PTH-induced osteoclast formation in vivo. ( A ) Osteoclast number was determined from TRAP-stained histologic sections of calvariae from mice stimulated with PTH or vehicle and intraperitoneally injected with ritonavir or vehicle. Ritonavir abrogates the osteoclast increase stimulated by PTH ( n = 3 mice per group; P

Techniques Used: In Vivo, Staining, Mouse Assay, Injection

Ritonavir inhibits RANKL-induced Akt activation. ( A ) RAW 264.7 cells pretreated with ritonavir (2 μg/ml) for 1 hour and stimulated with RANKL (+RANKL) for the indicated time points. Phospho-Akt (p-Akt), total Akt (Akt), and phospho-FKHR (p-FKHR) immunoblots were performed on cell extracts. Immunoblots reveal impaired Akt and FKHR phosphorylation with ritonavir pretreatment. ( B ) Osteoclasts were stimulated with either RANKL or M-CSF for the indicated time points, and cell extracts were immunoblotted for Akt activation. Ritonavir inhibits only RANKL-induced Akt activation but not that stimulated by M-CSF. Total Akt immunoblots confirm that similar amounts of cell extracts were analyzed. +V, vehicle pretreatment; +R, ritonavir pretreatment.
Figure Legend Snippet: Ritonavir inhibits RANKL-induced Akt activation. ( A ) RAW 264.7 cells pretreated with ritonavir (2 μg/ml) for 1 hour and stimulated with RANKL (+RANKL) for the indicated time points. Phospho-Akt (p-Akt), total Akt (Akt), and phospho-FKHR (p-FKHR) immunoblots were performed on cell extracts. Immunoblots reveal impaired Akt and FKHR phosphorylation with ritonavir pretreatment. ( B ) Osteoclasts were stimulated with either RANKL or M-CSF for the indicated time points, and cell extracts were immunoblotted for Akt activation. Ritonavir inhibits only RANKL-induced Akt activation but not that stimulated by M-CSF. Total Akt immunoblots confirm that similar amounts of cell extracts were analyzed. +V, vehicle pretreatment; +R, ritonavir pretreatment.

Techniques Used: Activation Assay, Western Blot

Osteoclastogenesis is impaired by ritonavir but not indinavir. ( A ) Osteoclasts were generated from bone marrow macrophages stimulated with RANKL and M-CSF for 4 days in the presence of the indicated doses of ritonavir or indinavir. TRAP solution assay quantitation of osteoclast formation shows that the IC 50 for ritonavir is near 10 μg/ml. In contrast, cultures exposed to indinavir show no inhibition or enhancement of osteoclast formation. ( B ) Representative fields of TRAP-stained osteoclasts in the presence of control medium, indinavir (10 μg/ml), and ritonavir (10 μg/ml). Magnification, ×100. ( C ) Ritonavir dose dependently suppresses osteoclast gene markers determined by RT-PCR analysis of osteoclasts on day 4 culture.
Figure Legend Snippet: Osteoclastogenesis is impaired by ritonavir but not indinavir. ( A ) Osteoclasts were generated from bone marrow macrophages stimulated with RANKL and M-CSF for 4 days in the presence of the indicated doses of ritonavir or indinavir. TRAP solution assay quantitation of osteoclast formation shows that the IC 50 for ritonavir is near 10 μg/ml. In contrast, cultures exposed to indinavir show no inhibition or enhancement of osteoclast formation. ( B ) Representative fields of TRAP-stained osteoclasts in the presence of control medium, indinavir (10 μg/ml), and ritonavir (10 μg/ml). Magnification, ×100. ( C ) Ritonavir dose dependently suppresses osteoclast gene markers determined by RT-PCR analysis of osteoclasts on day 4 culture.

Techniques Used: Generated, Quantitation Assay, Inhibition, Staining, Reverse Transcription Polymerase Chain Reaction

14) Product Images from "Reciprocal Effects of Antiretroviral Drugs Used To Treat HIV Infection on the Fibroblast Growth Factor 21/β-Klotho System"

Article Title: Reciprocal Effects of Antiretroviral Drugs Used To Treat HIV Infection on the Fibroblast Growth Factor 21/β-Klotho System

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.00029-18

Effects of antiretroviral drugs, tunicamycin, and thapsigargin on the expression of FGF21 , CHOP10 , and HSPA5 mRNAs and FGF21 release into the cell culture medium in human LHCN-M2 skeletal muscle cells differentiated in culture. LHCN-M2 myotubes differentiated in culture were treated for 24 h, as indicated, with the following drugs: zidovudine (AZT), 100 μM; stavudine (D4T), 100 μM; tenofovir disoproxil fumarate (TDF), 5 μM; nevirapine (NVP), 20 μM; efavirenz (EFV), 50 μM; rilpivirine (RPV), 10 μM; lopinavir-ritonavir 4:1 (LPV/r), 20 μM; ritonavir (RTV), 20 μM; lopinavir (LPV), 20 μM; nelfinavir (NFV), 20 μM; atazanavir (ATV), 50 μM; maraviroc (MRV), 4 μM; tunicamycin (TUN), 2 μM; thapsigargin (THAP), 2 μM. (A) mRNA levels are presented as means ± SEM from 4 to 5 independent experiments and are expressed relative to values for control cells (defined as 1). (B) FGF21 protein levels in cell culture medium. Data are presented as means ± SEM from 4 to 5 independent experiments. *, P
Figure Legend Snippet: Effects of antiretroviral drugs, tunicamycin, and thapsigargin on the expression of FGF21 , CHOP10 , and HSPA5 mRNAs and FGF21 release into the cell culture medium in human LHCN-M2 skeletal muscle cells differentiated in culture. LHCN-M2 myotubes differentiated in culture were treated for 24 h, as indicated, with the following drugs: zidovudine (AZT), 100 μM; stavudine (D4T), 100 μM; tenofovir disoproxil fumarate (TDF), 5 μM; nevirapine (NVP), 20 μM; efavirenz (EFV), 50 μM; rilpivirine (RPV), 10 μM; lopinavir-ritonavir 4:1 (LPV/r), 20 μM; ritonavir (RTV), 20 μM; lopinavir (LPV), 20 μM; nelfinavir (NFV), 20 μM; atazanavir (ATV), 50 μM; maraviroc (MRV), 4 μM; tunicamycin (TUN), 2 μM; thapsigargin (THAP), 2 μM. (A) mRNA levels are presented as means ± SEM from 4 to 5 independent experiments and are expressed relative to values for control cells (defined as 1). (B) FGF21 protein levels in cell culture medium. Data are presented as means ± SEM from 4 to 5 independent experiments. *, P

Techniques Used: Expressing, Cell Culture

Effects of antiretroviral drugs on the expression of FGF21 , KLB, CHOP10 , and HSPA5 mRNAs and on FGF21 promoter activity in human hepatic HepG2 cells. Cells were exposed, when indicated, to the following drugs: zidovudine (AZT), 100 μM; stavudine (D4T), 100 μM; tenofovir disoproxil fumarate (TDF), 5 μM; nevirapine (NVP), 20 μM; efavirenz (EFV), 50 μM; rilpivirine (RPV), 10 μM; lopinavir-ritonavir 4:1 (LPV/r), 20 μM; ritonavir (RTV), 20 μM; lopinavir (LPV), 20 μM; nelfinavir (NFV), 20 μM; atazanavir (ATV), 50 μM; raltegravir (RAL), 50 μM; elvitegravir (ELV), 50 μM; maraviroc (MRV), 4 μM; tunicamycin (TUN), 2 μM; thapsigargin (THAP), 2 μM. (A) mRNA levels are presented as means ± SEM from 4 to 5 independent experiments and are expressed relative to values for control cells (defined as 1). (B) FGF21 protein levels in cell culture medium. (C) Luciferase activity in HepG2 cells transiently transfected with plasmid constructs in which luciferase is driven by the −1,497/+5 (−1.5 kb-Luc) or −77/+5 (−77 bp-Luc) 5′ regions of the FGF21 gene. Cells were treated for 24 h with the indicated concentrations of drugs: EFV, 50 μM; LPV/r, 20 μM; THAP, 2 μM. Data are normalized to Renilla luciferase activity driven by the cotransfected pRL-CMV plasmid. Data are means ± SEM from 4 to 5 independent experiments. *, P
Figure Legend Snippet: Effects of antiretroviral drugs on the expression of FGF21 , KLB, CHOP10 , and HSPA5 mRNAs and on FGF21 promoter activity in human hepatic HepG2 cells. Cells were exposed, when indicated, to the following drugs: zidovudine (AZT), 100 μM; stavudine (D4T), 100 μM; tenofovir disoproxil fumarate (TDF), 5 μM; nevirapine (NVP), 20 μM; efavirenz (EFV), 50 μM; rilpivirine (RPV), 10 μM; lopinavir-ritonavir 4:1 (LPV/r), 20 μM; ritonavir (RTV), 20 μM; lopinavir (LPV), 20 μM; nelfinavir (NFV), 20 μM; atazanavir (ATV), 50 μM; raltegravir (RAL), 50 μM; elvitegravir (ELV), 50 μM; maraviroc (MRV), 4 μM; tunicamycin (TUN), 2 μM; thapsigargin (THAP), 2 μM. (A) mRNA levels are presented as means ± SEM from 4 to 5 independent experiments and are expressed relative to values for control cells (defined as 1). (B) FGF21 protein levels in cell culture medium. (C) Luciferase activity in HepG2 cells transiently transfected with plasmid constructs in which luciferase is driven by the −1,497/+5 (−1.5 kb-Luc) or −77/+5 (−77 bp-Luc) 5′ regions of the FGF21 gene. Cells were treated for 24 h with the indicated concentrations of drugs: EFV, 50 μM; LPV/r, 20 μM; THAP, 2 μM. Data are normalized to Renilla luciferase activity driven by the cotransfected pRL-CMV plasmid. Data are means ± SEM from 4 to 5 independent experiments. *, P

Techniques Used: Expressing, Activity Assay, Cell Culture, Luciferase, Transfection, Plasmid Preparation, Construct

Effects of the ER stress-response inhibitor PBA and the antioxidant Trolox on the actions of antiretroviral drugs on the expression of FGF21 , KLB , CHOP10 , and HSPA5 mRNAs in human SGBS adipocytes differentiated in culture. SGBS human preadipocytes were differentiated in culture into adipocytes and treated for 24 h with the following drugs: efavirenz (EFV), 20 μM; rilpivirine (RPV), 10 μM; lopinavir-ritonavir 4:1 (LPV/r), 20 μM; elvitegravir (ELV) 10 μM; tunicamycin (TUN), 2 μM; thapsigargin (THAP), 2 μM. Where indicated, cells were cultured in the presence of 2 mM PBA or 1 mM Trolox. Data are presented as means ± SEM from 4 to 5 independent experiments and are expressed relative to values for control cells (defined as 1). *, P
Figure Legend Snippet: Effects of the ER stress-response inhibitor PBA and the antioxidant Trolox on the actions of antiretroviral drugs on the expression of FGF21 , KLB , CHOP10 , and HSPA5 mRNAs in human SGBS adipocytes differentiated in culture. SGBS human preadipocytes were differentiated in culture into adipocytes and treated for 24 h with the following drugs: efavirenz (EFV), 20 μM; rilpivirine (RPV), 10 μM; lopinavir-ritonavir 4:1 (LPV/r), 20 μM; elvitegravir (ELV) 10 μM; tunicamycin (TUN), 2 μM; thapsigargin (THAP), 2 μM. Where indicated, cells were cultured in the presence of 2 mM PBA or 1 mM Trolox. Data are presented as means ± SEM from 4 to 5 independent experiments and are expressed relative to values for control cells (defined as 1). *, P

Techniques Used: Expressing, Cell Culture

Effects of antiretroviral drugs on the expression of FGF21 , KLB , CHOP10 , and HSPA5 mRNAs in human SGBS adipocytes and on KLB promoter activity in adipogenic cells. (A) SGBS human preadipocytes were differentiated in culture into adipocytes in the presence of the following drugs: zidovudine (AZT), 50 μM; stavudine (D4T), 50 μM; efavirenz (EFV), 5 μM; rilpivirine (RPV), 10 μM; lopinavir-ritonavir 4:1 (LPV/r), 20 μM; raltegravir (RAL), 5 μM; elvitegravir (ELV), 5 μM. (B) SGBS human adipocytes were differentiated in culture into adipocytes and treated for 24 h with the following drugs: AZT, 100 μM; D4T, 100 μM; EFV, 20 μM; RPV, 15 μM; LPV/r, 20 μM; ELV, 20 μM; tunicamycin (TUN), 2 μM; thapsigargin (THAP), 2 μM. Data are presented as means ± SEM from 4 to 5 independent experiments and are expressed relative to values for control cells (defined as 1). (C) Luciferase activity in adipogenic HIB-1B cells transiently transfected with a plasmid construct in which luciferase is driven by the −1,055/+45 region of the KLB gene. Cells were treated with the following drugs: EFV, 50 μM; LPV/r, 20 μM; TUN, 2 μM; THAP, 2 μM; rosiglitazone (ROSI), 2 μM. Data are normalized to Renilla luciferase activity driven by the cotransfected pRL-CMV plasmid. *, P
Figure Legend Snippet: Effects of antiretroviral drugs on the expression of FGF21 , KLB , CHOP10 , and HSPA5 mRNAs in human SGBS adipocytes and on KLB promoter activity in adipogenic cells. (A) SGBS human preadipocytes were differentiated in culture into adipocytes in the presence of the following drugs: zidovudine (AZT), 50 μM; stavudine (D4T), 50 μM; efavirenz (EFV), 5 μM; rilpivirine (RPV), 10 μM; lopinavir-ritonavir 4:1 (LPV/r), 20 μM; raltegravir (RAL), 5 μM; elvitegravir (ELV), 5 μM. (B) SGBS human adipocytes were differentiated in culture into adipocytes and treated for 24 h with the following drugs: AZT, 100 μM; D4T, 100 μM; EFV, 20 μM; RPV, 15 μM; LPV/r, 20 μM; ELV, 20 μM; tunicamycin (TUN), 2 μM; thapsigargin (THAP), 2 μM. Data are presented as means ± SEM from 4 to 5 independent experiments and are expressed relative to values for control cells (defined as 1). (C) Luciferase activity in adipogenic HIB-1B cells transiently transfected with a plasmid construct in which luciferase is driven by the −1,055/+45 region of the KLB gene. Cells were treated with the following drugs: EFV, 50 μM; LPV/r, 20 μM; TUN, 2 μM; THAP, 2 μM; rosiglitazone (ROSI), 2 μM. Data are normalized to Renilla luciferase activity driven by the cotransfected pRL-CMV plasmid. *, P

Techniques Used: Expressing, Activity Assay, Luciferase, Transfection, Plasmid Preparation, Construct

15) Product Images from "Potencies of Human Immunodeficiency Virus Protease Inhibitors In Vitro against Plasmodium falciparum and In Vivo against Murine Malaria"

Article Title: Potencies of Human Immunodeficiency Virus Protease Inhibitors In Vitro against Plasmodium falciparum and In Vivo against Murine Malaria

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.50.2.639-648.2006

Connolly surface of active site of PfPM-II (1lf3) in complex with docked ritonavir showing enzyme subsites S3-S2′.
Figure Legend Snippet: Connolly surface of active site of PfPM-II (1lf3) in complex with docked ritonavir showing enzyme subsites S3-S2′.

Techniques Used:

In vivo efficacy of HIV-1 protease inhibitors against murine malaria. Female C57BL/6J mice infected with 10 5 P. chabaudi AS-parasitized erythrocytes were treated orally, twice daily, for 8 consecutive days starting 24 h p.i. with either (A) vehicle, (B) 10 mg/kg each ritonavir and saquinavir, (C) 10 mg/kg ritonavir and 40 mg/kg lopinavir, (D) 10 mg/kg ritonavir, or (E) 10 mg/kg saquinavir. Parasitemia was monitored for 25 days from day 4 p.i. No parasitemia developed in Malarone-treated mice (not shown).
Figure Legend Snippet: In vivo efficacy of HIV-1 protease inhibitors against murine malaria. Female C57BL/6J mice infected with 10 5 P. chabaudi AS-parasitized erythrocytes were treated orally, twice daily, for 8 consecutive days starting 24 h p.i. with either (A) vehicle, (B) 10 mg/kg each ritonavir and saquinavir, (C) 10 mg/kg ritonavir and 40 mg/kg lopinavir, (D) 10 mg/kg ritonavir, or (E) 10 mg/kg saquinavir. Parasitemia was monitored for 25 days from day 4 p.i. No parasitemia developed in Malarone-treated mice (not shown).

Techniques Used: In Vivo, Mouse Assay, Infection

16) Product Images from "Contribution of CYP2C19 and CYP3A4 to the formation of the active nortilidine from the prodrug tilidine"

Article Title: Contribution of CYP2C19 and CYP3A4 to the formation of the active nortilidine from the prodrug tilidine

Journal: British Journal of Clinical Pharmacology

doi: 10.1111/j.1365-2125.2012.04261.x

Partial metabolic clearances and urinary excretion of tilidine and metabolites after oral administration of 100 mg tilidine solution to 14 healthy subjects during placebo (left) or ritonavir treatment (right)
Figure Legend Snippet: Partial metabolic clearances and urinary excretion of tilidine and metabolites after oral administration of 100 mg tilidine solution to 14 healthy subjects during placebo (left) or ritonavir treatment (right)

Techniques Used:

Determination of tilidine, its metabolites and ritonavir in plasma
Figure Legend Snippet: Determination of tilidine, its metabolites and ritonavir in plasma

Techniques Used:

17) Product Images from "Ritonavir analogues as a probe for deciphering the cytochrome P450 3A4 inhibitory mechanism"

Article Title: Ritonavir analogues as a probe for deciphering the cytochrome P450 3A4 inhibitory mechanism

Journal: Current topics in medicinal chemistry

doi:

A , Superposition of the ritonavir- and analogue-bound structures of CYP3A4. Ritonavir is shown in black; GS3 in blue; GS4-1 and GS4-2 are in green and gray, respectively; visible parts of GS5-1 and GS5-2 are in cyan; GS6 in magenta; GS7 in red; and GS8 in yellow. Molecular features defining the ligand binding affinity are boxed and numbered according to their contribution. I – the heme-ligating group is most important as it drives the ligand binding reaction and determines the strength and reversibility of the Fe-N bond. II – the desoxyritonavir backbone is preferable because it is more flexible and allows ligands to adopt a more optimal conformation in the active site. III – the aromatic moiety in Phe-2 position promotes π-π stacking interactions with the heme-ligating group and cation-π interactions with the Arg105 guanidinium group. IV – a bulky hydrophobic group at Phe-1 position is required for potent CYP3A4 inhibition. V – a hydrogen bond to Ser119 via the backbone amide nitrogen or carbonyl oxygen facilitates the CYP3A4-ligand association and stabilizes the ligand-bound form. VI – a poly-functional end-group can contribute to the binding affinity through polar, hydrophobic, π- π, S-π and possibly other interactions established with the residues of ‘polar umbrella’ and the F-F’-loop. B , Superposition of all available CYP3A4 structures showing that the F-F’-loop is very flexible and either adopts a unique conformation to optimize ligand-protein contacts or becomes disordered. Color coding: 1TQN – deep purple, 1WOE – green, 1WOF – orange, 1WOG – pale yellow, 2JOD – brown, 2VOM – gray, 3NXU – cyan, 3UA1 – purple, 3TJS – beige, 4I3Q – dark green, 4I4G – white, 4I4H – blue, 4K9T - black, 4K9U – pale green, 4K9V - magenta, 4K9W – red, and 4K9X – yellow. To simplify viewing, all ligands were excluded from the active site.
Figure Legend Snippet: A , Superposition of the ritonavir- and analogue-bound structures of CYP3A4. Ritonavir is shown in black; GS3 in blue; GS4-1 and GS4-2 are in green and gray, respectively; visible parts of GS5-1 and GS5-2 are in cyan; GS6 in magenta; GS7 in red; and GS8 in yellow. Molecular features defining the ligand binding affinity are boxed and numbered according to their contribution. I – the heme-ligating group is most important as it drives the ligand binding reaction and determines the strength and reversibility of the Fe-N bond. II – the desoxyritonavir backbone is preferable because it is more flexible and allows ligands to adopt a more optimal conformation in the active site. III – the aromatic moiety in Phe-2 position promotes π-π stacking interactions with the heme-ligating group and cation-π interactions with the Arg105 guanidinium group. IV – a bulky hydrophobic group at Phe-1 position is required for potent CYP3A4 inhibition. V – a hydrogen bond to Ser119 via the backbone amide nitrogen or carbonyl oxygen facilitates the CYP3A4-ligand association and stabilizes the ligand-bound form. VI – a poly-functional end-group can contribute to the binding affinity through polar, hydrophobic, π- π, S-π and possibly other interactions established with the residues of ‘polar umbrella’ and the F-F’-loop. B , Superposition of all available CYP3A4 structures showing that the F-F’-loop is very flexible and either adopts a unique conformation to optimize ligand-protein contacts or becomes disordered. Color coding: 1TQN – deep purple, 1WOE – green, 1WOF – orange, 1WOG – pale yellow, 2JOD – brown, 2VOM – gray, 3NXU – cyan, 3UA1 – purple, 3TJS – beige, 4I3Q – dark green, 4I4G – white, 4I4H – blue, 4K9T - black, 4K9U – pale green, 4K9V - magenta, 4K9W – red, and 4K9X – yellow. To simplify viewing, all ligands were excluded from the active site.

Techniques Used: Ligand Binding Assay, Inhibition, Functional Assay, Binding Assay

A , Absorbance spectra of the ferric ligand-free and ritonavir-bound CYP3A4 (black and red, respectively) and its ferrous ritonavir-bound form (blue). Absorbance maxima for each species are indicated. B , Atypical (V-shaped) dependence of the rate constant for the ritonavir binding reaction on ligand concentration. C , Active site of ritonavir-bound CYP3A4.
Figure Legend Snippet: A , Absorbance spectra of the ferric ligand-free and ritonavir-bound CYP3A4 (black and red, respectively) and its ferrous ritonavir-bound form (blue). Absorbance maxima for each species are indicated. B , Atypical (V-shaped) dependence of the rate constant for the ritonavir binding reaction on ligand concentration. C , Active site of ritonavir-bound CYP3A4.

Techniques Used: Binding Assay, Concentration Assay

Binding mode of DTMCR. DTMCR (green) ligates to CYP3A4 via the terminal amino group and rotates by 180° relative to ritonavir in order to place the Phe-2 group into the Phe-1 pocket. The F-F’ loop is well ordered in the ligand-free protein (shown in orange) but disordered in the CYP3A4-DTMCR complex. DTMCR does not clash with the 369–371 peptide but displaces the I-helix as much as ritonavir does. The I-helix and the 369–371 peptide of the ligand-free form are displayed in yellow.
Figure Legend Snippet: Binding mode of DTMCR. DTMCR (green) ligates to CYP3A4 via the terminal amino group and rotates by 180° relative to ritonavir in order to place the Phe-2 group into the Phe-1 pocket. The F-F’ loop is well ordered in the ligand-free protein (shown in orange) but disordered in the CYP3A4-DTMCR complex. DTMCR does not clash with the 369–371 peptide but displaces the I-helix as much as ritonavir does. The I-helix and the 369–371 peptide of the ligand-free form are displayed in yellow.

Techniques Used: Binding Assay

A , Absorbance spectra of the ferrous GS1-, GS2- and GS3-bound CYP3A4 (black, red and blue, respectively). B , Superposition of the ritonavir- and GS3-bound CYP3A4 structures (green/pale green and magenta/gray, respectively). GS3 has a more flexible backbone and places Phe-2 between the heme-ligating pyridine and the Arg105 guanidinium groups, thereby promoting π-π and cation-π interactions and preventing steric hindrance with the 369–371 peptide. Another notable difference with ritonavir is a peptide bond flip, due to which the GS3 carbonyl oxygen rather than amide nitrogen forms a hydrogen bond with Ser119 (shown as dotted lines).
Figure Legend Snippet: A , Absorbance spectra of the ferrous GS1-, GS2- and GS3-bound CYP3A4 (black, red and blue, respectively). B , Superposition of the ritonavir- and GS3-bound CYP3A4 structures (green/pale green and magenta/gray, respectively). GS3 has a more flexible backbone and places Phe-2 between the heme-ligating pyridine and the Arg105 guanidinium groups, thereby promoting π-π and cation-π interactions and preventing steric hindrance with the 369–371 peptide. Another notable difference with ritonavir is a peptide bond flip, due to which the GS3 carbonyl oxygen rather than amide nitrogen forms a hydrogen bond with Ser119 (shown as dotted lines).

Techniques Used:

Chemical structures of ritonavir and cobicistat.
Figure Legend Snippet: Chemical structures of ritonavir and cobicistat.

Techniques Used:

Pharmacophore derived from the structure/function studies on ritonavir and 10 analogues. Pharmacophoric features are: flexible backbone (the center carbon atom is shown in black), strong heme-ligating nitrogen donor (blue), hydrogen donor/acceptor (red), aromatic and hydrophobic moieties (cyan and green, respectively), and poly-functional end-group (yellow).
Figure Legend Snippet: Pharmacophore derived from the structure/function studies on ritonavir and 10 analogues. Pharmacophoric features are: flexible backbone (the center carbon atom is shown in black), strong heme-ligating nitrogen donor (blue), hydrogen donor/acceptor (red), aromatic and hydrophobic moieties (cyan and green, respectively), and poly-functional end-group (yellow).

Techniques Used: Derivative Assay, Functional Assay

18) Product Images from "Effects of the Human Immunodeficiency Virus-Protease Inhibitor, Ritonavir, on Basal and Catecholamine-Stimulated Lipolysis"

Article Title: Effects of the Human Immunodeficiency Virus-Protease Inhibitor, Ritonavir, on Basal and Catecholamine-Stimulated Lipolysis

Journal: The Journal of clinical endocrinology and metabolism

doi: 10.1210/jc.2004-2194

Activation of ERK 1 and 2 in 3T3-L1 adipocytes treated with ritonavir for 14 d. Samples from 2-h incubations were collected after 1-h preincubation with the ERK inhibitor PD 98059 [dissolved in 0.1% dimethylsulfoxide (DMSO)] or 0.1% DMSO. A, Representative Western blot; B, glycerol release; C, NEFA release; n = 14–15 from three independent experiments. †, P
Figure Legend Snippet: Activation of ERK 1 and 2 in 3T3-L1 adipocytes treated with ritonavir for 14 d. Samples from 2-h incubations were collected after 1-h preincubation with the ERK inhibitor PD 98059 [dissolved in 0.1% dimethylsulfoxide (DMSO)] or 0.1% DMSO. A, Representative Western blot; B, glycerol release; C, NEFA release; n = 14–15 from three independent experiments. †, P

Techniques Used: Activation Assay, Western Blot

Total cellular triglyceride (A) and AP-2 protein expression (B and C) in 3T3-L1 adipocytes treated with ritonavir (Rit) or control medium (0.1% ethanol) for 14 d. Cells were grown in 100-mm dishes. AP-2 protein expression by Western blot was measured in whole-cell lysates collected at 6, 10, and 14 d after initiation of differentiation (as described in Materials and Methods ). A, n = 5–6 from two independent experiments. B and C, n = 6 from two independent experiments.
Figure Legend Snippet: Total cellular triglyceride (A) and AP-2 protein expression (B and C) in 3T3-L1 adipocytes treated with ritonavir (Rit) or control medium (0.1% ethanol) for 14 d. Cells were grown in 100-mm dishes. AP-2 protein expression by Western blot was measured in whole-cell lysates collected at 6, 10, and 14 d after initiation of differentiation (as described in Materials and Methods ). A, n = 5–6 from two independent experiments. B and C, n = 6 from two independent experiments.

Techniques Used: Expressing, Western Blot

19) Product Images from "Drug-Drug Interaction Study of Ketoconazole and Ritonavir-Boosted Saquinavir ▿"

Article Title: Drug-Drug Interaction Study of Ketoconazole and Ritonavir-Boosted Saquinavir ▿

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.00769-08

Mean plasma concentration-time profiles of ketoconazole after 6 days of ketoconazole at 200 mg given once daily (open symbols, dotted line) and after 14 days of coadministration of ketoconazole with saquinavir/ritonavir at 1,000/100 mg twice daily (filled
Figure Legend Snippet: Mean plasma concentration-time profiles of ketoconazole after 6 days of ketoconazole at 200 mg given once daily (open symbols, dotted line) and after 14 days of coadministration of ketoconazole with saquinavir/ritonavir at 1,000/100 mg twice daily (filled

Techniques Used: Concentration Assay

Mean plasma concentration-time profiles of saquinavir (squares) and ritonavir (circles) after 14 days of saquinavir/ritonavir at 1,000/100 mg given twice daily (open symbols, dotted line) and after 14 days of coadministration of saquinavir/ritonavir with
Figure Legend Snippet: Mean plasma concentration-time profiles of saquinavir (squares) and ritonavir (circles) after 14 days of saquinavir/ritonavir at 1,000/100 mg given twice daily (open symbols, dotted line) and after 14 days of coadministration of saquinavir/ritonavir with

Techniques Used: Concentration Assay

20) Product Images from "Mechanism of ritonavir changes in methadone pharmacokinetics and pharmacodynamics I. Evidence against CYP3A mediation of methadone clearance"

Article Title: Mechanism of ritonavir changes in methadone pharmacokinetics and pharmacodynamics I. Evidence against CYP3A mediation of methadone clearance

Journal: Clinical pharmacology and therapeutics

doi:

Effect of acute and steady-state ritonavir on oral methadone disposition and metabolism. Shown are plasma (A, B) R-methadone and R-EDDP concentrations and (C, D) S-methadone and S-EDDP concentrations. Subjects received 11.2 mg oral methadone HCl (10.0
Figure Legend Snippet: Effect of acute and steady-state ritonavir on oral methadone disposition and metabolism. Shown are plasma (A, B) R-methadone and R-EDDP concentrations and (C, D) S-methadone and S-EDDP concentrations. Subjects received 11.2 mg oral methadone HCl (10.0

Techniques Used:

Effect of acute and steady-state ritonavir on intravenous methadone disposition and metabolism. Shown are plasma (A, B) R-methadone and R-EDDP concentrations and (C, D) S-methadone and S-EDDP concentrations. Subjects received 6.0 mg IV methadone HCl (5.4
Figure Legend Snippet: Effect of acute and steady-state ritonavir on intravenous methadone disposition and metabolism. Shown are plasma (A, B) R-methadone and R-EDDP concentrations and (C, D) S-methadone and S-EDDP concentrations. Subjects received 6.0 mg IV methadone HCl (5.4

Techniques Used:

Effect of acute and steady-state ritonavir on stereoselective methadone elimination. Shown are plasma R/S-methadone concentration ratios for (A) intravenous and (B) oral methadone. Each data point is the mean ± SD (n=12).
Figure Legend Snippet: Effect of acute and steady-state ritonavir on stereoselective methadone elimination. Shown are plasma R/S-methadone concentration ratios for (A) intravenous and (B) oral methadone. Each data point is the mean ± SD (n=12).

Techniques Used: Concentration Assay

Effect of acute and steady-state ritonavir on methadone pharmacodynamics. Subjects simultaneously received 11.2 mg oral and 6.0 mg IV methadone HCl. Results are shown for (A) total plasma R-methadone concentrations, (B) dark-adapted pupil diameter change
Figure Legend Snippet: Effect of acute and steady-state ritonavir on methadone pharmacodynamics. Subjects simultaneously received 11.2 mg oral and 6.0 mg IV methadone HCl. Results are shown for (A) total plasma R-methadone concentrations, (B) dark-adapted pupil diameter change

Techniques Used:

Study protocol for ritonavir-methadone interaction. Shaded boxes show drug administration and/or blood and urine sampling.
Figure Legend Snippet: Study protocol for ritonavir-methadone interaction. Shaded boxes show drug administration and/or blood and urine sampling.

Techniques Used: Sampling

21) Product Images from "Inhibition Profiling of Retroviral Protease Inhibitors Using an HIV-2 Modular System"

Article Title: Inhibition Profiling of Retroviral Protease Inhibitors Using an HIV-2 Modular System

Journal: Viruses

doi: 10.3390/v7122931

Linear correlation analysis of IC 50 obtained from in vitro enzymatic and cell culture assays using both the wild-type and the double mutant protease. As mentioned previously nelfinavir and ritonavir were excluded from the analysis due to their unique biotransformation properties in cell culture. Correlation in case of the wild-type is indicated by a dotted line, while that of the double mutant is shown by a continuous line. p values were calculated at 95% confidence intervals.
Figure Legend Snippet: Linear correlation analysis of IC 50 obtained from in vitro enzymatic and cell culture assays using both the wild-type and the double mutant protease. As mentioned previously nelfinavir and ritonavir were excluded from the analysis due to their unique biotransformation properties in cell culture. Correlation in case of the wild-type is indicated by a dotted line, while that of the double mutant is shown by a continuous line. p values were calculated at 95% confidence intervals.

Techniques Used: In Vitro, Cell Culture, Mutagenesis

22) Product Images from "Boosting-Dose Ritonavir Does Not Alter Peripheral Insulin Sensitivity in Healthy, HIVSeronegative Volunteers"

Article Title: Boosting-Dose Ritonavir Does Not Alter Peripheral Insulin Sensitivity in Healthy, HIVSeronegative Volunteers

Journal: Journal of acquired immune deficiency syndromes (1999)

doi: 10.1097/QAI.0b013e3181e6a7d9

(A) Plasma ritonavir levels during the euglycemic hyperinsulinemic clamp. Values presented are mean ± SEM. (B) Whole blood glucose levels (mg/dL) and rate of glucose infusion (mL/h) during the euglycemic hyperinsulinemic clamp after administration
Figure Legend Snippet: (A) Plasma ritonavir levels during the euglycemic hyperinsulinemic clamp. Values presented are mean ± SEM. (B) Whole blood glucose levels (mg/dL) and rate of glucose infusion (mL/h) during the euglycemic hyperinsulinemic clamp after administration

Techniques Used:

23) Product Images from "Different prelamin A forms accumulate in human fibroblasts: a study in experimental models and progeria"

Article Title: Different prelamin A forms accumulate in human fibroblasts: a study in experimental models and progeria

Journal: European Journal of Histochemistry : EJH

doi: 10.4081/ejh.2009.e6

Prelamin A staining in control and HGPS skin fibroblasts. Prelamin A staining is shown in human control fibroblasts untreated (control) or treated with prelamin A processing inhibitors and in HGPS fibroblasts. (A) Fibroblasts untreated or treated with FTI-277 or mevinolin to accumulate non-farnesylated prelamin A (preLA-CSIM). Antibody 1188-1 labeling is reported in the upper row, antibody 1188-2 labeling is reported in the lower row. (B) Fibroblasts untreated or treated with AFCMe or HIV protease inhibitors (combinations of lopinavir plus ritonavir and atazanavir plus ritonavir, as indicated) to accumulate farnesylated prelamin A. HGPS fibroblasts, which also accumulate a farnesylated prelamin A form, are on the right. Antibody 1188-1 labeling is reported in the upper row, antibody 1188-2 labeling is reported in the lower row. (C) HGPS fibroblasts treated with mevinolin for 48 hours to show reduced staining using 1188-2 antibody with respect to bright staining observed in untreated HGPS cells shown in (B) and (D). Prelamin A staining was revealed by FITC-conjugated anti-rabbit IgG (green). Bars, 10 µm.
Figure Legend Snippet: Prelamin A staining in control and HGPS skin fibroblasts. Prelamin A staining is shown in human control fibroblasts untreated (control) or treated with prelamin A processing inhibitors and in HGPS fibroblasts. (A) Fibroblasts untreated or treated with FTI-277 or mevinolin to accumulate non-farnesylated prelamin A (preLA-CSIM). Antibody 1188-1 labeling is reported in the upper row, antibody 1188-2 labeling is reported in the lower row. (B) Fibroblasts untreated or treated with AFCMe or HIV protease inhibitors (combinations of lopinavir plus ritonavir and atazanavir plus ritonavir, as indicated) to accumulate farnesylated prelamin A. HGPS fibroblasts, which also accumulate a farnesylated prelamin A form, are on the right. Antibody 1188-1 labeling is reported in the upper row, antibody 1188-2 labeling is reported in the lower row. (C) HGPS fibroblasts treated with mevinolin for 48 hours to show reduced staining using 1188-2 antibody with respect to bright staining observed in untreated HGPS cells shown in (B) and (D). Prelamin A staining was revealed by FITC-conjugated anti-rabbit IgG (green). Bars, 10 µm.

Techniques Used: Staining, Labeling

Prelamin A Western blot analysis in control and HGPS skin fibroblasts. Western blot analysis of human fibroblast lysates performed with antibody 1188-1, 1188-2 or anti-lamin A/C antibody is shown. (A) Analysis of cells forced to accumulate non-farnesylated prelamin A. Cellular lysates have been obtained from control untreated fibroblasts (control), or from fibroblasts treated with FTI-277 or mevinolin to accumulate non-farnesylated prelamin A. (B) Analysis of cells accumulating farnesylated prelamin A. Cells were treated with the HIV protease inhibitors atazanavir, amprenavir, indinavir, nelfinavir, ritonavir+lopinavir and ritonavir+atazanavir (left panels) to accumulate farnesylated prelamin A. Analysis of lysates from AFCMe -treated control fibroblasts and untreated HGPS fibroblasts, known to accumulate farnesylated prelamin A, is shown in the right panels. Atazanavir and amprenavir did not affect prelamin A processing and are used as negative controls. Actin is labelled as a loading control. Asterisks indicate the shift of the prelamin A band detected by anti-lamin A/C antibody.
Figure Legend Snippet: Prelamin A Western blot analysis in control and HGPS skin fibroblasts. Western blot analysis of human fibroblast lysates performed with antibody 1188-1, 1188-2 or anti-lamin A/C antibody is shown. (A) Analysis of cells forced to accumulate non-farnesylated prelamin A. Cellular lysates have been obtained from control untreated fibroblasts (control), or from fibroblasts treated with FTI-277 or mevinolin to accumulate non-farnesylated prelamin A. (B) Analysis of cells accumulating farnesylated prelamin A. Cells were treated with the HIV protease inhibitors atazanavir, amprenavir, indinavir, nelfinavir, ritonavir+lopinavir and ritonavir+atazanavir (left panels) to accumulate farnesylated prelamin A. Analysis of lysates from AFCMe -treated control fibroblasts and untreated HGPS fibroblasts, known to accumulate farnesylated prelamin A, is shown in the right panels. Atazanavir and amprenavir did not affect prelamin A processing and are used as negative controls. Actin is labelled as a loading control. Asterisks indicate the shift of the prelamin A band detected by anti-lamin A/C antibody.

Techniques Used: Western Blot

24) Product Images from "Population pharmacokinetics of intravenously and orally administered docetaxel with or without co-administration of ritonavir in patients with advanced cancer"

Article Title: Population pharmacokinetics of intravenously and orally administered docetaxel with or without co-administration of ritonavir in patients with advanced cancer

Journal: British Journal of Clinical Pharmacology

doi: 10.1111/j.1365-2125.2010.03621.x

Visual predictive check (VPC) plots: The grey surface is the 90% confidence area of the predicted median, and the 5 th and 95 th percentile of the prediction interval. The black line is the observed median and the grey dotted lines are the 5 th and 95 th percentile of the observed data. In A) oral docetaxel 100 mg and ritonavir 100 mg are given simultaneously, in B) oral docetaxel 100 mg and ritonavir 100 mg are given 1 h sequentially and in C) docetaxel 100 mg is given intravenously. On the y -axis the concentration of docetaxel in ng ml −1
Figure Legend Snippet: Visual predictive check (VPC) plots: The grey surface is the 90% confidence area of the predicted median, and the 5 th and 95 th percentile of the prediction interval. The black line is the observed median and the grey dotted lines are the 5 th and 95 th percentile of the observed data. In A) oral docetaxel 100 mg and ritonavir 100 mg are given simultaneously, in B) oral docetaxel 100 mg and ritonavir 100 mg are given 1 h sequentially and in C) docetaxel 100 mg is given intravenously. On the y -axis the concentration of docetaxel in ng ml −1

Techniques Used: Concentration Assay

The estimated clearance of docetaxel vs. time (h) in individual patients receiving 100 mg docetaxel and 100 mg ritonavir (RTV) simultaneously and the average concentration–time curve of 100 mg ritonavir (▴)
Figure Legend Snippet: The estimated clearance of docetaxel vs. time (h) in individual patients receiving 100 mg docetaxel and 100 mg ritonavir (RTV) simultaneously and the average concentration–time curve of 100 mg ritonavir (▴)

Techniques Used: Concentration Assay

25) Product Images from "Drug-Drug Interaction Study of Ketoconazole and Ritonavir-Boosted Saquinavir ▿"

Article Title: Drug-Drug Interaction Study of Ketoconazole and Ritonavir-Boosted Saquinavir ▿

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.00769-08

Mean plasma concentration-time profiles of ketoconazole after 6 days of ketoconazole at 200 mg given once daily (open symbols, dotted line) and after 14 days of coadministration of ketoconazole with saquinavir/ritonavir at 1,000/100 mg twice daily (filled
Figure Legend Snippet: Mean plasma concentration-time profiles of ketoconazole after 6 days of ketoconazole at 200 mg given once daily (open symbols, dotted line) and after 14 days of coadministration of ketoconazole with saquinavir/ritonavir at 1,000/100 mg twice daily (filled

Techniques Used: Concentration Assay

Mean plasma concentration-time profiles of saquinavir (squares) and ritonavir (circles) after 14 days of saquinavir/ritonavir at 1,000/100 mg given twice daily (open symbols, dotted line) and after 14 days of coadministration of saquinavir/ritonavir with
Figure Legend Snippet: Mean plasma concentration-time profiles of saquinavir (squares) and ritonavir (circles) after 14 days of saquinavir/ritonavir at 1,000/100 mg given twice daily (open symbols, dotted line) and after 14 days of coadministration of saquinavir/ritonavir with

Techniques Used: Concentration Assay

26) Product Images from "Mechanism of ritonavir changes in methadone pharmacokinetics and pharmacodynamics. II. Ritonavir effects on CYP3A and P-glycoprotein activities"

Article Title: Mechanism of ritonavir changes in methadone pharmacokinetics and pharmacodynamics. II. Ritonavir effects on CYP3A and P-glycoprotein activities

Journal: Clinical pharmacology and therapeutics

doi:

Effect of acute and steady-state ritonavir on first-pass and hepatic CYP3A activity, assessed using alfentanil as a CYP3A probe. Pupil diameter change from baseline (miosis) was used as a surrogate for alfentanil plasma concentrations. Shown is dose-adjusted
Figure Legend Snippet: Effect of acute and steady-state ritonavir on first-pass and hepatic CYP3A activity, assessed using alfentanil as a CYP3A probe. Pupil diameter change from baseline (miosis) was used as a surrogate for alfentanil plasma concentrations. Shown is dose-adjusted

Techniques Used: Activity Assay

Effect of acute ritonavir on first-pass and hepatic CYP3A activity, assessed with alfentanil as a CYP3A probe. Miosis was used as a surrogate for ALF plasma concentrations. Results are shown as the measured dark-adapted pupil diameter (not baseline subtracted)
Figure Legend Snippet: Effect of acute ritonavir on first-pass and hepatic CYP3A activity, assessed with alfentanil as a CYP3A probe. Miosis was used as a surrogate for ALF plasma concentrations. Results are shown as the measured dark-adapted pupil diameter (not baseline subtracted)

Techniques Used: Activity Assay

Effect of acute and steady-state ritonavir on intestinal transporter activity, assessed using fexofenadine as a transporter probe. Shown are plasma fexofenadine concentrations after 3d and 2.5 wk ritonavir. Each subject received 60 mg oral fexofenadine
Figure Legend Snippet: Effect of acute and steady-state ritonavir on intestinal transporter activity, assessed using fexofenadine as a transporter probe. Shown are plasma fexofenadine concentrations after 3d and 2.5 wk ritonavir. Each subject received 60 mg oral fexofenadine

Techniques Used: Activity Assay

Effect of acute and steady-state ritonavir on first-pass and hepatic CYP3A activity, assessed using alfentanil as a CYP3A probe. Shown are dose-adjusted alfentanil concentrations after (A ) oral and (B) intravenous administration. Subjects received 43
Figure Legend Snippet: Effect of acute and steady-state ritonavir on first-pass and hepatic CYP3A activity, assessed using alfentanil as a CYP3A probe. Shown are dose-adjusted alfentanil concentrations after (A ) oral and (B) intravenous administration. Subjects received 43

Techniques Used: Activity Assay

Study protocol for ritonavir-methadone interaction. Shaded boxes show drug administration and/or blood and urine sampling.
Figure Legend Snippet: Study protocol for ritonavir-methadone interaction. Shaded boxes show drug administration and/or blood and urine sampling.

Techniques Used: Sampling

27) Product Images from "Rapid Clinical Induction of Hepatic Cytochrome P4502B6 Activity by Ritonavir "

Article Title: Rapid Clinical Induction of Hepatic Cytochrome P4502B6 Activity by Ritonavir

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.01600-07

Plasma concentrations of racemic bupropion (A) and bupropion enantiomers (B and C). Results are the means ± SD ( n = 13 for controls and acute ritonavir treatment; n = 12 for steady-state ritonavir treatment). Some SD are omitted for clarity.
Figure Legend Snippet: Plasma concentrations of racemic bupropion (A) and bupropion enantiomers (B and C). Results are the means ± SD ( n = 13 for controls and acute ritonavir treatment; n = 12 for steady-state ritonavir treatment). Some SD are omitted for clarity.

Techniques Used:

28) Product Images from "Drug-Drug Interaction Study of Ketoconazole and Ritonavir-Boosted Saquinavir ▿"

Article Title: Drug-Drug Interaction Study of Ketoconazole and Ritonavir-Boosted Saquinavir ▿

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.00769-08

Mean plasma concentration-time profiles of ketoconazole after 6 days of ketoconazole at 200 mg given once daily (open symbols, dotted line) and after 14 days of coadministration of ketoconazole with saquinavir/ritonavir at 1,000/100 mg twice daily (filled
Figure Legend Snippet: Mean plasma concentration-time profiles of ketoconazole after 6 days of ketoconazole at 200 mg given once daily (open symbols, dotted line) and after 14 days of coadministration of ketoconazole with saquinavir/ritonavir at 1,000/100 mg twice daily (filled

Techniques Used: Concentration Assay

Mean plasma concentration-time profiles of saquinavir (squares) and ritonavir (circles) after 14 days of saquinavir/ritonavir at 1,000/100 mg given twice daily (open symbols, dotted line) and after 14 days of coadministration of saquinavir/ritonavir with
Figure Legend Snippet: Mean plasma concentration-time profiles of saquinavir (squares) and ritonavir (circles) after 14 days of saquinavir/ritonavir at 1,000/100 mg given twice daily (open symbols, dotted line) and after 14 days of coadministration of saquinavir/ritonavir with

Techniques Used: Concentration Assay

29) Product Images from "Absence of circadian variation in the pharmacokinetics of lopinavir/ritonavir given as a once daily dosing regimen in HIV-1-infected patients"

Article Title: Absence of circadian variation in the pharmacokinetics of lopinavir/ritonavir given as a once daily dosing regimen in HIV-1-infected patients

Journal:

doi: 10.1111/j.1365-2125.2005.02337.x

Mean (± SD) steady-state plasma lopinavir (A) and ritonavir (B) concentration vs time profile after administration of lopinavir/ritonavir 800/200 mg once daily with a standardized meal in the morning (open circles) and in the evening (closed circles)
Figure Legend Snippet: Mean (± SD) steady-state plasma lopinavir (A) and ritonavir (B) concentration vs time profile after administration of lopinavir/ritonavir 800/200 mg once daily with a standardized meal in the morning (open circles) and in the evening (closed circles)

Techniques Used: Concentration Assay

Individual changes in lopinavir concentration at 24 h postdose ( C 24h ) and maximum ritonavir concentration ( C max ; ) after steady-state administration of lopinavir/ritonavir 800/200 mg once daily with food in the morning (am) or in the
Figure Legend Snippet: Individual changes in lopinavir concentration at 24 h postdose ( C 24h ) and maximum ritonavir concentration ( C max ; ) after steady-state administration of lopinavir/ritonavir 800/200 mg once daily with food in the morning (am) or in the

Techniques Used: Concentration Assay

30) Product Images from "EFFECT OF ULTRA-HIGH PRESSURE HOMOGENIZATION ON THE INTERACTION BETWEEN BOVINE CASEIN MICELLES AND RITONAVIR"

Article Title: EFFECT OF ULTRA-HIGH PRESSURE HOMOGENIZATION ON THE INTERACTION BETWEEN BOVINE CASEIN MICELLES AND RITONAVIR

Journal: Pharmaceutical research

doi: 10.1007/s11095-014-1518-9

Stability of ritonavir-casein micellar systems and improvement of ritonavir dispersibility after interaction with caseins
Figure Legend Snippet: Stability of ritonavir-casein micellar systems and improvement of ritonavir dispersibility after interaction with caseins

Techniques Used:

HPLC chromatogram of ritonavir (RIT) recovered from skim milk. Peak marked as * corresponds to proteins that remained after the extraction process
Figure Legend Snippet: HPLC chromatogram of ritonavir (RIT) recovered from skim milk. Peak marked as * corresponds to proteins that remained after the extraction process

Techniques Used: High Performance Liquid Chromatography

Intrinsic fluorescence emission spectra of pure ritonavir (RIT) and skim milk (SM) controls and RIT-SM systems obtained at 0.1, 300 and 500 MPa
Figure Legend Snippet: Intrinsic fluorescence emission spectra of pure ritonavir (RIT) and skim milk (SM) controls and RIT-SM systems obtained at 0.1, 300 and 500 MPa

Techniques Used: Fluorescence

DSC thermograms of pure ritonavir (RIT), non-homogenized skim milk (SM) and RIT-SM mixtures with different RIT content (0.4 – 15%, w/w)
Figure Legend Snippet: DSC thermograms of pure ritonavir (RIT), non-homogenized skim milk (SM) and RIT-SM mixtures with different RIT content (0.4 – 15%, w/w)

Techniques Used:

31) Product Images from "Concentration-dependent effects and intracellular accumulation of HIV protease inhibitors in cultured CD4 T cells and primary human lymphocytes"

Article Title: Concentration-dependent effects and intracellular accumulation of HIV protease inhibitors in cultured CD4 T cells and primary human lymphocytes

Journal: Journal of Antimicrobial Chemotherapy

doi: 10.1093/jac/dkq082

Effects of (a) pre-incubating CEM, CEM E1000 (E1000) and CEM VBL (VBL) cells with fixed concentrations (30 µM) of unlabelled lopinavir (LPV) (alone and in combination with 1 µM tariquidar or 50 µM MK571), (b) co-incubating the PBMCs with 10 and 30 µM unlabelled LPV (alone and in combination with 1 µM tariquidar or 50 µM frusemide) on the accumulation of [ 14 C]LPV, (c) pre-incubating CEM, E1000 and VBL cells with various concentrations (0–30 µM) of unlabelled LPV followed by the addition of [ 3 H]saquinavir (SQV) and (d) pre-incubating CEM, VBL and E1000 cells with various concentrations (0–30 µM) of unlabelled LPV on the accumulation of [ 3 H] ritonavir (RTV). Bars indicate mean ± SD ( n = 4, with four independent observations from cultured CEM and its variant cells and n = 4 with four independent observations from each buffy coat PBMC sample). P values of * P
Figure Legend Snippet: Effects of (a) pre-incubating CEM, CEM E1000 (E1000) and CEM VBL (VBL) cells with fixed concentrations (30 µM) of unlabelled lopinavir (LPV) (alone and in combination with 1 µM tariquidar or 50 µM MK571), (b) co-incubating the PBMCs with 10 and 30 µM unlabelled LPV (alone and in combination with 1 µM tariquidar or 50 µM frusemide) on the accumulation of [ 14 C]LPV, (c) pre-incubating CEM, E1000 and VBL cells with various concentrations (0–30 µM) of unlabelled LPV followed by the addition of [ 3 H]saquinavir (SQV) and (d) pre-incubating CEM, VBL and E1000 cells with various concentrations (0–30 µM) of unlabelled LPV on the accumulation of [ 3 H] ritonavir (RTV). Bars indicate mean ± SD ( n = 4, with four independent observations from cultured CEM and its variant cells and n = 4 with four independent observations from each buffy coat PBMC sample). P values of * P

Techniques Used: Cell Culture, Variant Assay

Effects of (a) pre-incubating CEM, CEM E1000 (E1000) and CEM VBL (VBL) cells with various concentrations (0–30 µM) of unlabelled ritonavir (RTV), (b) fixed concentrations (30 µM) of RTV (alone and in combination with 1 µM tariquidar or 50 µM MK571) and (c) pre-incubating the PBMCs with 10 and 30 µM unlabelled RTV (alone and in combination with 1 µM tariquidar or 50 µM frusemide) on the accumulation of [ 3 H]RTV. Bars indicate mean ± SD ( n = 4, with four independent observations from cultured CEM and its variant cells and n = 4 with four independent observations from each buffy coat PBMC sample). P values of * P
Figure Legend Snippet: Effects of (a) pre-incubating CEM, CEM E1000 (E1000) and CEM VBL (VBL) cells with various concentrations (0–30 µM) of unlabelled ritonavir (RTV), (b) fixed concentrations (30 µM) of RTV (alone and in combination with 1 µM tariquidar or 50 µM MK571) and (c) pre-incubating the PBMCs with 10 and 30 µM unlabelled RTV (alone and in combination with 1 µM tariquidar or 50 µM frusemide) on the accumulation of [ 3 H]RTV. Bars indicate mean ± SD ( n = 4, with four independent observations from cultured CEM and its variant cells and n = 4 with four independent observations from each buffy coat PBMC sample). P values of * P

Techniques Used: Cell Culture, Variant Assay

32) Product Images from "Protease inhibitor-induced nausea and vomiting is attenuated by a peripherally acting, opioid-receptor antagonist in a rat model"

Article Title: Protease inhibitor-induced nausea and vomiting is attenuated by a peripherally acting, opioid-receptor antagonist in a rat model

Journal: AIDS Research and Therapy

doi: 10.1186/1742-6405-6-19

Effects of pretreatment with methylnaltrexone on kaolin intake induced by ritonavir in rats . Ritonavir-induced increase in kaolin intake was attenuated with methylnaltrexone in a dose-related manner ( P
Figure Legend Snippet: Effects of pretreatment with methylnaltrexone on kaolin intake induced by ritonavir in rats . Ritonavir-induced increase in kaolin intake was attenuated with methylnaltrexone in a dose-related manner ( P

Techniques Used:

Dose-related effects of pretreatment with ritonavir on kaolin intake . Rats treated with saline only consumed
Figure Legend Snippet: Dose-related effects of pretreatment with ritonavir on kaolin intake . Rats treated with saline only consumed

Techniques Used:

Effects of pretreatment with naloxone on kaolin intake induced by ritonavir in rats . Ritonavir-induced increase in kaolin intake was attenuated with naloxone in a dose-related manner ( P
Figure Legend Snippet: Effects of pretreatment with naloxone on kaolin intake induced by ritonavir in rats . Ritonavir-induced increase in kaolin intake was attenuated with naloxone in a dose-related manner ( P

Techniques Used:

Area under the curve (AUC) for kaolin intake from time 0 to 120 hr . Naloxone significantly reduced kaolin intake induced by ritonavir ( P
Figure Legend Snippet: Area under the curve (AUC) for kaolin intake from time 0 to 120 hr . Naloxone significantly reduced kaolin intake induced by ritonavir ( P

Techniques Used:

Area under the curve (AUC) for kaolin intake from time 0 to 120 hr . Methylnaltrexone significantly reduced kaolin intake induced by ritonavir ( P
Figure Legend Snippet: Area under the curve (AUC) for kaolin intake from time 0 to 120 hr . Methylnaltrexone significantly reduced kaolin intake induced by ritonavir ( P

Techniques Used:

33) Product Images from "Pyridine-Substituted Desoxyritonavir Is a More Potent Inhibitor of Cytochrome P450 3A4 than Ritonavir"

Article Title: Pyridine-Substituted Desoxyritonavir Is a More Potent Inhibitor of Cytochrome P450 3A4 than Ritonavir

Journal: Journal of medicinal chemistry

doi: 10.1021/jm400288z

Plots of the observed rate constants for the fast (○) and slow (●) kinetic phases of the ritonavir and 1–3 binding to WT CYP3A4 vs ligand concentration.
Figure Legend Snippet: Plots of the observed rate constants for the fast (○) and slow (●) kinetic phases of the ritonavir and 1–3 binding to WT CYP3A4 vs ligand concentration.

Techniques Used: Binding Assay, Concentration Assay

Plots of the observed rate constants for the fast (○) and slow (●) kinetic phases of the ritonavir and compounds 1–3 binding to CYP3A4 S119A vs ligand concentration.
Figure Legend Snippet: Plots of the observed rate constants for the fast (○) and slow (●) kinetic phases of the ritonavir and compounds 1–3 binding to CYP3A4 S119A vs ligand concentration.

Techniques Used: Binding Assay, Concentration Assay

Effect of ritonavir and compounds 1–3 on thermal stability (A) and the BFC hydroxylation activity of CYP3A4 (B). The denaturation and inhibitory assays were conducted as described in the Experimental Section. The T m and IC 50 values derived from
Figure Legend Snippet: Effect of ritonavir and compounds 1–3 on thermal stability (A) and the BFC hydroxylation activity of CYP3A4 (B). The denaturation and inhibitory assays were conducted as described in the Experimental Section. The T m and IC 50 values derived from

Techniques Used: Activity Assay, Derivative Assay

Chemical structures of ritonavir, cobicistat, and compounds 1 – 3 .
Figure Legend Snippet: Chemical structures of ritonavir, cobicistat, and compounds 1 – 3 .

Techniques Used:

34) Product Images from "Ritonavir-Saquinavir Dual Protease Inhibitor Compared to Ritonavir Alone in Human Immunodeficiency Virus-Infected Patients"

Article Title: Ritonavir-Saquinavir Dual Protease Inhibitor Compared to Ritonavir Alone in Human Immunodeficiency Virus-Infected Patients

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.45.12.3393-3402.2001

Time course for plasma viral load in the two groups of patients (25 in the ritonavir group and 22 in the ritonavir-saquinavir group) during the 48 weeks of follow-up. Data are means, and error bars represent SDs. Results of repeated-measures ANCOVA (mixed-model) analyses were as follows: time effect, P
Figure Legend Snippet: Time course for plasma viral load in the two groups of patients (25 in the ritonavir group and 22 in the ritonavir-saquinavir group) during the 48 weeks of follow-up. Data are means, and error bars represent SDs. Results of repeated-measures ANCOVA (mixed-model) analyses were as follows: time effect, P

Techniques Used:

Time course for plasma hepatic aminotransferase (ALAT) levels in the two groups of patients (25 in the ritonavir group and 22 in the ritonavir-saquinavir group) during the 48 weeks of follow-up. Data are means, and error bars represent SDs. Results of repeated-measures ANCOVA (mixed-model) analyses were as follows: time effect, P
Figure Legend Snippet: Time course for plasma hepatic aminotransferase (ALAT) levels in the two groups of patients (25 in the ritonavir group and 22 in the ritonavir-saquinavir group) during the 48 weeks of follow-up. Data are means, and error bars represent SDs. Results of repeated-measures ANCOVA (mixed-model) analyses were as follows: time effect, P

Techniques Used:

35) Product Images from "Pharmacokinetics of Adjusted-Dose Lopinavir-Ritonavir Combined with Rifampin in Healthy Volunteers"

Article Title: Pharmacokinetics of Adjusted-Dose Lopinavir-Ritonavir Combined with Rifampin in Healthy Volunteers

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.48.5.1553-1560.2004

Trough lopinavir levels throughout the study. Treatments were as follows: days 1 to 10, lopinavir-ritonavir at 400/100 mg BID; days 11 to 15, lopinavir-ritonavir at 400/100 mg BID plus rifampin; days 16 and 17, lopinavir-ritonavir dose escalation plus rifampin; days 18 to 24, lopinavir-ritonavir at 800/200 mg BID plus rifampin for arm 1 and lopinavir-ritonavir at 400/400 mg BID plus rifampin for arm 2. •, arm 1 ( n = 10); □, arm 2 ( n = 9). Data are presented as arithmetic means, and error bars indicate standard deviations.
Figure Legend Snippet: Trough lopinavir levels throughout the study. Treatments were as follows: days 1 to 10, lopinavir-ritonavir at 400/100 mg BID; days 11 to 15, lopinavir-ritonavir at 400/100 mg BID plus rifampin; days 16 and 17, lopinavir-ritonavir dose escalation plus rifampin; days 18 to 24, lopinavir-ritonavir at 800/200 mg BID plus rifampin for arm 1 and lopinavir-ritonavir at 400/400 mg BID plus rifampin for arm 2. •, arm 1 ( n = 10); □, arm 2 ( n = 9). Data are presented as arithmetic means, and error bars indicate standard deviations.

Techniques Used:

36) Product Images from "Anti-Human Immunodeficiency Virus Activity of YK-FH312 (a Betulinic Acid Derivative), a Novel Compound Blocking Viral Maturation"

Article Title: Anti-Human Immunodeficiency Virus Activity of YK-FH312 (a Betulinic Acid Derivative), a Novel Compound Blocking Viral Maturation

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.45.4.1225-1230.2001

Inhibitory effects on syncytium formation in coculture of MOLT-4 and MOLT-4/HIV-1 IIIB cells pretreated with one of several compounds. MOLT-4/HIV-1 IIIB cells were cultured for 3 days with YK-FH312 (5 μg/ml), ritonavir (5 μg/ml), AZT (1 μM), or curdlan sulfate (1 μg/ml) and then cocultured with MOLT-4 for 24 h. The percentage of fusion inhibition was calculated as described in Materials and Methods.
Figure Legend Snippet: Inhibitory effects on syncytium formation in coculture of MOLT-4 and MOLT-4/HIV-1 IIIB cells pretreated with one of several compounds. MOLT-4/HIV-1 IIIB cells were cultured for 3 days with YK-FH312 (5 μg/ml), ritonavir (5 μg/ml), AZT (1 μM), or curdlan sulfate (1 μg/ml) and then cocultured with MOLT-4 for 24 h. The percentage of fusion inhibition was calculated as described in Materials and Methods.

Techniques Used: Cell Culture, Inhibition

Effects of various compounds on infectious HIV production in chronically infected MOLT-4/HIV-1 IIIB cells. (a) MOLT-4/HIV-1 IIIB cells cultured without compound or with 5 μg of YK-FH312 per ml, 5 μg of ritonavir per ml, or 1 μM AZT. The infectious titers of the culture supernatants were determined by MAGI assay. TCID 50 , 50% tissue culture infective dose. (b and c) Electron microscopic photographs of YK-FH312-treated MOLT-4/HIV-1 IIIB cells (b) and mock-treated cells (c). The magnifications of panels b and c are similar. No HIV virions were found in the YK-FH312-treated culture in contrast to the mock-treated culture.
Figure Legend Snippet: Effects of various compounds on infectious HIV production in chronically infected MOLT-4/HIV-1 IIIB cells. (a) MOLT-4/HIV-1 IIIB cells cultured without compound or with 5 μg of YK-FH312 per ml, 5 μg of ritonavir per ml, or 1 μM AZT. The infectious titers of the culture supernatants were determined by MAGI assay. TCID 50 , 50% tissue culture infective dose. (b and c) Electron microscopic photographs of YK-FH312-treated MOLT-4/HIV-1 IIIB cells (b) and mock-treated cells (c). The magnifications of panels b and c are similar. No HIV virions were found in the YK-FH312-treated culture in contrast to the mock-treated culture.

Techniques Used: Infection, Cell Culture

Time-of-addition assay. MT-4 cells were infected with HIV-1 IIIB at a high MOI. After 60 min of virus adsorption, the cells were washed. Compounds were then added to parallel cultures at different times postinfection or immediately after HIV-1 exposure to the cells without adsorption (at 0 h, only curdlan sulfate was added). At 24 h postinfection, cells and supernatants were collected by centrifugation. (a) Levels of p24 core antigen in culture supernatants treated with YK-FH312 (5 μg/ml) (●), ritonavir (5 μg/ml) (■), AZT (1 μM) (□), or curdlan sulfate (5 μg/ml) (▵). The broken line shows the p24 concentration at 24 h postinfection in the compound-free culture supernatant. Results are the mean concentrations of p24 detected in duplicate experiments. (b) Western blot analysis of cell-associated viral protein.
Figure Legend Snippet: Time-of-addition assay. MT-4 cells were infected with HIV-1 IIIB at a high MOI. After 60 min of virus adsorption, the cells were washed. Compounds were then added to parallel cultures at different times postinfection or immediately after HIV-1 exposure to the cells without adsorption (at 0 h, only curdlan sulfate was added). At 24 h postinfection, cells and supernatants were collected by centrifugation. (a) Levels of p24 core antigen in culture supernatants treated with YK-FH312 (5 μg/ml) (●), ritonavir (5 μg/ml) (■), AZT (1 μM) (□), or curdlan sulfate (5 μg/ml) (▵). The broken line shows the p24 concentration at 24 h postinfection in the compound-free culture supernatant. Results are the mean concentrations of p24 detected in duplicate experiments. (b) Western blot analysis of cell-associated viral protein.

Techniques Used: Infection, Adsorption, Centrifugation, Concentration Assay, Western Blot

37) Product Images from "Initial Cleavage of the Human Immunodeficiency Virus Type 1 GagPol Precursor by Its Activated Protease Occurs by an Intramolecular Mechanism"

Article Title: Initial Cleavage of the Human Immunodeficiency Virus Type 1 GagPol Precursor by Its Activated Protease Occurs by an Intramolecular Mechanism

Journal: Journal of Virology

doi: 10.1128/JVI.78.16.8477-8485.2004

Comparison of the effects of the competitive inhibitor ritonavir on activated GagPol protease and trans protease. (A) Wild-type GagPol was translated in vitro for 2 h in duplicate reactions containing increasing concentrations of ritonavir (ABT-538) to monitor the effects of the drug on activity of GagPol protease. The protease within GagPol activates and cleaves the precursor at the primary p2/NC and secondary TF F440/L441 sites. The concentration of GagPol in the reaction mixture is approximately 1 nM. The concentration of ritonavir is given above the lanes. (B) Effect of ritonavir on trans -cleavage of the GagPol precursor in vitro. A 325 nM concentration of mature recombinant protease monomers was added in trans to PR D25A mutated GagPol (160 pM) with various concentrations of ritonavir (above). Reactions shown were stopped at 10 min of incubation. The gels shown are representative of triplicate experiments. Products are presented in abbreviated form by their N- and C-terminal domains only. Numbers at left of each panel are molecular masses in kilodaltons.
Figure Legend Snippet: Comparison of the effects of the competitive inhibitor ritonavir on activated GagPol protease and trans protease. (A) Wild-type GagPol was translated in vitro for 2 h in duplicate reactions containing increasing concentrations of ritonavir (ABT-538) to monitor the effects of the drug on activity of GagPol protease. The protease within GagPol activates and cleaves the precursor at the primary p2/NC and secondary TF F440/L441 sites. The concentration of GagPol in the reaction mixture is approximately 1 nM. The concentration of ritonavir is given above the lanes. (B) Effect of ritonavir on trans -cleavage of the GagPol precursor in vitro. A 325 nM concentration of mature recombinant protease monomers was added in trans to PR D25A mutated GagPol (160 pM) with various concentrations of ritonavir (above). Reactions shown were stopped at 10 min of incubation. The gels shown are representative of triplicate experiments. Products are presented in abbreviated form by their N- and C-terminal domains only. Numbers at left of each panel are molecular masses in kilodaltons.

Techniques Used: In Vitro, Activity Assay, Concentration Assay, Recombinant, Incubation

Comparison of the susceptibilities of cleavage at the p2/NC and TF sites to inhibition for cis versus trans cleavage. Plots show the percent inhibition for the individual p2/NC and TF F440/L441 sites for GagPol protease (A) or trans -protease (B) with increasing concentrations of ritonavir. Plots were derived from densitometric analysis of SDS-polyacrylamide gels as described in Materials and Methods. The estimated IC 50 s for the inhibition of the individual sites for the GagPol protease are 189 nM for TF F440/L441 and 5.17 μM for p2/NC. The estimated IC 50 s for the trans protease are 18 nM for TF F440/L441 and 64 nM for p2/NC. Curves were determined as explained in Materials and Methods with a minimum of three independent replicates. Error bars indicate standard errors of the means.
Figure Legend Snippet: Comparison of the susceptibilities of cleavage at the p2/NC and TF sites to inhibition for cis versus trans cleavage. Plots show the percent inhibition for the individual p2/NC and TF F440/L441 sites for GagPol protease (A) or trans -protease (B) with increasing concentrations of ritonavir. Plots were derived from densitometric analysis of SDS-polyacrylamide gels as described in Materials and Methods. The estimated IC 50 s for the inhibition of the individual sites for the GagPol protease are 189 nM for TF F440/L441 and 5.17 μM for p2/NC. The estimated IC 50 s for the trans protease are 18 nM for TF F440/L441 and 64 nM for p2/NC. Curves were determined as explained in Materials and Methods with a minimum of three independent replicates. Error bars indicate standard errors of the means.

Techniques Used: Inhibition, Derivative Assay

38) Product Images from "Inhibitory Activity of Human Immunodeficiency Virus Aspartyl Protease Inhibitors against Encephalitozoon intestinalis Evaluated by Cell Culture-Quantitative PCR Assay"

Article Title: Inhibitory Activity of Human Immunodeficiency Virus Aspartyl Protease Inhibitors against Encephalitozoon intestinalis Evaluated by Cell Culture-Quantitative PCR Assay

Journal:

doi: 10.1128/AAC.49.6.2362-2366.2005

Inhibitory effects of albendazole (A), ritonavir (B), lopinavir (C), and saquinavir (D) on E. intestinalis growth in U-373-MG human glioblastoma cells. Number of E. intestinalis spores per culture well as assessed by real-time PCR ( y axis) versus drug
Figure Legend Snippet: Inhibitory effects of albendazole (A), ritonavir (B), lopinavir (C), and saquinavir (D) on E. intestinalis growth in U-373-MG human glioblastoma cells. Number of E. intestinalis spores per culture well as assessed by real-time PCR ( y axis) versus drug

Techniques Used: Real-time Polymerase Chain Reaction

39) Product Images from "Drug-Drug Interaction Study of Ketoconazole and Ritonavir-Boosted Saquinavir ▿"

Article Title: Drug-Drug Interaction Study of Ketoconazole and Ritonavir-Boosted Saquinavir ▿

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.00769-08

Mean plasma concentration-time profiles of ketoconazole after 6 days of ketoconazole at 200 mg given once daily (open symbols, dotted line) and after 14 days of coadministration of ketoconazole with saquinavir/ritonavir at 1,000/100 mg twice daily (filled
Figure Legend Snippet: Mean plasma concentration-time profiles of ketoconazole after 6 days of ketoconazole at 200 mg given once daily (open symbols, dotted line) and after 14 days of coadministration of ketoconazole with saquinavir/ritonavir at 1,000/100 mg twice daily (filled

Techniques Used: Concentration Assay

Mean plasma concentration-time profiles of saquinavir (squares) and ritonavir (circles) after 14 days of saquinavir/ritonavir at 1,000/100 mg given twice daily (open symbols, dotted line) and after 14 days of coadministration of saquinavir/ritonavir with
Figure Legend Snippet: Mean plasma concentration-time profiles of saquinavir (squares) and ritonavir (circles) after 14 days of saquinavir/ritonavir at 1,000/100 mg given twice daily (open symbols, dotted line) and after 14 days of coadministration of saquinavir/ritonavir with

Techniques Used: Concentration Assay

40) Product Images from "Loss of Viral Fitness Associated with Multiple Gag and Gag-Pol Processing Defects in Human Immunodeficiency Virus Type 1 Variants Selected for Resistance to Protease Inhibitors In Vivo"

Article Title: Loss of Viral Fitness Associated with Multiple Gag and Gag-Pol Processing Defects in Human Immunodeficiency Virus Type 1 Variants Selected for Resistance to Protease Inhibitors In Vivo

Journal: Journal of Virology

doi:

Single-cycle infectivity of recombinant viruses carrying pretherapy (gray bars) or postresistance (blade bars) HIV protease sequences from patients treated with protease inhibitors. The single-cycle titer of each recombinant virus carrying the postresistance protease was measured by titration on P4 (HeLa-CD4 LTR-LacZ) cells and expressed as a percentage of the titer of the pretherapy virus from the same patient. Postresistance viruses from patients 202, 401, 402, and 506 are resistant to ritonavir; postresistance virus from patient 246 is resistant to saquinavir. Viral input was normalized according to the HIV-1 p24 antigen content of transfected HeLa cell supernatants. The results presented are the mean standard deviation for at least three separate titration experiments for three different transfections.
Figure Legend Snippet: Single-cycle infectivity of recombinant viruses carrying pretherapy (gray bars) or postresistance (blade bars) HIV protease sequences from patients treated with protease inhibitors. The single-cycle titer of each recombinant virus carrying the postresistance protease was measured by titration on P4 (HeLa-CD4 LTR-LacZ) cells and expressed as a percentage of the titer of the pretherapy virus from the same patient. Postresistance viruses from patients 202, 401, 402, and 506 are resistant to ritonavir; postresistance virus from patient 246 is resistant to saquinavir. Viral input was normalized according to the HIV-1 p24 antigen content of transfected HeLa cell supernatants. The results presented are the mean standard deviation for at least three separate titration experiments for three different transfections.

Techniques Used: Infection, Recombinant, Titration, Transfection, Standard Deviation

Replication kinetics of recombinant viruses carrying pretherapy (□) or postresistance (⧫) HIV protease sequences in MT4 cells (A) and HUT78 cells (B). MT4 and HUT78 cells were infected with HIV-1 p24-normalized amounts of particles from recombinant viruses carrying pretherapy or postresistance protease sequences from ritonavir-treated patients 202, 401, and 402 and from saquinavir-treated patient 246. The kinetics of virus production in the infected cultures were monitored over time with an HIV-1 p24 ELISA.
Figure Legend Snippet: Replication kinetics of recombinant viruses carrying pretherapy (□) or postresistance (⧫) HIV protease sequences in MT4 cells (A) and HUT78 cells (B). MT4 and HUT78 cells were infected with HIV-1 p24-normalized amounts of particles from recombinant viruses carrying pretherapy or postresistance protease sequences from ritonavir-treated patients 202, 401, and 402 and from saquinavir-treated patient 246. The kinetics of virus production in the infected cultures were monitored over time with an HIV-1 p24 ELISA.

Techniques Used: Recombinant, Infection, Enzyme-linked Immunosorbent Assay

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Article Snippet: Plasma HIV-1 RNA was quantified using the Abbott m2000 RealTime System (Abbott Molecular, Des Plaines, Illinois).

Article Title: Lopinavir/ritonavir significantly influences pharmacokinetic exposure of artemether/lumefantrine in HIV-infected Ugandan adults
Article Snippet: However, caution and safety monitoring of HIV/malaria-coinfected patients receiving artemether/lumefantrine with lopinavir/ritonavir is advised.

Article Title: Antiretroviral treatment and its impact on oral health outcomes in 5 to 7 year old Ugandan children
Article Snippet: In other studies involving the ANRS 12174 trial participants, Blanche et al observed less weight gain in infants given lopinavir–ritonavir while Kariyawasam et al. found lopinavir–ritonavir to be associated with dose dependent adrenal dysfunction.

Mass Spectrometry:

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Reverse Transcriptase Assay:

Article Title: In Vitro Antioxidant Properties, HIV-1 Reverse Transcriptase and Acetylcholinesterase Inhibitory Effects of Traditional Herbal Preparations Sold in South Africa
Article Snippet: .. Ms. S. Khumalo (Social Counsellor UKZN-AIDS Programme) is thanked for providing the antiretroviral drugs; Combivir® (GlaxoSmithKline) and Kaletra® (Abbott) used as positive controls in the HIV-1 reverse transcriptase assay. ..

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    Abbott Laboratories lopinavir ritonavir
    Mean (±SEM) plasma concentration versus time of (a) artemether, (b) dihydroartemisinin and (c) lumefantrine for participants taking artemether/lumefantrine alone (AL alone) and artemether/lumefantrine in combination with <t>lopinavir/ritonavir</t> (AL plus LPV/r).
    Lopinavir Ritonavir, supplied by Abbott Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Abbott Laboratories ritonavir
    Ninety-five percent prediction intervals (P2.5–P97.5) determined from simulated data of <t>atazanavir/ritonavir</t> administered at (a) 300/100 mg once daily, (b) 200/100 mg once daily and (c) 150/100 mg once daily. Observed data are superimposed for the three evaluated regimens.
    Ritonavir, supplied by Abbott Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ritonavir/product/Abbott Laboratories
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    Mean (±SEM) plasma concentration versus time of (a) artemether, (b) dihydroartemisinin and (c) lumefantrine for participants taking artemether/lumefantrine alone (AL alone) and artemether/lumefantrine in combination with lopinavir/ritonavir (AL plus LPV/r).

    Journal: Journal of Antimicrobial Chemotherapy

    Article Title: Lopinavir/ritonavir significantly influences pharmacokinetic exposure of artemether/lumefantrine in HIV-infected Ugandan adults

    doi: 10.1093/jac/dkr596

    Figure Lengend Snippet: Mean (±SEM) plasma concentration versus time of (a) artemether, (b) dihydroartemisinin and (c) lumefantrine for participants taking artemether/lumefantrine alone (AL alone) and artemether/lumefantrine in combination with lopinavir/ritonavir (AL plus LPV/r).

    Article Snippet: However, caution and safety monitoring of HIV/malaria-coinfected patients receiving artemether/lumefantrine with lopinavir/ritonavir is advised.

    Techniques: Concentration Assay

    Distribution of mean dmft (decayed, missing filled teeth) by tooth type in the maxilla for lopinavir-ritonavir (top left) and lamivudine (top right) group. Also distribution of mean dmft in mandible lopinavir-ritonavir (bottom left) and lamivudine group (bottom right).

    Journal: Medicine

    Article Title: Antiretroviral treatment and its impact on oral health outcomes in 5 to 7 year old Ugandan children

    doi: 10.1097/MD.0000000000022352

    Figure Lengend Snippet: Distribution of mean dmft (decayed, missing filled teeth) by tooth type in the maxilla for lopinavir-ritonavir (top left) and lamivudine (top right) group. Also distribution of mean dmft in mandible lopinavir-ritonavir (bottom left) and lamivudine group (bottom right).

    Article Snippet: In other studies involving the ANRS 12174 trial participants, Blanche et al observed less weight gain in infants given lopinavir–ritonavir while Kariyawasam et al. found lopinavir–ritonavir to be associated with dose dependent adrenal dysfunction.

    Techniques:

    Average numbers of retained primary teeth and erupted permanent teeth in lopinavir-ritonavir and lamivudine treatment groups.

    Journal: Medicine

    Article Title: Antiretroviral treatment and its impact on oral health outcomes in 5 to 7 year old Ugandan children

    doi: 10.1097/MD.0000000000022352

    Figure Lengend Snippet: Average numbers of retained primary teeth and erupted permanent teeth in lopinavir-ritonavir and lamivudine treatment groups.

    Article Snippet: In other studies involving the ANRS 12174 trial participants, Blanche et al observed less weight gain in infants given lopinavir–ritonavir while Kariyawasam et al. found lopinavir–ritonavir to be associated with dose dependent adrenal dysfunction.

    Techniques:

    Ninety-five percent prediction intervals (P2.5–P97.5) determined from simulated data of atazanavir/ritonavir administered at (a) 300/100 mg once daily, (b) 200/100 mg once daily and (c) 150/100 mg once daily. Observed data are superimposed for the three evaluated regimens.

    Journal: Journal of Antimicrobial Chemotherapy

    Article Title: Population pharmacokinetics of ritonavir-boosted atazanavir in HIV-infected patients and healthy volunteers

    doi: 10.1093/jac/dkp102

    Figure Lengend Snippet: Ninety-five percent prediction intervals (P2.5–P97.5) determined from simulated data of atazanavir/ritonavir administered at (a) 300/100 mg once daily, (b) 200/100 mg once daily and (c) 150/100 mg once daily. Observed data are superimposed for the three evaluated regimens.

    Article Snippet: It is approved in Europe and the USA at a dose of 300 mg boosted with ritonavir (NORVIR®, Abbott Laboratories, Chicago, IL, USA) 100 mg once daily (atazanavir/ritonavir 300/100 mg once daily) to be taken with food, , but is also approved in the USA unboosted at 400 mg once daily for treatment-naive patients.

    Techniques: