p pkr Search Results


pperk  (MedChemExpress)
94
MedChemExpress pperk
Pperk, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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pkr [p thr446] antibody  (Bio-Techne corporation)
90
Bio-Techne corporation pkr [p thr446] antibody
Pkr [P Thr446] Antibody, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti-p-pkr monoclonal antibody  (ABclonal Biotechnology)
90
ABclonal Biotechnology anti-p-pkr monoclonal antibody
Anti P Pkr Monoclonal Antibody, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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antibody to p-pkr gtx32348  (GeneTex)
90
GeneTex antibody to p-pkr gtx32348
Antibody To P Pkr Gtx32348, supplied by GeneTex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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p-pkr(t446  (Absolute Biotech Inc)
90
Absolute Biotech Inc p-pkr(t446
PKR binds to stem-loop domains (SLDs) 5–6 in the HRV2 IRES as a dimer, resulting in autophosphorylation of the kinase activation loop (see <xref ref-type=Fig. S2 and for extended data). (A) Schematic representation of the HRV2 IRES SLD structure with an approximate footprint for eukaryotic initiation factor (eIF) 4G:eIF4A . (B) Binding of PKR, ADAR1, PCBP2, and DHX9 to different SLD fragments as indicated. Cytosolic fractions of A375 cells, “plain” or infected with PVSRIPO (MOI 10, 48 h), were incubated with biotinylated RNA fragments (30 min) prior to pull down with Streptavidin beads. Bound proteins were analyzed by immunoblot (see Fig. S2 for corresponding input blots). (C) PKR and DHX9 binding with biotinylated wild-type (WT) SLD 5 and three distinct SLD 5 variants carrying mutations (Mut 1–3) disrupting base-pairing structure as shown. (D) C16 prevented PKR activation, evident as autophosphorylation of T446 in the kinase activation loop, upon binding to biotinylated SLD 1–3, SLD 5–6, or poly(I·C). Methylcrotonyl-coa carboxylase subunit 1 (MCCC1) nonspecifically associates with streptavidin beads (in the absence of biotinylated RNA bait) and was used as a control to ensure equal loading. The assay was performed twice, and representative results are shown. Figure S3 shows the results of a repeat in vitro phosphorylation assay. (E and F) PKR competes with eIF4G for SLD 5–6 binding. The in vitro binding assay was performed as described (see Materials and Methods), keeping constant the concentrations of recombinant GST-eIF4G(Ct), Flag-eIF4A, and biotinylated RNA bait and varying the concentration of His-SUMO-PKR for a PKR/eIF4G ratio ranging from 0.1 to 1. Immunoblots of input and proteins after RNA pull down are shown (E). The assay was performed twice, and representative results are depicted. Relative levels of eIF4G and PRK after pull down were plotted, where maximal binding was set at 100% (F). Graphs represent the averages of 2 independent experiments. *, P < 0.05, **, P < 0.005. " width="250" height="auto" />
P Pkr(T446, supplied by Absolute Biotech Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/p-pkr(t446/product/Absolute Biotech Inc
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mouse anti-pkr  (Huabio Inc)
90
Huabio Inc mouse anti-pkr
PKR binds to stem-loop domains (SLDs) 5–6 in the HRV2 IRES as a dimer, resulting in autophosphorylation of the kinase activation loop (see <xref ref-type=Fig. S2 and for extended data). (A) Schematic representation of the HRV2 IRES SLD structure with an approximate footprint for eukaryotic initiation factor (eIF) 4G:eIF4A . (B) Binding of PKR, ADAR1, PCBP2, and DHX9 to different SLD fragments as indicated. Cytosolic fractions of A375 cells, “plain” or infected with PVSRIPO (MOI 10, 48 h), were incubated with biotinylated RNA fragments (30 min) prior to pull down with Streptavidin beads. Bound proteins were analyzed by immunoblot (see Fig. S2 for corresponding input blots). (C) PKR and DHX9 binding with biotinylated wild-type (WT) SLD 5 and three distinct SLD 5 variants carrying mutations (Mut 1–3) disrupting base-pairing structure as shown. (D) C16 prevented PKR activation, evident as autophosphorylation of T446 in the kinase activation loop, upon binding to biotinylated SLD 1–3, SLD 5–6, or poly(I·C). Methylcrotonyl-coa carboxylase subunit 1 (MCCC1) nonspecifically associates with streptavidin beads (in the absence of biotinylated RNA bait) and was used as a control to ensure equal loading. The assay was performed twice, and representative results are shown. Figure S3 shows the results of a repeat in vitro phosphorylation assay. (E and F) PKR competes with eIF4G for SLD 5–6 binding. The in vitro binding assay was performed as described (see Materials and Methods), keeping constant the concentrations of recombinant GST-eIF4G(Ct), Flag-eIF4A, and biotinylated RNA bait and varying the concentration of His-SUMO-PKR for a PKR/eIF4G ratio ranging from 0.1 to 1. Immunoblots of input and proteins after RNA pull down are shown (E). The assay was performed twice, and representative results are depicted. Relative levels of eIF4G and PRK after pull down were plotted, where maximal binding was set at 100% (F). Graphs represent the averages of 2 independent experiments. *, P < 0.05, **, P < 0.005. " width="250" height="auto" />
Mouse Anti Pkr, supplied by Huabio Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rabbit anti-mouse pkr-p antibody  (Cedarlane)
90
Cedarlane rabbit anti-mouse pkr-p antibody
PKR binds to stem-loop domains (SLDs) 5–6 in the HRV2 IRES as a dimer, resulting in autophosphorylation of the kinase activation loop (see <xref ref-type=Fig. S2 and for extended data). (A) Schematic representation of the HRV2 IRES SLD structure with an approximate footprint for eukaryotic initiation factor (eIF) 4G:eIF4A . (B) Binding of PKR, ADAR1, PCBP2, and DHX9 to different SLD fragments as indicated. Cytosolic fractions of A375 cells, “plain” or infected with PVSRIPO (MOI 10, 48 h), were incubated with biotinylated RNA fragments (30 min) prior to pull down with Streptavidin beads. Bound proteins were analyzed by immunoblot (see Fig. S2 for corresponding input blots). (C) PKR and DHX9 binding with biotinylated wild-type (WT) SLD 5 and three distinct SLD 5 variants carrying mutations (Mut 1–3) disrupting base-pairing structure as shown. (D) C16 prevented PKR activation, evident as autophosphorylation of T446 in the kinase activation loop, upon binding to biotinylated SLD 1–3, SLD 5–6, or poly(I·C). Methylcrotonyl-coa carboxylase subunit 1 (MCCC1) nonspecifically associates with streptavidin beads (in the absence of biotinylated RNA bait) and was used as a control to ensure equal loading. The assay was performed twice, and representative results are shown. Figure S3 shows the results of a repeat in vitro phosphorylation assay. (E and F) PKR competes with eIF4G for SLD 5–6 binding. The in vitro binding assay was performed as described (see Materials and Methods), keeping constant the concentrations of recombinant GST-eIF4G(Ct), Flag-eIF4A, and biotinylated RNA bait and varying the concentration of His-SUMO-PKR for a PKR/eIF4G ratio ranging from 0.1 to 1. Immunoblots of input and proteins after RNA pull down are shown (E). The assay was performed twice, and representative results are depicted. Relative levels of eIF4G and PRK after pull down were plotted, where maximal binding was set at 100% (F). Graphs represent the averages of 2 independent experiments. *, P < 0.05, **, P < 0.005. " width="250" height="auto" />
Rabbit Anti Mouse Pkr P Antibody, supplied by Cedarlane, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rabbit anti phospho pkr at thr446  (Trevigen)
90
Trevigen rabbit anti phospho pkr at thr446
PKR binds to stem-loop domains (SLDs) 5–6 in the HRV2 IRES as a dimer, resulting in autophosphorylation of the kinase activation loop (see <xref ref-type=Fig. S2 and for extended data). (A) Schematic representation of the HRV2 IRES SLD structure with an approximate footprint for eukaryotic initiation factor (eIF) 4G:eIF4A . (B) Binding of PKR, ADAR1, PCBP2, and DHX9 to different SLD fragments as indicated. Cytosolic fractions of A375 cells, “plain” or infected with PVSRIPO (MOI 10, 48 h), were incubated with biotinylated RNA fragments (30 min) prior to pull down with Streptavidin beads. Bound proteins were analyzed by immunoblot (see Fig. S2 for corresponding input blots). (C) PKR and DHX9 binding with biotinylated wild-type (WT) SLD 5 and three distinct SLD 5 variants carrying mutations (Mut 1–3) disrupting base-pairing structure as shown. (D) C16 prevented PKR activation, evident as autophosphorylation of T446 in the kinase activation loop, upon binding to biotinylated SLD 1–3, SLD 5–6, or poly(I·C). Methylcrotonyl-coa carboxylase subunit 1 (MCCC1) nonspecifically associates with streptavidin beads (in the absence of biotinylated RNA bait) and was used as a control to ensure equal loading. The assay was performed twice, and representative results are shown. Figure S3 shows the results of a repeat in vitro phosphorylation assay. (E and F) PKR competes with eIF4G for SLD 5–6 binding. The in vitro binding assay was performed as described (see Materials and Methods), keeping constant the concentrations of recombinant GST-eIF4G(Ct), Flag-eIF4A, and biotinylated RNA bait and varying the concentration of His-SUMO-PKR for a PKR/eIF4G ratio ranging from 0.1 to 1. Immunoblots of input and proteins after RNA pull down are shown (E). The assay was performed twice, and representative results are depicted. Relative levels of eIF4G and PRK after pull down were plotted, where maximal binding was set at 100% (F). Graphs represent the averages of 2 independent experiments. *, P < 0.05, **, P < 0.005. " width="250" height="auto" />
Rabbit Anti Phospho Pkr At Thr446, supplied by Trevigen, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rabbit anti p pkr thr446  (Trevigen)
92
Trevigen rabbit anti p pkr thr446
PKR binds to stem-loop domains (SLDs) 5–6 in the HRV2 IRES as a dimer, resulting in autophosphorylation of the kinase activation loop (see <xref ref-type=Fig. S2 and for extended data). (A) Schematic representation of the HRV2 IRES SLD structure with an approximate footprint for eukaryotic initiation factor (eIF) 4G:eIF4A . (B) Binding of PKR, ADAR1, PCBP2, and DHX9 to different SLD fragments as indicated. Cytosolic fractions of A375 cells, “plain” or infected with PVSRIPO (MOI 10, 48 h), were incubated with biotinylated RNA fragments (30 min) prior to pull down with Streptavidin beads. Bound proteins were analyzed by immunoblot (see Fig. S2 for corresponding input blots). (C) PKR and DHX9 binding with biotinylated wild-type (WT) SLD 5 and three distinct SLD 5 variants carrying mutations (Mut 1–3) disrupting base-pairing structure as shown. (D) C16 prevented PKR activation, evident as autophosphorylation of T446 in the kinase activation loop, upon binding to biotinylated SLD 1–3, SLD 5–6, or poly(I·C). Methylcrotonyl-coa carboxylase subunit 1 (MCCC1) nonspecifically associates with streptavidin beads (in the absence of biotinylated RNA bait) and was used as a control to ensure equal loading. The assay was performed twice, and representative results are shown. Figure S3 shows the results of a repeat in vitro phosphorylation assay. (E and F) PKR competes with eIF4G for SLD 5–6 binding. The in vitro binding assay was performed as described (see Materials and Methods), keeping constant the concentrations of recombinant GST-eIF4G(Ct), Flag-eIF4A, and biotinylated RNA bait and varying the concentration of His-SUMO-PKR for a PKR/eIF4G ratio ranging from 0.1 to 1. Immunoblots of input and proteins after RNA pull down are shown (E). The assay was performed twice, and representative results are depicted. Relative levels of eIF4G and PRK after pull down were plotted, where maximal binding was set at 100% (F). Graphs represent the averages of 2 independent experiments. *, P < 0.05, **, P < 0.005. " width="250" height="auto" />
Rabbit Anti P Pkr Thr446, supplied by Trevigen, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


PKR binds to stem-loop domains (SLDs) 5–6 in the HRV2 IRES as a dimer, resulting in autophosphorylation of the kinase activation loop (see <xref ref-type=Fig. S2 and for extended data). (A) Schematic representation of the HRV2 IRES SLD structure with an approximate footprint for eukaryotic initiation factor (eIF) 4G:eIF4A . (B) Binding of PKR, ADAR1, PCBP2, and DHX9 to different SLD fragments as indicated. Cytosolic fractions of A375 cells, “plain” or infected with PVSRIPO (MOI 10, 48 h), were incubated with biotinylated RNA fragments (30 min) prior to pull down with Streptavidin beads. Bound proteins were analyzed by immunoblot (see Fig. S2 for corresponding input blots). (C) PKR and DHX9 binding with biotinylated wild-type (WT) SLD 5 and three distinct SLD 5 variants carrying mutations (Mut 1–3) disrupting base-pairing structure as shown. (D) C16 prevented PKR activation, evident as autophosphorylation of T446 in the kinase activation loop, upon binding to biotinylated SLD 1–3, SLD 5–6, or poly(I·C). Methylcrotonyl-coa carboxylase subunit 1 (MCCC1) nonspecifically associates with streptavidin beads (in the absence of biotinylated RNA bait) and was used as a control to ensure equal loading. The assay was performed twice, and representative results are shown. Figure S3 shows the results of a repeat in vitro phosphorylation assay. (E and F) PKR competes with eIF4G for SLD 5–6 binding. The in vitro binding assay was performed as described (see Materials and Methods), keeping constant the concentrations of recombinant GST-eIF4G(Ct), Flag-eIF4A, and biotinylated RNA bait and varying the concentration of His-SUMO-PKR for a PKR/eIF4G ratio ranging from 0.1 to 1. Immunoblots of input and proteins after RNA pull down are shown (E). The assay was performed twice, and representative results are depicted. Relative levels of eIF4G and PRK after pull down were plotted, where maximal binding was set at 100% (F). Graphs represent the averages of 2 independent experiments. *, P < 0.05, **, P < 0.005. " width="100%" height="100%">

Journal: mBio

Article Title: PKR Binds Enterovirus IRESs, Displaces Host Translation Factors, and Impairs Viral Translation to Enable Innate Antiviral Signaling

doi: 10.1128/mbio.00854-22

Figure Lengend Snippet: PKR binds to stem-loop domains (SLDs) 5–6 in the HRV2 IRES as a dimer, resulting in autophosphorylation of the kinase activation loop (see Fig. S2 and for extended data). (A) Schematic representation of the HRV2 IRES SLD structure with an approximate footprint for eukaryotic initiation factor (eIF) 4G:eIF4A . (B) Binding of PKR, ADAR1, PCBP2, and DHX9 to different SLD fragments as indicated. Cytosolic fractions of A375 cells, “plain” or infected with PVSRIPO (MOI 10, 48 h), were incubated with biotinylated RNA fragments (30 min) prior to pull down with Streptavidin beads. Bound proteins were analyzed by immunoblot (see Fig. S2 for corresponding input blots). (C) PKR and DHX9 binding with biotinylated wild-type (WT) SLD 5 and three distinct SLD 5 variants carrying mutations (Mut 1–3) disrupting base-pairing structure as shown. (D) C16 prevented PKR activation, evident as autophosphorylation of T446 in the kinase activation loop, upon binding to biotinylated SLD 1–3, SLD 5–6, or poly(I·C). Methylcrotonyl-coa carboxylase subunit 1 (MCCC1) nonspecifically associates with streptavidin beads (in the absence of biotinylated RNA bait) and was used as a control to ensure equal loading. The assay was performed twice, and representative results are shown. Figure S3 shows the results of a repeat in vitro phosphorylation assay. (E and F) PKR competes with eIF4G for SLD 5–6 binding. The in vitro binding assay was performed as described (see Materials and Methods), keeping constant the concentrations of recombinant GST-eIF4G(Ct), Flag-eIF4A, and biotinylated RNA bait and varying the concentration of His-SUMO-PKR for a PKR/eIF4G ratio ranging from 0.1 to 1. Immunoblots of input and proteins after RNA pull down are shown (E). The assay was performed twice, and representative results are depicted. Relative levels of eIF4G and PRK after pull down were plotted, where maximal binding was set at 100% (F). Graphs represent the averages of 2 independent experiments. *, P < 0.05, **, P < 0.005.

Article Snippet: Primary antibodies used in this study were against eIF4G1, eIF4A, GAPDH, IRF3, p-IRF3(S396), STAT1, p-STAT1(Y701), IFNβ, IFIT1, PCBP2, PKR, ADAR, Dicer, IFI16, PACT, MDA5, TBK1, p-TBK1(S172), eIF2a, p-eIF2α(S51) (all Cell Signaling Technology), DHX9, LGP2, IFIT5 (all Proteintech), HelZ2, MCCC1 (ThermoFisher), DHX30 (Novus), NF90 (BD Biosciences), α-tubulin (Sigma-Aldrich), and p-PKR(T446) (LSBio).

Techniques: Activation Assay, Binding Assay, Infection, Incubation, Western Blot, In Vitro, Phosphorylation Assay, Recombinant, Concentration Assay