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  • 92
    Millipore α α dibromotoluene
    α α Dibromotoluene, supplied by Millipore, 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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    α α dibromotoluene - by Bioz Stars, 2020-08
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    88
    Millipore α dichlorodiphenylmethane
    α Dichlorodiphenylmethane, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Cell Signaling Technology Inc alpha ikb α
    Alpha Ikb α, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alpha ikb α/product/Cell Signaling Technology Inc
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    85
    Millipore α α azodiisobutyramidine dihydrochloride aaph
    α α Azodiisobutyramidine Dihydrochloride Aaph, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore α trifluorotoluene
    α Trifluorotoluene, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore α isonitrosopropiophenone α ispf
    α Isonitrosopropiophenone α Ispf, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore α hexylcinnamaldehyde
    α Hexylcinnamaldehyde, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Abcam α tocopherol
    α Tocopherol, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore α dendrotoxin α dtx
    <t>α-Dendrotoxin</t> (α-DTX) blocks a noninactivating current in CZ calyces. A : 100 nM α-DTX blocked a component of the outward current in a CZ calyx. The blocked current ( I subtracted ) activated rapidly and showed no inactivation. B : I-V plots show current amplitude measured at the end of each 40-ms pulse vs. voltage (same cell as A ). The α-DTX-sensitive current activated at potentials more depolarized than −60 mV. C : a single action potential was evoked after injection of a brief hyperpolarizing current in a CZ calyx ( left ). α-DTX (100 nM) increased the amplitude of the evoked action potential, increased the afterhyperpolarization potential, and resulted in a second spike ( right ).
    α Dendrotoxin α Dtx, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore α hexabromocyclododecane α hbcd
    <t>α-Dendrotoxin</t> (α-DTX) blocks a noninactivating current in CZ calyces. A : 100 nM α-DTX blocked a component of the outward current in a CZ calyx. The blocked current ( I subtracted ) activated rapidly and showed no inactivation. B : I-V plots show current amplitude measured at the end of each 40-ms pulse vs. voltage (same cell as A ). The α-DTX-sensitive current activated at potentials more depolarized than −60 mV. C : a single action potential was evoked after injection of a brief hyperpolarizing current in a CZ calyx ( left ). α-DTX (100 nM) increased the amplitude of the evoked action potential, increased the afterhyperpolarization potential, and resulted in a second spike ( right ).
    α Hexabromocyclododecane α Hbcd, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tnf α tnf α
    The levels of cytokines and chemokines in the BALF of PBS and OVA-sensitized and -challenged mice. After euthanizing the mice BALF was immediately collected and centrifuged. The supernatant was collected and frozen. The levels of cytokines and chemokines in the BALF of OVA-sensitized and -challenged mice compared to PBS control mice with different vitamin D groups. (A) IL-4; (B) IL-5; (C) IL-10 and (D) IL-13, <t>TNF-α,(E),</t> IL-6 (F), and IL-17(G), RANTES(H) and IP-10 (I) in BALF of OVA-sensitized and -challenged mice compared to PBS control mice in all vitamin D groups. Data are shown as means (±SEM) for six animals in each experimental group. *P
    Tnf α Tnf α, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    α 1  (TaKaRa)
    94
    TaKaRa α 1
    The levels of cytokines and chemokines in the BALF of PBS and OVA-sensitized and -challenged mice. After euthanizing the mice BALF was immediately collected and centrifuged. The supernatant was collected and frozen. The levels of cytokines and chemokines in the BALF of OVA-sensitized and -challenged mice compared to PBS control mice with different vitamin D groups. (A) IL-4; (B) IL-5; (C) IL-10 and (D) IL-13, <t>TNF-α,(E),</t> IL-6 (F), and IL-17(G), RANTES(H) and IP-10 (I) in BALF of OVA-sensitized and -challenged mice compared to PBS control mice in all vitamin D groups. Data are shown as means (±SEM) for six animals in each experimental group. *P
    α 1, supplied by TaKaRa, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Santa Cruz Biotechnology alpha α tubulin
    The levels of cytokines and chemokines in the BALF of PBS and OVA-sensitized and -challenged mice. After euthanizing the mice BALF was immediately collected and centrifuged. The supernatant was collected and frozen. The levels of cytokines and chemokines in the BALF of OVA-sensitized and -challenged mice compared to PBS control mice with different vitamin D groups. (A) IL-4; (B) IL-5; (C) IL-10 and (D) IL-13, <t>TNF-α,(E),</t> IL-6 (F), and IL-17(G), RANTES(H) and IP-10 (I) in BALF of OVA-sensitized and -challenged mice compared to PBS control mice in all vitamin D groups. Data are shown as means (±SEM) for six animals in each experimental group. *P
    Alpha α Tubulin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore α amylase α amylase
    Amidoximation, activation and immobilization of <t>α-amylase</t> onto acrylic fibre.
    α Amylase α Amylase, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore α naphthoflavone α nf
    <t>α-NF</t> stimulation decreases the LC3 in keratinocytes. Cells were treated with different concentrations of PM (25, 100, 200 μg/mL) and α-NF (6 h; 5 μM) for 24 h and analyzed by Western blot. β-actin was used as a loading control.
    α Naphthoflavone α Nf, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore α allocryptopine
    <t>α-NF</t> stimulation decreases the LC3 in keratinocytes. Cells were treated with different concentrations of PM (25, 100, 200 μg/mL) and α-NF (6 h; 5 μM) for 24 h and analyzed by Western blot. β-actin was used as a loading control.
    α Allocryptopine, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore α gurjunene
    Proposed Biosynthetic Mechanism for Formation of <t>(−)-α-Gurjunene</t> (3), 5-Hydroxy-α-Gurjunene (7), and Related Sesquiterpene Alcohols Generated by MpMTPSL4 from All- trans Farnesyl Diphosphate [(2 E ,6 E )-FPP]. .
    α Gurjunene, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam α alpha linker
    Proposed Biosynthetic Mechanism for Formation of <t>(−)-α-Gurjunene</t> (3), 5-Hydroxy-α-Gurjunene (7), and Related Sesquiterpene Alcohols Generated by MpMTPSL4 from All- trans Farnesyl Diphosphate [(2 E ,6 E )-FPP]. .
    α Alpha Linker, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore α catenin
    Function-blocking antibody to N-cadherin blocks <t>α-catenin</t> from association with junctional complexes, assembly of a cortical actin cytoskeleton, and fiber cell elongation Epithelial explants were cultured in the presence of the N-Cadherin function-blocking antibody NCD-2 or control rat IgG. (A) The effect of N-cadherin function-blocking antibody on the association of α-catenin and β-catenin with N-cadherin complexes was determined by co-immunoprecipitation analysis (Immunoprecipitate: N-cadherin, Blot: α-catenin or βcatenin). Results were compared to control explants exposed to rat IgG. Four-hour exposure to NCD-2 resulted in reduced association of α-catenin with N-cadherin complexes with no effect on the link between N-cadherin and β-catenin (left panels). Long-term exposure to NCD-2 (twenty-four hours, right panels) blocked association of α-catenin with N-cadherin junctions and, in addition, resulted in downregulation of N-cadherin expression. (B) Immunolocalization of α-catenin in epithelial explants exposed to NCD-2 or control IgG for 4 hrs. Following fixation the localization of the NCD-2 antibody or IgG was determined by incubation with a fluorescent-conjugated secondary antibody and the samples were double-stained with antibody to α-catenin. Right had panels are high magnification overlays, the top panel a co-localization of control IgG antibody with α-catenin, the bottom panel a co-localization of NCD2 antibody with α-catenin. Samples were viewed by confocal microscopy and Z-stacks collected. Images presented represent a single optical plane within the Z-stack in the apicolateral region of the cells. The results showed a loss of α-catenin from cell-cell interfaces of explants treated with NCD-2. Results are representative of at least 3 independent studies; Bar, 10 µm. (C) Cells in the transition zone (TZ) of NCD-2 treated explants (after a four exposure) were stained with fluorescent-conjugated phalloidin to visualize actin (blue), and fluorescent-conjugated secondary antibodies to localize NCD-2 or control IgG (green). Imaging of these ex vivo explants by confocal microscopy showed that NCD-2 had localized to N-cadherin junctions at cell-cell interfaces of differentiating fiber cells in the TZ, and disrupted the formation of the cortical actin skeleton in these differentiating fiber cells. Images were collected as Z-stacks and data shown represent a single optical plane within the Z-stack; Bar, 10 µm. (D) Measurements of fiber cell length in the TZ region of explants exposed to NCD-2 or control rat IgG for four hours showed that destabilization of N-cadherin junctions with NCD-2 blocked the elongation of lens fiber cells, demonstrating that N-cadherin-linked actin organization was responsible for lens fiber cell morphogenesis. All results are representative of at least 3 independent studies. Arrows denote the same position in double stained images.
    α Catenin, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 340 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore lxr α
    Function-blocking antibody to N-cadherin blocks <t>α-catenin</t> from association with junctional complexes, assembly of a cortical actin cytoskeleton, and fiber cell elongation Epithelial explants were cultured in the presence of the N-Cadherin function-blocking antibody NCD-2 or control rat IgG. (A) The effect of N-cadherin function-blocking antibody on the association of α-catenin and β-catenin with N-cadherin complexes was determined by co-immunoprecipitation analysis (Immunoprecipitate: N-cadherin, Blot: α-catenin or βcatenin). Results were compared to control explants exposed to rat IgG. Four-hour exposure to NCD-2 resulted in reduced association of α-catenin with N-cadherin complexes with no effect on the link between N-cadherin and β-catenin (left panels). Long-term exposure to NCD-2 (twenty-four hours, right panels) blocked association of α-catenin with N-cadherin junctions and, in addition, resulted in downregulation of N-cadherin expression. (B) Immunolocalization of α-catenin in epithelial explants exposed to NCD-2 or control IgG for 4 hrs. Following fixation the localization of the NCD-2 antibody or IgG was determined by incubation with a fluorescent-conjugated secondary antibody and the samples were double-stained with antibody to α-catenin. Right had panels are high magnification overlays, the top panel a co-localization of control IgG antibody with α-catenin, the bottom panel a co-localization of NCD2 antibody with α-catenin. Samples were viewed by confocal microscopy and Z-stacks collected. Images presented represent a single optical plane within the Z-stack in the apicolateral region of the cells. The results showed a loss of α-catenin from cell-cell interfaces of explants treated with NCD-2. Results are representative of at least 3 independent studies; Bar, 10 µm. (C) Cells in the transition zone (TZ) of NCD-2 treated explants (after a four exposure) were stained with fluorescent-conjugated phalloidin to visualize actin (blue), and fluorescent-conjugated secondary antibodies to localize NCD-2 or control IgG (green). Imaging of these ex vivo explants by confocal microscopy showed that NCD-2 had localized to N-cadherin junctions at cell-cell interfaces of differentiating fiber cells in the TZ, and disrupted the formation of the cortical actin skeleton in these differentiating fiber cells. Images were collected as Z-stacks and data shown represent a single optical plane within the Z-stack; Bar, 10 µm. (D) Measurements of fiber cell length in the TZ region of explants exposed to NCD-2 or control rat IgG for four hours showed that destabilization of N-cadherin junctions with NCD-2 blocked the elongation of lens fiber cells, demonstrating that N-cadherin-linked actin organization was responsible for lens fiber cell morphogenesis. All results are representative of at least 3 independent studies. Arrows denote the same position in double stained images.
    Lxr α, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore α hch
    Computational results of hexachlorocyclohexane <t>(HCH)</t> binding to bases. Representative image of the gradient isosurface (left), the corresponding plots of reduced density gradient versus the sign of the second Hessian eigenvalues (right) of a <t>adenine–α-HCH,</t> b cytosine–α-HCH, c guanine–α-HCH, d thymine–α-HCH, together with the molecular orbitals of e DNA bases–α-HCH, f DNA bases–β-HCH, and g DNA bases–γ-HCH. The surfaces are colored on a blue–green–red scale according to the sign( λ 2 ) ρ values (range −0.05 to 0.05 a.u.). Green areas between molecules indicate a weak Van der Waals force. Large brown and olive spheres represent the positive and negative phases, respectively, of the electronic wave function
    α Hch, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore α tetralone
    Binding interaction of <t>α-tetralone</t> in the substrate binding site of PyAeADHII/NADPH predicted by AutoDock. a) Binding mode 1, α-tetralone was positioned on top of the nicotinamide ring as a stacking interaction, and the oxygen atom formed a H-bonding interaction with the side chain of residue Asn-39 (3.5 Å). b) α-tetralone again forms stacking interaction with nicotinamide ring, but the oxygen atom was orientated towards residue Arg-88 forming a H-bonding interaction (3.0 Å). PyAeADHII is shown as a cartoon (green) and residues in the substrate binding site are shown as sticks (carbon colored in yellow, nitrogen in blue, oxygen in red). NADPH (carbons are in grey) and the substrate α-tetralone (carbon are in orange) are shown as sticks.
    α Tetralone, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore α amanitin
    Outline of the BioGRO method. ( a ) The colours of RNA polymerases (RNAP) represent different transcriptional states. Only active elongating RNA pol II (green) is able to run-on. ( b ) Analysis of the size of the run-on elongation with Biotin-UTP. Biotinylated RNAs appear as a diffuse luminescent stain signal centred at about 50 nucleotides (nt). ( c ) BioGRO after a selective inhibition of RNA pol II with <t>α-amanitin.</t> The graph shows the comparison made between BioGRO signals in the presence or absence (control) of α-amanitin. In black, the RNA pol II genes and their trend line. The tRNA genes and their trend line are depicted in red. Green dots mark the RNA pol III transcripts that do not belong to the tRNA type.
    α Amanitin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1880 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    α-Dendrotoxin (α-DTX) blocks a noninactivating current in CZ calyces. A : 100 nM α-DTX blocked a component of the outward current in a CZ calyx. The blocked current ( I subtracted ) activated rapidly and showed no inactivation. B : I-V plots show current amplitude measured at the end of each 40-ms pulse vs. voltage (same cell as A ). The α-DTX-sensitive current activated at potentials more depolarized than −60 mV. C : a single action potential was evoked after injection of a brief hyperpolarizing current in a CZ calyx ( left ). α-DTX (100 nM) increased the amplitude of the evoked action potential, increased the afterhyperpolarization potential, and resulted in a second spike ( right ).

    Journal: Journal of Neurophysiology

    Article Title: Zonal variations in K+ currents in vestibular crista calyx terminals

    doi: 10.1152/jn.00399.2014

    Figure Lengend Snippet: α-Dendrotoxin (α-DTX) blocks a noninactivating current in CZ calyces. A : 100 nM α-DTX blocked a component of the outward current in a CZ calyx. The blocked current ( I subtracted ) activated rapidly and showed no inactivation. B : I-V plots show current amplitude measured at the end of each 40-ms pulse vs. voltage (same cell as A ). The α-DTX-sensitive current activated at potentials more depolarized than −60 mV. C : a single action potential was evoked after injection of a brief hyperpolarizing current in a CZ calyx ( left ). α-DTX (100 nM) increased the amplitude of the evoked action potential, increased the afterhyperpolarization potential, and resulted in a second spike ( right ).

    Article Snippet: 4-AP, diclofenac sodium salt, and α-dendrotoxin (α-DTX) were obtained from Sigma-Aldrich.

    Techniques: Mass Spectrometry, Injection

    The levels of cytokines and chemokines in the BALF of PBS and OVA-sensitized and -challenged mice. After euthanizing the mice BALF was immediately collected and centrifuged. The supernatant was collected and frozen. The levels of cytokines and chemokines in the BALF of OVA-sensitized and -challenged mice compared to PBS control mice with different vitamin D groups. (A) IL-4; (B) IL-5; (C) IL-10 and (D) IL-13, TNF-α,(E), IL-6 (F), and IL-17(G), RANTES(H) and IP-10 (I) in BALF of OVA-sensitized and -challenged mice compared to PBS control mice in all vitamin D groups. Data are shown as means (±SEM) for six animals in each experimental group. *P

    Journal: Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology

    Article Title: Vitamin D Supplementation Reduces Airway Hyperresponsiveness and Allergic Airway Inflammation in a Murine Model

    doi: 10.1111/cea.12102

    Figure Lengend Snippet: The levels of cytokines and chemokines in the BALF of PBS and OVA-sensitized and -challenged mice. After euthanizing the mice BALF was immediately collected and centrifuged. The supernatant was collected and frozen. The levels of cytokines and chemokines in the BALF of OVA-sensitized and -challenged mice compared to PBS control mice with different vitamin D groups. (A) IL-4; (B) IL-5; (C) IL-10 and (D) IL-13, TNF-α,(E), IL-6 (F), and IL-17(G), RANTES(H) and IP-10 (I) in BALF of OVA-sensitized and -challenged mice compared to PBS control mice in all vitamin D groups. Data are shown as means (±SEM) for six animals in each experimental group. *P

    Article Snippet: The levels of IL-4, IL-5, IL-6, IL-10, IL-13, IL-17,RANTES, IP-10 and TNF-α TNF-α in the BAL fluid supernatants were measured by the Milliplex mouse cytokine/chemokine kit (Millipore, Billerica, MA) on a Luminex 200 analyzer (Luminex Corp, Austin, TX, USA) following Manufacturer's recommendations The analysis was done in duplicate, and the cytokine concentrations were calculated against the standards using Beadview® software (ver.

    Techniques: Mouse Assay

    Amidoximation, activation and immobilization of α-amylase onto acrylic fibre.

    Journal: Royal Society Open Science

    Article Title: α-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride

    doi: 10.1098/rsos.172164

    Figure Lengend Snippet: Amidoximation, activation and immobilization of α-amylase onto acrylic fibre.

    Article Snippet: 2.1. α-Amylase α-Amylase from Bacillus subtilis was purchased from Sigma-Aldrich.

    Techniques: Activation Assay

    Reuse of immobilized α-amylase.

    Journal: Royal Society Open Science

    Article Title: α-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride

    doi: 10.1098/rsos.172164

    Figure Lengend Snippet: Reuse of immobilized α-amylase.

    Article Snippet: 2.1. α-Amylase α-Amylase from Bacillus subtilis was purchased from Sigma-Aldrich.

    Techniques:

    Effect of immobilization time on the relative activity of the immobilized α-amylase.

    Journal: Royal Society Open Science

    Article Title: α-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride

    doi: 10.1098/rsos.172164

    Figure Lengend Snippet: Effect of immobilization time on the relative activity of the immobilized α-amylase.

    Article Snippet: 2.1. α-Amylase α-Amylase from Bacillus subtilis was purchased from Sigma-Aldrich.

    Techniques: Activity Assay

    FTIR spectra of acrylic, amidoximated acrylic, activated acrylic and immobilized α-amylase fabric samples.

    Journal: Royal Society Open Science

    Article Title: α-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride

    doi: 10.1098/rsos.172164

    Figure Lengend Snippet: FTIR spectra of acrylic, amidoximated acrylic, activated acrylic and immobilized α-amylase fabric samples.

    Article Snippet: 2.1. α-Amylase α-Amylase from Bacillus subtilis was purchased from Sigma-Aldrich.

    Techniques:

    Optimum pH ( a ), optimum temperature ( b ), thermal stability ( c ) and k m ( d ) of soluble and immobilized α-amylase. Each point represents the average of two experiments.

    Journal: Royal Society Open Science

    Article Title: α-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride

    doi: 10.1098/rsos.172164

    Figure Lengend Snippet: Optimum pH ( a ), optimum temperature ( b ), thermal stability ( c ) and k m ( d ) of soluble and immobilized α-amylase. Each point represents the average of two experiments.

    Article Snippet: 2.1. α-Amylase α-Amylase from Bacillus subtilis was purchased from Sigma-Aldrich.

    Techniques:

    Low and high magnification (inset) FESEM images of (a ) pure acrylic fibre, ( b , c ) acrylic fibres treated with NH 2 OH · HCl and cyanuric chloride, respectively, ( d ) immobilization of α-amylase after chemical treatment.

    Journal: Royal Society Open Science

    Article Title: α-Amylase immobilization on amidoximated acrylic microfibres activated by cyanuric chloride

    doi: 10.1098/rsos.172164

    Figure Lengend Snippet: Low and high magnification (inset) FESEM images of (a ) pure acrylic fibre, ( b , c ) acrylic fibres treated with NH 2 OH · HCl and cyanuric chloride, respectively, ( d ) immobilization of α-amylase after chemical treatment.

    Article Snippet: 2.1. α-Amylase α-Amylase from Bacillus subtilis was purchased from Sigma-Aldrich.

    Techniques:

    α-NF stimulation decreases the LC3 in keratinocytes. Cells were treated with different concentrations of PM (25, 100, 200 μg/mL) and α-NF (6 h; 5 μM) for 24 h and analyzed by Western blot. β-actin was used as a loading control.

    Journal: Biomolecules & Therapeutics

    Article Title: Particulate Matter-Induced Aryl Hydrocarbon Receptor Regulates Autophagy in Keratinocytes

    doi: 10.4062/biomolther.2019.025

    Figure Lengend Snippet: α-NF stimulation decreases the LC3 in keratinocytes. Cells were treated with different concentrations of PM (25, 100, 200 μg/mL) and α-NF (6 h; 5 μM) for 24 h and analyzed by Western blot. β-actin was used as a loading control.

    Article Snippet: LipofectamineTM RNAiMAX Transfection Reagent was purchased from Invitrogen (CA, USA). α-Naphthoflavone (α-NF), 3-Methyladenine (3-MA), and Bafilomycin A1 (BAF) were purchased from Sigma Aldrich (St. Louis, MO, USA).

    Techniques: Western Blot

    α-NF stimulation decreases the expression of CYP1A1 in keratinocytes. Cells were treated with PM 50 μg/mL in the absence or presence of α-NF (6 h; 5 μM) for 3 h and analyzed by (A) RT-PCR and (B) qRT-PCR. Values are presented as the mean ± SD of three determinations (n=3). ** p

    Journal: Biomolecules & Therapeutics

    Article Title: Particulate Matter-Induced Aryl Hydrocarbon Receptor Regulates Autophagy in Keratinocytes

    doi: 10.4062/biomolther.2019.025

    Figure Lengend Snippet: α-NF stimulation decreases the expression of CYP1A1 in keratinocytes. Cells were treated with PM 50 μg/mL in the absence or presence of α-NF (6 h; 5 μM) for 3 h and analyzed by (A) RT-PCR and (B) qRT-PCR. Values are presented as the mean ± SD of three determinations (n=3). ** p

    Article Snippet: LipofectamineTM RNAiMAX Transfection Reagent was purchased from Invitrogen (CA, USA). α-Naphthoflavone (α-NF), 3-Methyladenine (3-MA), and Bafilomycin A1 (BAF) were purchased from Sigma Aldrich (St. Louis, MO, USA).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Quantitative RT-PCR

    Proposed Biosynthetic Mechanism for Formation of (−)-α-Gurjunene (3), 5-Hydroxy-α-Gurjunene (7), and Related Sesquiterpene Alcohols Generated by MpMTPSL4 from All- trans Farnesyl Diphosphate [(2 E ,6 E )-FPP]. .

    Journal: The Plant Cell

    Article Title: Molecular Diversity of Terpene Synthases in the Liverwort Marchantia polymorpha [OPEN]

    doi: 10.1105/tpc.16.00062

    Figure Lengend Snippet: Proposed Biosynthetic Mechanism for Formation of (−)-α-Gurjunene (3), 5-Hydroxy-α-Gurjunene (7), and Related Sesquiterpene Alcohols Generated by MpMTPSL4 from All- trans Farnesyl Diphosphate [(2 E ,6 E )-FPP]. .

    Article Snippet: Full confirmation of peak 3 corresponding to ()-α-gurjunene was obtained by direct and 1 H-NMR comparisons with an authentic standard (Sigma-Aldrich).

    Techniques: Generated

    Function-blocking antibody to N-cadherin blocks α-catenin from association with junctional complexes, assembly of a cortical actin cytoskeleton, and fiber cell elongation Epithelial explants were cultured in the presence of the N-Cadherin function-blocking antibody NCD-2 or control rat IgG. (A) The effect of N-cadherin function-blocking antibody on the association of α-catenin and β-catenin with N-cadherin complexes was determined by co-immunoprecipitation analysis (Immunoprecipitate: N-cadherin, Blot: α-catenin or βcatenin). Results were compared to control explants exposed to rat IgG. Four-hour exposure to NCD-2 resulted in reduced association of α-catenin with N-cadherin complexes with no effect on the link between N-cadherin and β-catenin (left panels). Long-term exposure to NCD-2 (twenty-four hours, right panels) blocked association of α-catenin with N-cadherin junctions and, in addition, resulted in downregulation of N-cadherin expression. (B) Immunolocalization of α-catenin in epithelial explants exposed to NCD-2 or control IgG for 4 hrs. Following fixation the localization of the NCD-2 antibody or IgG was determined by incubation with a fluorescent-conjugated secondary antibody and the samples were double-stained with antibody to α-catenin. Right had panels are high magnification overlays, the top panel a co-localization of control IgG antibody with α-catenin, the bottom panel a co-localization of NCD2 antibody with α-catenin. Samples were viewed by confocal microscopy and Z-stacks collected. Images presented represent a single optical plane within the Z-stack in the apicolateral region of the cells. The results showed a loss of α-catenin from cell-cell interfaces of explants treated with NCD-2. Results are representative of at least 3 independent studies; Bar, 10 µm. (C) Cells in the transition zone (TZ) of NCD-2 treated explants (after a four exposure) were stained with fluorescent-conjugated phalloidin to visualize actin (blue), and fluorescent-conjugated secondary antibodies to localize NCD-2 or control IgG (green). Imaging of these ex vivo explants by confocal microscopy showed that NCD-2 had localized to N-cadherin junctions at cell-cell interfaces of differentiating fiber cells in the TZ, and disrupted the formation of the cortical actin skeleton in these differentiating fiber cells. Images were collected as Z-stacks and data shown represent a single optical plane within the Z-stack; Bar, 10 µm. (D) Measurements of fiber cell length in the TZ region of explants exposed to NCD-2 or control rat IgG for four hours showed that destabilization of N-cadherin junctions with NCD-2 blocked the elongation of lens fiber cells, demonstrating that N-cadherin-linked actin organization was responsible for lens fiber cell morphogenesis. All results are representative of at least 3 independent studies. Arrows denote the same position in double stained images.

    Journal: Developmental biology

    Article Title: MODULATION OF N-CADHERIN JUNCTIONS AND THEIR ROLE AS EPICENTERS OF DIFFERENTIATION-SPECIFIC ACTIN REGULATION IN THE DEVELOPING LENS

    doi: 10.1016/j.ydbio.2010.10.009

    Figure Lengend Snippet: Function-blocking antibody to N-cadherin blocks α-catenin from association with junctional complexes, assembly of a cortical actin cytoskeleton, and fiber cell elongation Epithelial explants were cultured in the presence of the N-Cadherin function-blocking antibody NCD-2 or control rat IgG. (A) The effect of N-cadherin function-blocking antibody on the association of α-catenin and β-catenin with N-cadherin complexes was determined by co-immunoprecipitation analysis (Immunoprecipitate: N-cadherin, Blot: α-catenin or βcatenin). Results were compared to control explants exposed to rat IgG. Four-hour exposure to NCD-2 resulted in reduced association of α-catenin with N-cadherin complexes with no effect on the link between N-cadherin and β-catenin (left panels). Long-term exposure to NCD-2 (twenty-four hours, right panels) blocked association of α-catenin with N-cadherin junctions and, in addition, resulted in downregulation of N-cadherin expression. (B) Immunolocalization of α-catenin in epithelial explants exposed to NCD-2 or control IgG for 4 hrs. Following fixation the localization of the NCD-2 antibody or IgG was determined by incubation with a fluorescent-conjugated secondary antibody and the samples were double-stained with antibody to α-catenin. Right had panels are high magnification overlays, the top panel a co-localization of control IgG antibody with α-catenin, the bottom panel a co-localization of NCD2 antibody with α-catenin. Samples were viewed by confocal microscopy and Z-stacks collected. Images presented represent a single optical plane within the Z-stack in the apicolateral region of the cells. The results showed a loss of α-catenin from cell-cell interfaces of explants treated with NCD-2. Results are representative of at least 3 independent studies; Bar, 10 µm. (C) Cells in the transition zone (TZ) of NCD-2 treated explants (after a four exposure) were stained with fluorescent-conjugated phalloidin to visualize actin (blue), and fluorescent-conjugated secondary antibodies to localize NCD-2 or control IgG (green). Imaging of these ex vivo explants by confocal microscopy showed that NCD-2 had localized to N-cadherin junctions at cell-cell interfaces of differentiating fiber cells in the TZ, and disrupted the formation of the cortical actin skeleton in these differentiating fiber cells. Images were collected as Z-stacks and data shown represent a single optical plane within the Z-stack; Bar, 10 µm. (D) Measurements of fiber cell length in the TZ region of explants exposed to NCD-2 or control rat IgG for four hours showed that destabilization of N-cadherin junctions with NCD-2 blocked the elongation of lens fiber cells, demonstrating that N-cadherin-linked actin organization was responsible for lens fiber cell morphogenesis. All results are representative of at least 3 independent studies. Arrows denote the same position in double stained images.

    Article Snippet: For immunostaining, samples were incubated sequentially with primary antibody (N-cadherin (Zymed), β-catenin (BD Transduction, San Jose, CA), α-catenin (Sigma, St. Louis, MO), or cortactin (Upstate, Lake Placid, NY)) and fluorescence-conjugated secondary antibody (Jackson ImmunoResearch Laboratories, West Grove, PA).

    Techniques: Blocking Assay, Cell Culture, Immunoprecipitation, Expressing, Incubation, Staining, Confocal Microscopy, Imaging, Ex Vivo

    Localization of α-catenin to cell-cell interfaces is coincident with the maturation of N-cadherin junctions and the initiation of differentiation (A–C) Immunolocalization of α-catenin in epithelial explants viewed as individual optical sections from Z-stacks collected by confocal microscopy showed dramatic changes in the distribution of α-catenin between the EC (A), EQ (B) and TZ (C) zones. High levels of α-catenin at lateral membranes first were detected in the EQ zone (B). The images in B represent the four apical-most optical sections. In the TZ, linear aligned puncta of α-catenin were observed all along cell-cell interfaces of these elongating cells. All images in A-C were acquired with the same settings and the results are representative of at least 3 independent studies; bar, 10 µm. (D) Cross-sections of the cortical fiber zone (FP) near the posterior region of the E10 lens were viewed by confocal microscopy following immunostaining for N-cadherin, β-catenin and α-catenin; N-cadherin and β-catenin sections were co-stained for F-actin. Both β-catenin and α-catenin localized to lateral cell-cell interfaces, but not to cell vertices, coincident with F-actin, as modeled in the diagram in D. Images are representative of 3 independent studies; bar, 10 µm.

    Journal: Developmental biology

    Article Title: MODULATION OF N-CADHERIN JUNCTIONS AND THEIR ROLE AS EPICENTERS OF DIFFERENTIATION-SPECIFIC ACTIN REGULATION IN THE DEVELOPING LENS

    doi: 10.1016/j.ydbio.2010.10.009

    Figure Lengend Snippet: Localization of α-catenin to cell-cell interfaces is coincident with the maturation of N-cadherin junctions and the initiation of differentiation (A–C) Immunolocalization of α-catenin in epithelial explants viewed as individual optical sections from Z-stacks collected by confocal microscopy showed dramatic changes in the distribution of α-catenin between the EC (A), EQ (B) and TZ (C) zones. High levels of α-catenin at lateral membranes first were detected in the EQ zone (B). The images in B represent the four apical-most optical sections. In the TZ, linear aligned puncta of α-catenin were observed all along cell-cell interfaces of these elongating cells. All images in A-C were acquired with the same settings and the results are representative of at least 3 independent studies; bar, 10 µm. (D) Cross-sections of the cortical fiber zone (FP) near the posterior region of the E10 lens were viewed by confocal microscopy following immunostaining for N-cadherin, β-catenin and α-catenin; N-cadherin and β-catenin sections were co-stained for F-actin. Both β-catenin and α-catenin localized to lateral cell-cell interfaces, but not to cell vertices, coincident with F-actin, as modeled in the diagram in D. Images are representative of 3 independent studies; bar, 10 µm.

    Article Snippet: For immunostaining, samples were incubated sequentially with primary antibody (N-cadherin (Zymed), β-catenin (BD Transduction, San Jose, CA), α-catenin (Sigma, St. Louis, MO), or cortactin (Upstate, Lake Placid, NY)) and fluorescence-conjugated secondary antibody (Jackson ImmunoResearch Laboratories, West Grove, PA).

    Techniques: Confocal Microscopy, Immunostaining, Staining

    Association of α-catenin with N-cadherin complexes is coincident with the maturation of N-cadherin junctions (A) Model of E10 chick lens microdissection to yield the four regions of differentiation: EC, EQ, FP, and FC. (B) Differentiation-state specific recruitment of α-catenin to N-cadherin junctions determined by co-immunoprecipitation analysis; immunoprecipitate for N-cadherin followed by Western Blotting for α-catenin and β-catenin. Densitometric analyses are represented as the ratio of β- or α-catenin to N-cadherin, normalized to EC. There was a great increase in association of α-catenin with N-cadherin junctional complexes in the EQ zone of differentiation initiation, which was maintained throughout lens fiber cell differentiation with no change in the association of β-catenin with N-cadherin. (C) Double immunoprecipitation analysis was used to examine the association of α-catenin with N-cadherin/β-catenin complexes. N-cadherin complexes were isolated with an antibody column and then subsequently immunoprecipitated for β-catenin, thereby isolating N-cadherin/β-catenin complexes. Association of α-catenin with this complex was determined by Western Blot analysis. The results showed that α-catenin was highly recruited to N-cadherin/β-catenin junctions in the EQ zone, coordinated with the zipping up of N-cadherin junctions and remained highly associated with N-cadherin/β-catenin junctions in the differentiating cortical fiber cells of the FP zone.

    Journal: Developmental biology

    Article Title: MODULATION OF N-CADHERIN JUNCTIONS AND THEIR ROLE AS EPICENTERS OF DIFFERENTIATION-SPECIFIC ACTIN REGULATION IN THE DEVELOPING LENS

    doi: 10.1016/j.ydbio.2010.10.009

    Figure Lengend Snippet: Association of α-catenin with N-cadherin complexes is coincident with the maturation of N-cadherin junctions (A) Model of E10 chick lens microdissection to yield the four regions of differentiation: EC, EQ, FP, and FC. (B) Differentiation-state specific recruitment of α-catenin to N-cadherin junctions determined by co-immunoprecipitation analysis; immunoprecipitate for N-cadherin followed by Western Blotting for α-catenin and β-catenin. Densitometric analyses are represented as the ratio of β- or α-catenin to N-cadherin, normalized to EC. There was a great increase in association of α-catenin with N-cadherin junctional complexes in the EQ zone of differentiation initiation, which was maintained throughout lens fiber cell differentiation with no change in the association of β-catenin with N-cadherin. (C) Double immunoprecipitation analysis was used to examine the association of α-catenin with N-cadherin/β-catenin complexes. N-cadherin complexes were isolated with an antibody column and then subsequently immunoprecipitated for β-catenin, thereby isolating N-cadherin/β-catenin complexes. Association of α-catenin with this complex was determined by Western Blot analysis. The results showed that α-catenin was highly recruited to N-cadherin/β-catenin junctions in the EQ zone, coordinated with the zipping up of N-cadherin junctions and remained highly associated with N-cadherin/β-catenin junctions in the differentiating cortical fiber cells of the FP zone.

    Article Snippet: For immunostaining, samples were incubated sequentially with primary antibody (N-cadherin (Zymed), β-catenin (BD Transduction, San Jose, CA), α-catenin (Sigma, St. Louis, MO), or cortactin (Upstate, Lake Placid, NY)) and fluorescence-conjugated secondary antibody (Jackson ImmunoResearch Laboratories, West Grove, PA).

    Techniques: Laser Capture Microdissection, Immunoprecipitation, Western Blot, Cell Differentiation, Isolation

    α-catenin in the maturation of N-cadherin/β-catenin junctions with lens epithelial cell differentiation Lens epithelial cells are diagrammed through their elongation into lens fiber cells in the transition zone, focusing on the role of α-catenin in the maturation of N-cadherin junctions along lateral cell borders. Each color represents a distinct N-cadherin junctional complex: blue – N-cadherin junctions with no associated α- or β-catenin; red – N-cadherin/β-catenin junctions with no associated α-catenin; orange - N-cadherin/β-catenin junctions with a low level of associated α-catenin; yellow - N-cadherin/β-catenin junctions with a high level of associated α-catenin.

    Journal: Developmental biology

    Article Title: MODULATION OF N-CADHERIN JUNCTIONS AND THEIR ROLE AS EPICENTERS OF DIFFERENTIATION-SPECIFIC ACTIN REGULATION IN THE DEVELOPING LENS

    doi: 10.1016/j.ydbio.2010.10.009

    Figure Lengend Snippet: α-catenin in the maturation of N-cadherin/β-catenin junctions with lens epithelial cell differentiation Lens epithelial cells are diagrammed through their elongation into lens fiber cells in the transition zone, focusing on the role of α-catenin in the maturation of N-cadherin junctions along lateral cell borders. Each color represents a distinct N-cadherin junctional complex: blue – N-cadherin junctions with no associated α- or β-catenin; red – N-cadherin/β-catenin junctions with no associated α-catenin; orange - N-cadherin/β-catenin junctions with a low level of associated α-catenin; yellow - N-cadherin/β-catenin junctions with a high level of associated α-catenin.

    Article Snippet: For immunostaining, samples were incubated sequentially with primary antibody (N-cadherin (Zymed), β-catenin (BD Transduction, San Jose, CA), α-catenin (Sigma, St. Louis, MO), or cortactin (Upstate, Lake Placid, NY)) and fluorescence-conjugated secondary antibody (Jackson ImmunoResearch Laboratories, West Grove, PA).

    Techniques: Cell Differentiation

    Computational results of hexachlorocyclohexane (HCH) binding to bases. Representative image of the gradient isosurface (left), the corresponding plots of reduced density gradient versus the sign of the second Hessian eigenvalues (right) of a adenine–α-HCH, b cytosine–α-HCH, c guanine–α-HCH, d thymine–α-HCH, together with the molecular orbitals of e DNA bases–α-HCH, f DNA bases–β-HCH, and g DNA bases–γ-HCH. The surfaces are colored on a blue–green–red scale according to the sign( λ 2 ) ρ values (range −0.05 to 0.05 a.u.). Green areas between molecules indicate a weak Van der Waals force. Large brown and olive spheres represent the positive and negative phases, respectively, of the electronic wave function

    Journal: Communications Biology

    Article Title: Organochlorinated pesticides expedite the enzymatic degradation of DNA

    doi: 10.1038/s42003-019-0326-5

    Figure Lengend Snippet: Computational results of hexachlorocyclohexane (HCH) binding to bases. Representative image of the gradient isosurface (left), the corresponding plots of reduced density gradient versus the sign of the second Hessian eigenvalues (right) of a adenine–α-HCH, b cytosine–α-HCH, c guanine–α-HCH, d thymine–α-HCH, together with the molecular orbitals of e DNA bases–α-HCH, f DNA bases–β-HCH, and g DNA bases–γ-HCH. The surfaces are colored on a blue–green–red scale according to the sign( λ 2 ) ρ values (range −0.05 to 0.05 a.u.). Green areas between molecules indicate a weak Van der Waals force. Large brown and olive spheres represent the positive and negative phases, respectively, of the electronic wave function

    Article Snippet: Chemicals Salmon sperm DNA with an average molar mass of 1.3 × 106 Da and %G-C content of 41.2%, α-HCH, β-HCH, and γ-HCH were purchased from Sigma Chemical Co. (St. Louis, MO, USA).

    Techniques: Binding Assay

    Structural changes in DNA and stability of DNA–hexachlorocyclohexane (HCH) complexes. a Circular dichroism spectra of DNA (black line), α-HCH–DNA (red line), β-HCH–DNA (olive line), and γ-HCH–DNA (blue line). Red arrow indicates a shift in molar ellipticity. b Optimized DNA–HCH structure. c RMSD over 80,000 ps α-HCH–DNA (red line), β-HCH–DNA (olive line), and γ-HCH–DNA (blue line)

    Journal: Communications Biology

    Article Title: Organochlorinated pesticides expedite the enzymatic degradation of DNA

    doi: 10.1038/s42003-019-0326-5

    Figure Lengend Snippet: Structural changes in DNA and stability of DNA–hexachlorocyclohexane (HCH) complexes. a Circular dichroism spectra of DNA (black line), α-HCH–DNA (red line), β-HCH–DNA (olive line), and γ-HCH–DNA (blue line). Red arrow indicates a shift in molar ellipticity. b Optimized DNA–HCH structure. c RMSD over 80,000 ps α-HCH–DNA (red line), β-HCH–DNA (olive line), and γ-HCH–DNA (blue line)

    Article Snippet: Chemicals Salmon sperm DNA with an average molar mass of 1.3 × 106 Da and %G-C content of 41.2%, α-HCH, β-HCH, and γ-HCH were purchased from Sigma Chemical Co. (St. Louis, MO, USA).

    Techniques:

    Gel electrophoresis of DNA fragments. a α-HCH, b β-HCH, and c γ-HCH (0–4.0 mg L −1 ). a, b, c, d, e, f, g, h, and i represent hexachlorocyclohexane (HCH) concentrations of 0, 0.5, 1.0, 1.5, 2.0, 2.5, 3.0, 3.5, and 4.0 mg L −1 , respectively. Ck, control treatment without DNase I

    Journal: Communications Biology

    Article Title: Organochlorinated pesticides expedite the enzymatic degradation of DNA

    doi: 10.1038/s42003-019-0326-5

    Figure Lengend Snippet: Gel electrophoresis of DNA fragments. a α-HCH, b β-HCH, and c γ-HCH (0–4.0 mg L −1 ). a, b, c, d, e, f, g, h, and i represent hexachlorocyclohexane (HCH) concentrations of 0, 0.5, 1.0, 1.5, 2.0, 2.5, 3.0, 3.5, and 4.0 mg L −1 , respectively. Ck, control treatment without DNase I

    Article Snippet: Chemicals Salmon sperm DNA with an average molar mass of 1.3 × 106 Da and %G-C content of 41.2%, α-HCH, β-HCH, and γ-HCH were purchased from Sigma Chemical Co. (St. Louis, MO, USA).

    Techniques: Nucleic Acid Electrophoresis

    Increase of DNA absorbance caused by DNase I in the presence of hexachlorocyclohexanes (HCHs). a The DNA absorbance changes influenced by α-HCH. b The DNA absorbance changes influenced by β-HCH. c The DNA absorbance changes influenced by γ-HCH. Each absorbance data point was the average of 10 measurements

    Journal: Communications Biology

    Article Title: Organochlorinated pesticides expedite the enzymatic degradation of DNA

    doi: 10.1038/s42003-019-0326-5

    Figure Lengend Snippet: Increase of DNA absorbance caused by DNase I in the presence of hexachlorocyclohexanes (HCHs). a The DNA absorbance changes influenced by α-HCH. b The DNA absorbance changes influenced by β-HCH. c The DNA absorbance changes influenced by γ-HCH. Each absorbance data point was the average of 10 measurements

    Article Snippet: Chemicals Salmon sperm DNA with an average molar mass of 1.3 × 106 Da and %G-C content of 41.2%, α-HCH, β-HCH, and γ-HCH were purchased from Sigma Chemical Co. (St. Louis, MO, USA).

    Techniques:

    Binding interaction of α-tetralone in the substrate binding site of PyAeADHII/NADPH predicted by AutoDock. a) Binding mode 1, α-tetralone was positioned on top of the nicotinamide ring as a stacking interaction, and the oxygen atom formed a H-bonding interaction with the side chain of residue Asn-39 (3.5 Å). b) α-tetralone again forms stacking interaction with nicotinamide ring, but the oxygen atom was orientated towards residue Arg-88 forming a H-bonding interaction (3.0 Å). PyAeADHII is shown as a cartoon (green) and residues in the substrate binding site are shown as sticks (carbon colored in yellow, nitrogen in blue, oxygen in red). NADPH (carbons are in grey) and the substrate α-tetralone (carbon are in orange) are shown as sticks.

    Journal: PLoS ONE

    Article Title: Physicochemical Characterization of a Thermostable Alcohol Dehydrogenase from Pyrobaculum aerophilum

    doi: 10.1371/journal.pone.0063828

    Figure Lengend Snippet: Binding interaction of α-tetralone in the substrate binding site of PyAeADHII/NADPH predicted by AutoDock. a) Binding mode 1, α-tetralone was positioned on top of the nicotinamide ring as a stacking interaction, and the oxygen atom formed a H-bonding interaction with the side chain of residue Asn-39 (3.5 Å). b) α-tetralone again forms stacking interaction with nicotinamide ring, but the oxygen atom was orientated towards residue Arg-88 forming a H-bonding interaction (3.0 Å). PyAeADHII is shown as a cartoon (green) and residues in the substrate binding site are shown as sticks (carbon colored in yellow, nitrogen in blue, oxygen in red). NADPH (carbons are in grey) and the substrate α-tetralone (carbon are in orange) are shown as sticks.

    Article Snippet: The standard assay for the reduction reaction of α-tetralone was performed by adding 2.6 μM final concentration of the enzyme to a preheated assay mixture containing 3 mM substrate (α-tetralone; Sigma-Aldrich #T19003, Lot S28914 or from Tokyo Chemical Industry #T0134), 0.3 mM NADPH (Sigma-Aldrich #N5130) in 50 mM sodium phosphate (pH 7.5) .

    Techniques: Binding Assay

    Inhibition of PyAeADHII at 70°C by flunarizine dihydrochloride. The assay was performed with 260 nM PyAeADHII in 50 mM NaPO4 pH 7.5, 3 mM α-tetralone, 0.3 mM NADPH in the presence of 80–1200 µM flunarizine dihydrochloride in DMSO/isopropanol. a) Absorbance of NADPH (340 nm) was measured over time at different flunarizine concentrations. b) The rate of NADPH conversion (Δa.u. = absorbance unit change/minute) versus flunarizine concentration.

    Journal: PLoS ONE

    Article Title: Physicochemical Characterization of a Thermostable Alcohol Dehydrogenase from Pyrobaculum aerophilum

    doi: 10.1371/journal.pone.0063828

    Figure Lengend Snippet: Inhibition of PyAeADHII at 70°C by flunarizine dihydrochloride. The assay was performed with 260 nM PyAeADHII in 50 mM NaPO4 pH 7.5, 3 mM α-tetralone, 0.3 mM NADPH in the presence of 80–1200 µM flunarizine dihydrochloride in DMSO/isopropanol. a) Absorbance of NADPH (340 nm) was measured over time at different flunarizine concentrations. b) The rate of NADPH conversion (Δa.u. = absorbance unit change/minute) versus flunarizine concentration.

    Article Snippet: The standard assay for the reduction reaction of α-tetralone was performed by adding 2.6 μM final concentration of the enzyme to a preheated assay mixture containing 3 mM substrate (α-tetralone; Sigma-Aldrich #T19003, Lot S28914 or from Tokyo Chemical Industry #T0134), 0.3 mM NADPH (Sigma-Aldrich #N5130) in 50 mM sodium phosphate (pH 7.5) .

    Techniques: Inhibition, Concentration Assay

    Outline of the BioGRO method. ( a ) The colours of RNA polymerases (RNAP) represent different transcriptional states. Only active elongating RNA pol II (green) is able to run-on. ( b ) Analysis of the size of the run-on elongation with Biotin-UTP. Biotinylated RNAs appear as a diffuse luminescent stain signal centred at about 50 nucleotides (nt). ( c ) BioGRO after a selective inhibition of RNA pol II with α-amanitin. The graph shows the comparison made between BioGRO signals in the presence or absence (control) of α-amanitin. In black, the RNA pol II genes and their trend line. The tRNA genes and their trend line are depicted in red. Green dots mark the RNA pol III transcripts that do not belong to the tRNA type.

    Journal: Nucleic Acids Research

    Article Title: Chromatin-dependent regulation of RNA polymerases II and III activity throughout the transcription cycle

    doi: 10.1093/nar/gku1349

    Figure Lengend Snippet: Outline of the BioGRO method. ( a ) The colours of RNA polymerases (RNAP) represent different transcriptional states. Only active elongating RNA pol II (green) is able to run-on. ( b ) Analysis of the size of the run-on elongation with Biotin-UTP. Biotinylated RNAs appear as a diffuse luminescent stain signal centred at about 50 nucleotides (nt). ( c ) BioGRO after a selective inhibition of RNA pol II with α-amanitin. The graph shows the comparison made between BioGRO signals in the presence or absence (control) of α-amanitin. In black, the RNA pol II genes and their trend line. The tRNA genes and their trend line are depicted in red. Green dots mark the RNA pol III transcripts that do not belong to the tRNA type.

    Article Snippet: Selective inhibition of RNA pol II In order to selectively inhibit the enzymatic activity of RNA pol II, the permeabilized cells were incubated 5 min before RNase A degradation with 50 μM of α-amanitin (Sigma).

    Techniques: Staining, Inhibition

    RNA pol III nascentome. In the upper part: ( a ) left panel: analysis of a metagene 5′ assay after the selective inhibition of RNA pol II with α-amanitin. Central panel: metagene tRNAs genes without intron. Right panel: metagene genes of tRNAs with introns. The entries at the top of both figures refer to the pre-tRNA structure: extensions 5′ and 3′ in orange, green introns. In the lower part, the correlations between: ( b ) the RNA pol III ChIP data from Kumar and Bhargava ( 31 ) and the BioGRO data; ( c ) the average nTR measured by BioGRO tRNAs of each family and the number of copies of the genes that make each family; ( d ) between BioGRO nTR and the amount of tRNAs for each family, taken from Tuller et al. ( 94 ).

    Journal: Nucleic Acids Research

    Article Title: Chromatin-dependent regulation of RNA polymerases II and III activity throughout the transcription cycle

    doi: 10.1093/nar/gku1349

    Figure Lengend Snippet: RNA pol III nascentome. In the upper part: ( a ) left panel: analysis of a metagene 5′ assay after the selective inhibition of RNA pol II with α-amanitin. Central panel: metagene tRNAs genes without intron. Right panel: metagene genes of tRNAs with introns. The entries at the top of both figures refer to the pre-tRNA structure: extensions 5′ and 3′ in orange, green introns. In the lower part, the correlations between: ( b ) the RNA pol III ChIP data from Kumar and Bhargava ( 31 ) and the BioGRO data; ( c ) the average nTR measured by BioGRO tRNAs of each family and the number of copies of the genes that make each family; ( d ) between BioGRO nTR and the amount of tRNAs for each family, taken from Tuller et al. ( 94 ).

    Article Snippet: Selective inhibition of RNA pol II In order to selectively inhibit the enzymatic activity of RNA pol II, the permeabilized cells were incubated 5 min before RNase A degradation with 50 μM of α-amanitin (Sigma).

    Techniques: Inhibition, Chromatin Immunoprecipitation