recombination detection program (rdp 4.95) Search Results


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Jena Bioscience n m eda adp atto 495
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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R&D Systems osm
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Adafruit Industries usb cable usb a-plug to micro-usb data cable
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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RenderX Inc xsl·fo renderx
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Kodansha Ltd the kodansha japanese-english dictionary
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Carl Roth GmbH koh
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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86
Thermo Fisher optimem
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Dow Corning ® hv-495 hv-495 emulsion
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Ribobio co small interfering rnas for mir-495
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Chemie GmbH disperbyk 161
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Johns Hopkins HealthCare principles of law, revised
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Evident Corporation bp470-495
P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of <t>EDA–ADP–ATTO-495</t> to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.
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Image Search Results


P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of EDA–ADP–ATTO-495 to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.

Journal: The Journal of Biological Chemistry

Article Title: Adapted ATPase domain communication overcomes the cytotoxicity of p97 inhibitors

doi: 10.1074/jbc.RA118.004301

Figure Lengend Snippet: P472L mutation does not disrupt the binding sites of p97 inhibitors. A, ITC was used to measure the binding of CB-5083 to p97 and the P472L mutant. Top panels are raw data, and lower panels show isotherms with fitted curves and representative KD values. B, effect of increasing NMS-873 concentrations on TR-FRET generated by p97 and the P472L mutant in the presence of BODIPY-FL–ATP, and a terbium-labeled anti-His tag antibody was measured (n = 4, S.D.). Apparent KD values extrapolated from NMS-873–dependent increases in TR-FRET are shown. C, fluorescence polarization experiments were performed (n = 2, S.D.) to measure the enhanced binding of EDA–ADP–ATTO-495 to p97 and the P472L mutant with increasing NMS-873 concentrations. Apparent KD values with S.E. are shown.

Article Snippet: The 2-fold serial dilutions of p97 proteins (maximum 40 μ m , purified from bacteria) were mixed with 20 n m BODIPY-FL–ATP (ThermoFisher Scientific) or 10 n m EDA–ADP–ATTO-495 (Jena Bioscience) in black low volume 384-well plates.

Techniques: Mutagenesis, Binding Assay, Generated, Labeling, Fluorescence