Search Results - (Author, Cooperation:J. J. Chou)
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1Latest Papers from Table of Contents or Articles in PressK. Oxenoid ; Y. Dong ; C. Cao ; T. Cui ; Y. Sancak ; A. L. Markhard ; Z. Grabarek ; L. Kong ; Z. Liu ; B. Ouyang ; Y. Cong ; V. K. Mootha ; J. J. Chou
Nature Publishing Group (NPG)
Published 2016Staff ViewPublication Date: 2016-05-03Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsPublished by: -
2Latest Papers from Table of Contents or Articles in PressM. J. Berardi ; W. M. Shih ; S. C. Harrison ; J. J. Chou
Nature Publishing Group (NPG)
Published 2011Staff ViewPublication Date: 2011-07-26Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Adenine Nucleotide Translocator 1/chemistry/metabolism ; Animals ; Binding Sites ; Cattle ; Databases, Protein ; Guanosine Diphosphate/chemistry/metabolism ; Ion Channels/*chemistry/metabolism ; Mice ; Mitochondrial ADP, ATP Translocases/chemistry ; Mitochondrial Proteins/*chemistry/metabolism ; Models, Molecular ; Nitrogen Oxides/chemistry/metabolism ; Nuclear Magnetic Resonance, Biomolecular/*methods ; Protein ConformationPublished by: -
3Latest Papers from Table of Contents or Articles in PressB. OuYang ; S. Xie ; M. J. Berardi ; X. Zhao ; J. Dev ; W. Yu ; B. Sun ; J. J. Chou
Nature Publishing Group (NPG)
Published 2013Staff ViewPublication Date: 2013-06-07Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Adamantane/analogs & derivatives/chemistry/metabolism/pharmacology ; Binding Sites ; Diffusion ; Hepacivirus/*chemistry ; Microscopy, Electron ; Models, Biological ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Porosity ; Rimantadine/chemistry/metabolism/pharmacology ; Structure-Activity Relationship ; Viral Proteins/antagonists & inhibitors/*chemistry/metabolism/ultrastructurePublished by: -
4Articles: DFG German National LicensesStaff View
ISSN: 0308-521XSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, NutritionType of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesAlthaus, I. W. ; Chou, J. J. ; Gonzales, A. J. ; LeMay, R. J. ; Deibel, M. R. ; Chou, K. -C. ; Kezdy, F. J. ; Romero, D. L. ; Thomas, R. C. ; Aristoff, P. A. ; Tarpley, W. G. ; Reusser, F.
Springer
Published 1994Staff ViewISSN: 1420-9071Keywords: HIV RT ; polysulfonate ; inhibitor ; steady-state kineticsSource: Springer Online Journal Archives 1860-2000Topics: BiologyMedicineNotes: Abstract The tetramer of ethylenesulfonic acid (U-9843) is a potent inhibitor of HIV-1 RT* and possesses excellent antiviral activity at nontoxic doses in HIV-1 infected lymphocytes grown in tissue culture. Kinetic studies of the HIV-1 RT-catalyzed RNA-directed DNA polymerase activity were carried out in order to determine if the inhibitor interacts with the template: primer or the deoxyribonucleotide triphosphate (dNTP) binding sites of the polymerase. Michaelis-Menten kinetics, which are based on the establishment of a rapid equilibrium between the enzyme and its substrates, proved inadequate for the analysis of the experimental data. The data were thus analyzed using steady-state Briggs-Haldane kinetics assuming that the template:primer binds to the enzyme first, followed by the binding of the dNTP and that the polymerase is a processive enzyme. Based on these assumptions, a velocity equation was derived which allows the calculation of all the specific forward and backward rate constants for the reactions occurring between the enzyme, its substrates and the inhibitor. The calculated rate constants are in agreement with this model and the results indicated that U-9843 acts as a noncompetitive inhibitor with respect to both the template:primer and dNTP binding sites. Hence, U-9843 exhibits the same binding affinity for the free enzyme as for the enzyme-substrate complexes and must inhibit the RT polymerase by interacting with a site distinct from the substrate binding sites. Thus, U-9843 appears to impair an event occurring after the formation of the enzyme-substrate complexes, which involves either an event leading up to the formation of the phosphoester bond, the formation of the ester bond itself or translocation of the enzyme relative to its template:primer following the formation of the ester bond.Type of Medium: Electronic ResourceURL: