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Brian W. Metcalf
Researcher at Smith, Kline & French
Publications - 152
Citations - 4081
Brian W. Metcalf is an academic researcher from Smith, Kline & French. The author has contributed to research in topics: Steroid & Alkyl. The author has an hindex of 34, co-authored 149 publications receiving 4038 citations. Previous affiliations of Brian W. Metcalf include Incyte.
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Journal ArticleDOI
4‐Amino‐hex‐5‐enoic Acid, a Selective Catalytic Inhibitor of 4‐Aminobutyric‐Acid Aminotransferase in Mammalian Brain
TL;DR: The irreversible inhibition of mammalian 4-aminobutyrate aminotransferase by 4-amino-hex-5-enoic acid is selective and there is no inhibition of this enzyme from Pseudomonas fluorescens with the inhibitor at mM concentrations.
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Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor
Christine Debouck,Joselina G. Gorniak,James E. Strickler,Thomas D. Meek,Brian W. Metcalf,Martin Rosenberg +5 more
TL;DR: This system will allow detailed structure-function analysis of the HIV protease and provides a simple assay for the development of potential therapeutic agents directed against this critical viral enzyme.
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Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analogues.
Thomas D. Meek,Dennis M. Lambert,Geoffrey B. Dreyer,Thomas Joseph Carr,Thaddeus A. Tomaszek,Michael L. Moore,James E. Strickler,Christine Debouck,Lawrence J. Hyland,Thomas J. Matthews,Brian W. Metcalf,S. R. Petteway +11 more
TL;DR: It is demonstrated that synthetic peptide analogues, which are potent inhibitors of purified HIV-1 protease, inhibit the processing of the viral polyproteins in cultures of HIV- 1-infected T lymphocytes and attenuate viral infectivity.
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Inhibition of human immunodeficiency virus 1 protease in vitro: rational design of substrate analogue inhibitors
Geoffrey B. Dreyer,Brian W. Metcalf,Thaddeus A. Tomaszek,Thomas Joseph Carr,Chandler Ac rd,Lawrence J. Hyland,Stephen A. Fakhoury,Victoria W. Magaard,Michael L. Moore,James E. Strickler +9 more
TL;DR: Inhibitors of the protease from human immunodeficiency virus 1 (HIV-1) were designed, synthesized, and kinetically characterized and effectively blocked the proteolytic processing of a recombinant form of Pr55gag by HIV-1 protease in a cell-free assay.
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Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease
Thomas D. Meek,Brian D. Dayton,Brian W. Metcalf,Geoffrey B. Dreyer,James E. Strickler,Joselina G. Gorniak,Martin Rosenberg,Michael L. Moore,Victoria W. Magaard,Christine Debouck +9 more
TL;DR: Recombinant human immunodeficiency virus 1 (HIV-1) protease, purified from a bacterial expression system, processed a recombinant form of its natural substrate, Pr55gag, into protein fragments that possess molecular weights commensurate with those of the virion gag proteins.