Zobrazeno 1 - 10
of 11
pro vyhledávání: '"T. Narayana Bhat"'
Autor:
Sherman F. Stinson, David J. Clanton, Tyra House, Betty Yu, T. Narayana Bhat, John W. Erickson, Ramnarayan S. Randad, Michael A. Eissenstat, Lucyna Lubkowska, Sergei V. Gulnik
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 8:3537-3542
A series of novel unsymmetrical anthranilamide-containing HIV protease inhibitors was designed. The structure-activity studies revealed a series of potent P2–P3′ inhibitors that incorporate an anthranilamide group at the P2′ position. A reducti
Autor:
Stephen J. Stahl, Paul T. Wingfield, Darón I. Freedberg, T. Narayana Bhat, and John W. Erickson, Dennis A. Torchia, Yun-Xing Wang, Yoshiaki Kiso, Joshua D. Kaufman
Publikováno v:
Journal of the American Chemical Society. 118:12287-12290
KNI-272 is a peptidomimetic transition state analog inhibitor, having very high specificity and binding affinity for the HIV-1 protease. In order to understand the interactions that enhance drug bi...
Autor:
Betty Yu, Tracy M. Lynch, Rajan H. Naik, Sergei V. Gulnik, Ramnarayan S. Randad, Abelardo Silva, Anna Bujacz, Sanjeev Munshi, Lucyna Lubkowska, John W. Erickson, T. Narayana Bhat, David J. Clanton
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 5:2557-2562
Guided by the structure of HIV PR complexed with 2S,3R,4S,5S-2,5-bis[N,N'-((3-hydroxy-2-methylphenyl)carbonyl)amino]-3,4-dihydroxy-1,6-diphenyl hexane (1), a novel, achiral, non-peptidic anthranil (Ant) group was designed as a P2/P2′ ligand. Symmet
Autor:
T. Narayana Bhat, Ramnarayan S. Randad, Sanjeev Munshi, John W. Erickson, Betty Yu, Sergei V. Gulnik, Lucyna Lubkowska
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 5:1707-1712
Readily accessible, non-peptidic, achiral 2-methylbenzamides were designed to serve as P2/P2′ ligands for symmetry-based inhibitors of HIV-1 Protease. Introduction of 3-hydroxy substituent provided a potent inhibitor 7 ( K i = 0.8 nM).
Autor:
Igor A. Topol, T. Narayana Bhat, Beishan Liu, Sergei V. Gulnik, Hiroaki Mitsuya, Eric T. Baldwin, John W. Erickson, Tsutomu Mimoto, Yoshiaki Kiso
Publikováno v:
Structure. 3:581-590
Background: HIV-1 protease (HIV PR), an aspartic protease, cleaves Phe–Pro bonds in the Gag and Gag–Pol viral polyproteins. Substrate-based peptide mimics constitute a major class of inhibitors of HIV PR presently being developed for AIDS treatme
Autor:
Sherman F. Stinson, David J. Clanton, Lucyna Lubkowska, T. Narayana Bhat, Betty Yu, Sergei V. Gulnik, Michael A. Eissenstat, Ramnarayan S. Randad, Tyra House, John W. Erickson
Publikováno v:
ChemInform. 30
A series of novel unsymmetrical anthranilamide-containing HIV protease inhibitors was designed. The structure-activity studies revealed a series of potent P2–P3′ inhibitors that incorporate an anthranilamide group at the P2′ position. A reducti
Autor:
M.-M. Riottot, Ve´ronique Chitarra, T. Narayana Bhat, Graham A. Bentley, Silvia Spinelli, Roberto J. Poljak, He´le`ne Souchon, Anne Houdusse, G. Boulot, J.-L. Eisele
Publikováno v:
Journal of Crystal Growth. 122:337-343
The variable Fv fragments of antibodies, cloned in recombinant plasmids, can be expressed in bacteria as functional proteins having immunochemical properties which are very similar or identical with those of the corresponding parts of the parent euka
Publikováno v:
Aspartic Proteinases ISBN: 9781461357612
Cathepsin D (EC 3.4.23.5) (CatD) is an intracellular aspartic protease (AP) that is normally found in the lysosomes of higher eukaryotes. CatD shares two structural features with lysosomal enzymes that distinguish it from most secreted, extracellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f9e80c456e357520af7308a84c0d6031
https://doi.org/10.1007/978-1-4615-1871-6_22
https://doi.org/10.1007/978-1-4615-1871-6_22
Autor:
John W. Erickson, Eric T. Baldwin, Sergi Gulnik, Beishan Liu, T. Narayana Bhat, Hiroaki Mitsuya, Yoshiaki Kiso
Publikováno v:
Aspartic Proteinases ISBN: 9781461357612
Inhibitors of human immunodeficiency virus type 1 protease (HIV PR) are the subject of wide interest for the development of therapeutic drugs against AIDS [1–4]. The crystal structures of numerous HIV PR/inhibitor complexes have been solved to aid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b942738e95b33623dba87effb5fd9ea
https://doi.org/10.1007/978-1-4615-1871-6_57
https://doi.org/10.1007/978-1-4615-1871-6_57
Autor:
Jean Luc Eiselé, E. Sally Ward, T. Narayana Bhat, Roberto J. Poljak, Greg Winter, G. Boulot, Graham A. Bentley
Publikováno v:
Journal of molecular biology. 213(4)
The associated heavy (V H ) and light (V L ) chain variable domains (F V ) of the monoclonal anti-lysozyme antibody D1.3, secreted from Escherichia coli , have been crystallized in their antigen-bound and free forms. FvD1.3 gives tetragonal crystals,