Flexibility and function in HIV-1 protease-Reference-Cited by-同舟云学术

Flexibility and function in HIV-1 protease

Published:1995-04 Issue:4 Volume:2 Page:274-280
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Nicholson Linda K.,Yamazaki Toshimasa,Torchia Dennis A.,Grzesiek Stephan,Bax Ad,Stahl Stephen J.,Kaufman Joshua D.,Wingfield Paul T.,Lam Patrick Y.S,Jadhav Prabhakar K.,Hodge C. Nicholas,Domaille Peter J.,Chang Chong-Hwan

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsb0495-274.pdf

Reference42 articles.

1. Active human immunodeficiency virus protease is required for viral infectivity.

2. Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A.

3. Rational Design of Potent, Bioavailable, Nonpeptide Cyclic Ureas as HIV Protease Inhibitors

4. NMR Evidence for the Displacement of a Conserved Interior Water Molecule in HIV Protease by a Non-Peptide Cyclic Urea-Based Inhibitor

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