An Allosteric Modulator of HIV-1 Protease Shows Equipotent Inhibition of Wild-Type and Drug-Resistant Proteases-Reference-Cited by-同舟云学术

An Allosteric Modulator of HIV-1 Protease Shows Equipotent Inhibition of Wild-Type and Drug-Resistant Proteases

Published:2014-08-01 Issue:15 Volume:57 Page:6468-6478
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Ung Peter M.-U.¹,Dunbar James B.¹,Gestwicki Jason E.²,Carlson Heather A.¹

Affiliation:

1. Department of Medicinal Chemistry, College of Pharmacy, University of Michigan, 428 Church Street, Ann Arbor, Michigan 48109-1065, United States

2. Department of Pathology and the Life Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, Michigan 48109-2216, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm5008352

Reference71 articles.

1. A poke in the eye: Inhibiting HIV-1 protease through its flap-recognition pocket

2. Fragment-Based Screen against HIV Protease

3. The Energy Landscapes and Motions of Proteins

4. The role of dynamic conformational ensembles in biomolecular recognition

5. Molecular modeling studies of HIV-1 reverse transcriptase nonnucleoside inhibitors: Total energy of complexation as a predictor of drug placement and activity

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