Year: 1995
Type: article
Abstract: The human immunodeficiency virus Gag- and Pol-encoded proteins are expressed as long polypeptide precursors that are proteolytically cleaved into mature proteins found in infectious virions. This cleavage is catalyzed by the virus-encoded aspartyl protease and is required for virus replication(1, 2, 3). As such, the viral protease has become a target for HIV 1 therapeutics, resulting in many HIV protease inhibitors reaching clinical trials. Most of these drugs are substrate-based inhibitors, whose design has been facilitated by an abundance of crystal structure data for both the native enzyme and enzyme-inhibitor complexes(4).
Source: Journal of Biological Chemistry
Authors: Todd Ridky, Jonathan Leis
Institution: Case Western Reserve University
Language: English
Subfield: Infectious Diseases
Field: Medicine
Domain: Health Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2035341183