N-terminal domain of pepsin as a model for retroviral dimeric aspartyl protease
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference18 articles.
1. Structural evidence for gene duplication in the evolution of the acid proteases
2. A structural model for the retroviral proteases
3. Inhibition of retroviral protease activity by an aspartyl proteinase inhibitor
4. Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1
5. Molecular Modeling of the HIV-1 Protease and Its Substrate Binding Site
Cited by 9 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Rabbit endogenous retrovirus-H encodes a functional protease FN1;Journal of General Virology;2003-01-01
2. STABILITY OF PEPSIN (EC 3.4.23.1) DURING IN VITRO PROTEIN DIGESTIBILITY ASSAY2;Journal of Food Biochemistry;2002-09
3. New hydroxyethylamine HIV protease inhibitors that suppress viral replication;Journal of Medicinal Chemistry;1992-10
4. Enzymic activities of two-chain pepsinogen, two-chain pepsin, and the amino-terminal lobe of pepsinogen.;Journal of Biological Chemistry;1992-10
5. Structural and evolutionary relationships between retroviral and eukaryotic aspartic proteinases;Biochemistry;1991-05-01
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