ArticleThe Biochemical journal1990
The selectivity of statine-based inhibitors against various human aspartic proteinases.
Article in The Biochemical journal, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 41 citations in OpenAlex.
- Cathepsin D-Managing the Delicate Balance.Pharmaceutics · 2021Review
- Selective detection of Cathepsin E proteolytic activity.Biochimica et biophysica acta · 2010Article
- Modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin.Protein science : a publication of the Protein Society · 2000Article
- Structure-based subsite specificity mapping of human cathepsin D using statine-based inhibitors.Protein science : a publication of the Protein Society · 1997Article
- Crystal structure of human pepsin and its complex with pepstatin.Protein science : a publication of the Protein Society · 1995Article
- CGP 53437, an orally bioavailable inhibitor of human immunodeficiency virus type 1 protease with potent antiviral activity.Antimicrobial agents and chemotherapy · 1993Article
- Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Two crystal structures for cathepsin D: the lysosomal targeting signal and active site.The EMBO journal · 1993Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interactions of five human enzymes (renin, pepsin, gastricsin, cathepsin D and cathepsin E) and the aspartic proteinase from Endothia parasitica with several series of synthetic inhibitors were examined. All of the inhibitors contained the dipeptide analogue statine or its phenylalanine or cyclohexylalanine homologues in the P1-P1' positions. The residues occupying the peripheral sub-sites (P4 to P3') were varied systematically and inhibitory constants were determined for the interactions with each of the proteinases. Inhibitors were elucidated that specifically inhibited human renin and did not affect any of the other human enzymes or the fungal proteinase. With suitable selection of residues to occupy individual sub-sites, effective inhibitors of specific human aspartic proteinases may now be designed.
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