Interdependency of Sequence and Positional Specificities for Cysteine Proteases of the Papain Family ‡
✍ Scribed by Nägler, Dorit K.; Tam, Wendy; Storer, Andrew C.; Krupa, Joanne C.; Mort, John S.; Ménard, Robert
- Book ID
- 120316171
- Publisher
- American Chemical Society
- Year
- 1999
- Tongue
- English
- Weight
- 137 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0006-2960
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## Abstract Recent characterization of multiple classes of functionalized azapeptides as effective covalent inhibitors of cysteine proteases prompted us to investigate __O__‐acyl hydroxamates and their azapeptide analogues for use as activity‐based probes (ABPs). We report here a new class of azagl
Synthetic peptides corresponding to the proregions of papain-like cysteine proteases have been shown to be good and selective inhibitors of their parental enzymes. The molecular basis for their selectivity, quite remarkable in some cases, is not fully understood. The recent determination of the crys