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1 agmentation propensities produced by a novel alpha-lytic protease.
2 two peptide boronic acid inhibitors bound to alpha-lytic protease.
3 His57 in the Ala-Ala-Pro-Val-cmk complex of alpha-lytic protease.
4 lutamate residues in uniformly (13)C-labeled alpha-lytic protease.
8 the extracellular bacterial serine protease alpha-lytic protease (alphaLP) has been solved at 0.83 A
12 have solved two X-ray crystal structures of alpha-lytic protease (alphaLP) that mimic aspects of the
16 roblast activation protein alpha (FAPalpha), alpha-lytic protease (alphaLP), trypsin, and chymotrypsi
18 olding of the extracellular serine protease, alpha-lytic protease (alphaLP; EC 3.4.21.12) reveals a n
20 proton of the catalytic histidine in resting alpha-lytic protease and subtilisin BPN' resonates, when
21 ilar observations with the bacterial enzymes alpha-lytic protease and subtilisin, and stands in sharp
24 strate specificity, the backbone dynamics of alpha-lytic protease have been investigated using 15N re
32 ntative of the pro regions of subtilisin and alpha-lytic protease, which are generally considered to
33 their respective targets, the pro region of alpha-lytic protease with its dual roles in folding and
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