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1 urn might be selectively removed by the PSMA exopeptidase.
2 ive carboxypeptidase E, a peptide-processing exopeptidase.
3 bind to MHC class II and are then trimmed by exopeptidase.
4 sis of N-carbamyl versus the peptide bond in exopeptidases.
5 no acids by the combined action of endo- and exopeptidases.
6 ight clusters and that most are generated by exopeptidase activities that confer cancer type-specific
7 enzyme (purified < or = 2000-fold) displayed exopeptidase activity in cleaving successive end-termina
8 mes, we demonstrate that PGI-LysAP has broad exopeptidase activity which may enhance V. vulnificus in
10 ll identified metabolites were formed due to exopeptidase- (amino- or carboxy-), amidase-, or endopep
13 athepsin B and L, T. gondii cathepsin Cs are exopeptidases and remove dipeptides from unblocked N-ter
15 e N-terminally truncated by endoproteases or exopeptidases, and many were further modified by Aat.
16 Both pancreatic CpB and TAFIa are zinc-based exopeptidases, and the proteins share a 47% sequence ide
17 oyed in the extracts by a bestatin-sensitive exopeptidase, apparently by the puromycin-sensitive amin
19 regulated in MIN6 cells, whereas that of the exopeptidase, carboxypeptidase H, was unaffected by gluc
21 resistant to matrix metalloproteinase-2 and exopeptidase cleavage but retains chemotactic bioactivit
23 ntially measuring the products of processive exopeptidase digestion, or by using a molecular motor to
26 ssibility of a general approach to designing exopeptidase inhibitors starting from the structure of t
30 reveals an alpha/beta scaffold akin to zinc exopeptidases of the peptidase M20 family and lacks the
31 ar to that seen in the post-proline cleaving exopeptidases prolylcarboxypeptidase and CD26/dipeptidyl
32 ages in plasma proteins created by endo- and exopeptidases, providing information about the activitie
33 extraction and characterized with regard to exopeptidase specificity and sensitivity to proteinase i
34 idyl peptidases (DPPs), with which it shares exopeptidase specificity, and prolyl oligopeptidase (PRE
35 Glutamate carboxypeptidase II (GCPII) is an exopeptidase that catalyzes the hydrolysis of N-acetylat
37 ysis inhibitor (TAFI) is the precursor of an exopeptidase that is identical to plasma procarboxypepti
38 e carboxypeptidase E/H gene which encodes an exopeptidase that removes C-terminal basic residues from
39 idase I (TPP I, CLN2 protein) is a lysosomal exopeptidase that sequentially removes tripeptides from
42 etalloproteases represents a large number of exopeptidases that cleave single amino acid residues fro
43 al the substrate specificity of any endo- or exopeptidase using liquid chromatography-tandem mass spe
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