ライフサイエンスコーパス: exopeptidase

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 strates and products of major EECs endo- and exopeptidases.

7 ight clusters and that most are generated by exopeptidase activities that confer cancer type-specific

8 enzyme (purified < or = 2000-fold) displayed exopeptidase activity in cleaving successive end-termina

9 he hydrolysates, which was attributed to the exopeptidase activity of Protease M.

10 mes, we demonstrate that PGI-LysAP has broad exopeptidase activity which may enhance V. vulnificus in

11 ty coupled with carboxyl, amino, and leucine exopeptidase activity, resulting in relatively more hydr

12 substrate, whereas the human enzyme exhibits exopeptidase activity.

13 ing at the alpha carbon, in keeping with its exopeptidase activity.

14 ll identified metabolites were formed due to exopeptidase- (amino- or carboxy-), amidase-, or endopep

15 A nonspecific exopeptidase, aminopeptidase N (APN), is inhibited seque

16 However, SDF-1 is cleaved by exopeptidases and matrix metalloproteinase-2, generating

17 athepsin B and L, T. gondii cathepsin Cs are exopeptidases and remove dipeptides from unblocked N-ter

18 independent fashion by the action of various exopeptidases and the endopeptidase furin.

19 e N-terminally truncated by endoproteases or exopeptidases, and many were further modified by Aat.

20 Both pancreatic CpB and TAFIa are zinc-based exopeptidases, and the proteins share a 47% sequence ide

21 oyed in the extracts by a bestatin-sensitive exopeptidase, apparently by the puromycin-sensitive amin

22 tease (mMCP) 5, the tryptase mMCP-6, and the exopeptidase carboxypeptidase A (mMC-CPA).

23 regulated in MIN6 cells, whereas that of the exopeptidase, carboxypeptidase H, was unaffected by gluc

24 udied a plasmodial ortholog of the lysosomal exopeptidase cathepsin C.

25 resistant to matrix metalloproteinase-2 and exopeptidase cleavage but retains chemotactic bioactivit

26 BM, collagen Type IV, requires prolidase, an exopeptidase cleaving the imidodipeptides containing pro

27 Removal of amino-terminal alanine by exopeptidase digestion restored protease inhibitor activ

28 ntially measuring the products of processive exopeptidase digestion, or by using a molecular motor to

29 The approach combines exopeptidase digestions of the proteome with two-dimensi

30 nes are rapidly inactivated in plasma by the exopeptidase dipeptidyl peptidase (DPP) IV.

31 corticoid-regulated genes, we identified the exopeptidase dipeptidyl peptidase-4 (DPP4) as a critical

32 onA-like lectins/glucanases and Zn-dependent exopeptidases domains.

33 aminopeptidase) of the binuclear N-terminal exopeptidase family.

34 d Protamex(R), used alone or followed by the exopeptidase Flavourzyme(R).

35 ification of EEC-expressed endopeptidase and exopeptidase genes.

36 opeptidases of different selectivity and one exopeptidase in order to produce hydrolysates with antid

37 ssibility of a general approach to designing exopeptidase inhibitors starting from the structure of t

38 TPP2 is a serine exopeptidase involved in extralysosomal peptide degradat

39 Carboxypeptidase E (CPE), an exopeptidase involved in proneuropeptide processing, is

40 In animals, one important intermediate exopeptidase is tripeptidyl peptidase (TPP)II, which dig

41 yzed by trypsin and Protease M, a novel endo/exopeptidase mix from Aspergillus oryzae.

42 Tripeptidyl peptidase II (TPP II) is an exopeptidase of the subtilisin type of serine proteases

43 reveals an alpha/beta scaffold akin to zinc exopeptidases of the peptidase M20 family and lacks the

44 ar to that seen in the post-proline cleaving exopeptidases prolylcarboxypeptidase and CD26/dipeptidyl

45 ages in plasma proteins created by endo- and exopeptidases, providing information about the activitie

46 extraction and characterized with regard to exopeptidase specificity and sensitivity to proteinase i

47 idyl peptidases (DPPs), with which it shares exopeptidase specificity, and prolyl oligopeptidase (PRE

48 Glutamate carboxypeptidase II (GCPII) is an exopeptidase that catalyzes the hydrolysis of N-acetylat

49 Plasma carboxypeptidase B (PCB) is an exopeptidase that exerts an antifibrinolytic effect by r

50 ysis inhibitor (TAFI) is the precursor of an exopeptidase that is identical to plasma procarboxypepti

51 e carboxypeptidase E/H gene which encodes an exopeptidase that removes C-terminal basic residues from

52 idase I (TPP I, CLN2 protein) is a lysosomal exopeptidase that sequentially removes tripeptides from

53 ce, plants likely contain other intermediate exopeptidases that assist in amino acid recycling.

54 d the selectivity of compounds against other exopeptidases that cleave basic residues.

55 etalloproteases represents a large number of exopeptidases that cleave single amino acid residues fro

56 drolysis during gastroduodenal digestion and exopeptidases that hydrolyse peptides in the small intes

57 7 leucyl aminopeptidases are metal-dependent exopeptidases that rely on oligomerization to diversify

58 al the substrate specificity of any endo- or exopeptidase using liquid chromatography-tandem mass spe

59 PSMA is a unique exopeptidase with reactivity toward poly-gamma-glutamate