ライフサイエンスコーパス: dipeptidyl peptidase I

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1 o its active form by the cysteine proteinase dipeptidyl peptidase I.

2 he processing enzyme for proteinase 3 is not dipeptidyl peptidase I.

3 molecular basis for the regulation of human dipeptidyl-peptidase I.

4 Dipeptidyl-peptidase I, a lysosomal cysteine proteinase,

5 dipeptide on beta-pro'tryptase is removed by dipeptidyl peptidase I at acid pH in the absence of hepa

6 as not delayed in perforin-deficient mice or dipeptidyl peptidase I-deficient mice, which fail to pro

7 onditions under which it may be activated by dipeptidyl peptidase I (DPP I).

8 rectly inhibits the activity of MMP20, KLK4, dipeptidyl peptidase I (DPPI) (an in vitro activator of

9 The cysteine protease dipeptidyl peptidase I (DPPI) activates granule-associat

10 lammation, we generated a mouse deficient in dipeptidyl peptidase I (DPPI) and established that DPPI

11 Dipeptidyl peptidase I (DPPI) is a cysteine aminopeptida

12 Dipeptidyl peptidase I (DPPI) is a cysteine protease fou

13 Dipeptidyl peptidase I (DPPI) is a cysteine protease req

14 Dipeptidyl peptidase I (DPPI) is a granule protease that

15 Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine pr

16 Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine pr

17 Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine pr

18 Dipeptidyl peptidase I (DPPI) is the sole activator in v

19 e injected TxA into ileal loops in PAR(2) or dipeptidyl peptidase I (DPPI) knockout mice or in wild-t

20 CTL express high levels of dipeptidyl peptidase I (DPPI), a granule thiol protease

21 In this study, we show that the absence of dipeptidyl peptidase I (DPPI), a lysosomal cysteine prot

22 the lysosomal cysteine protease cathepsin C/dipeptidyl peptidase I (DPPI).

23 However, treatment of cells with a dipeptidyl peptidase I inhibitor, Gly-Phe-diazomethyl ke

24 Cathepsin C, or dipeptidyl peptidase I, is a lysosomal cysteine protease

25 Northern analyses demonstrated that the dipeptidyl-peptidase I message is expressed at high leve

26 ukin-2 resulted in a significant increase in dipeptidyl-peptidase I mRNA levels, suggesting that this

27 CD26/dipeptidyl peptidase is responsible for serum cleavage o

28 n inactivating mutation in the gene encoding dipeptidyl peptidase I, resulting in neutrophils lacking

29 aring features like propeptide processing by dipeptidyl peptidase I, storage, and release as an activ

30 In the present investigation the gene for dipeptidyl-peptidase I was cloned and characterized.

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