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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.