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1 lagenolytic, gelatinolytic, elastolytic, and caseinolytic activities in vivo by the transduced fibrob
2 n batch mode, by evaluating protein loading, caseinolytic activity and the coagulation properties of
3 and substrate conditions using esterase and caseinolytic activity assays and time course hydrolysis
4 olytic activity at 92 and 72 kDa, as well as caseinolytic activity at 57, 45, and 19 kDa in the lipid
7 onal antibodies against proteinase 3 removed caseinolytic activity from wound fluid, and that purifie
11 gs suggested that the enzyme responsible for caseinolytic activity might be proteinase 3, an elastase
12 Val was a reasonably potent inhibitor of the caseinolytic activity of 20 S proteasome, producing 50%
15 tone produced half-maximum inhibition of the caseinolytic activity of mu-calpain at concentrations of
19 tioned medium of these cultures (measured as caseinolytic activity) was enhanced by L-NMA; however, t
21 ey showed a high ratio of milk-clotting over caseinolytic activity, indicating they had an excellent
22 ly expressed DEK1 domain II does not display caseinolytic activity, suggesting an important role for
26 eports the detection and characterization of caseinolytic and milk-clotting activities from Moringa o
27 yperlipemic groups elaborated gelatinolytic, caseinolytic, and elastinolytic activity attributable to
29 DEK1 domain II&III exhibits activity in the caseinolytic assay in the absence of calcium, although t
30 tructure of the proteolytic component of the caseinolytic Clp protease (ClpP) from E. coli at 2.3 A r
32 ed by the mitochondrial AAA+ unfoldase CLPX (caseinolytic mitochondrial matrix peptidase chaperone su
35 d six different sites of the hexamer protein Caseinolytic Peptidase B (ClpB) of Thermus thermophilus
36 y to HEAT SHOCK PROTEIN 101, which encodes a caseinolytic peptidase B chaperonin required for thermot
40 fied heterozygous missense variants of CLPB (caseinolytic peptidase B) in 5 severe congenital neutrop
41 y, we showed that the mitochondrial protease caseinolytic peptidase P (ClpP) is both a cell-intrinsic
43 and that purified proteinase 3 had a similar caseinolytic profile and inhibitor sensitivity to burn f
46 (CLPP), a key component of the mitochondrial caseinolytic protease (CLP) serine endopeptidase, as bei
49 e, while its hibernation is inhibited by the caseinolytic protease (Clp) system in a zinc-dependent m
54 t Shock Protein 101 (HSP101), the homolog of Caseinolytic Protease B (CLPB) proteins, has functional
55 s thaliana), the At1g74310 locus encodes for caseinolytic protease B-cytoplasmic (ClpB-C)/heat shock
63 n 60 (HSP60, a mitochondrial chaperonin) and caseinolytic protease P (ClpP, a mitochondrial protease)
64 inhibit proteases such as the proteasome or caseinolytic protease P, highlighting their potential in
65 recombination system we have deleted clpP1 (caseinolytic protease P1), one of the three genes (clpP1
66 ngle-cell transcriptomics, we identified the caseinolytic protease proteolytic subunit (CLPP), a key
68 A well-conserved protein complex named ClpP (caseinolytic protease) plays a vital role in adaptation
69 losis (Mtb) harbors a well-orchestrated Clp (caseinolytic protease) proteolytic machinery consisting
70 heat shock protein 78 (LdHSP78), a putative caseinolytic protease, as important for parasite infecti
76 ined for the expression of gelatinolytic and caseinolytic proteases as well as for proteinase inhibit