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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
5                The enzymes exhibited optimum caseinolytic activity at 60 degrees C and a pH range of
6                   HT had the highest rate of caseinolytic activity at the lowest concentration (0.1 m
7 onal antibodies against proteinase 3 removed caseinolytic activity from wound fluid, and that purifie
8                                              Caseinolytic activity in wound fluid increased markedly
9                   In this study, we analyzed caseinolytic activity in wound fluid obtained from acute
10                                         Weak caseinolytic activity inhibitable by cysteine protease i
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%
13 alytic Cys residue to Ser leads to a loss of caseinolytic activity of DEK1 domain II&III.
14                          There was increased caseinolytic activity of MMP-3 and collagenolytic activi
15 tone produced half-maximum inhibition of the caseinolytic activity of mu-calpain at concentrations of
16                                              Caseinolytic activity of the precipitated protein fracti
17 on, as determined both by immunoblotting and caseinolytic activity on agar plates.
18                                      Highest caseinolytic activity on azocasein was detected after pr
19 tioned medium of these cultures (measured as caseinolytic activity) was enhanced by L-NMA; however, t
20                    Abnormally high levels of caseinolytic activity, consistent with NE, were detected
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
23 0 mg mL(-1) to achieve their maximum rate of caseinolytic activity.
24 artilage matrix loss with increased secreted caseinolytic activity.
25 nzyme accounted for approximately 80% of the caseinolytic activity.
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
28                                            A caseinolytic assay and Western blotting indicated that s
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
31 due to a down-regulation of gelatinolytic or caseinolytic matrix metalloproteinases.
32 ed by the mitochondrial AAA+ unfoldase CLPX (caseinolytic mitochondrial matrix peptidase chaperone su
33                                          The caseinolytic mitochondrial matrix peptidase chaperone su
34                          Whereas the plastid caseinolytic peptidase (Clp) P protease system is essent
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
37 can, we identified biallelic variants in the caseinolytic peptidase B homolog (CLPB).
38                                 CLPB encodes caseinolytic peptidase B homolog ClpB, a member of the A
39                                 Among these, caseinolytic peptidase B protein homolog (CLPB) is local
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
42                                              Caseinolytic peptidase P (ClpP), a double-ring peptidase
43 and that purified proteinase 3 had a similar caseinolytic profile and inhibitor sensitivity to burn f
44                                  The plastid caseinolytic protease (Clp) complex plays essential role
45                                          The caseinolytic protease (Clp) protease system has been exp
46 (CLPP), a key component of the mitochondrial caseinolytic protease (CLP) serine endopeptidase, as bei
47                       Here, we show that the caseinolytic protease (Clp) substrate adaptor ClpS1 and
48                                          The caseinolytic protease (Clp) system has recently emerged
49 e, while its hibernation is inhibited by the caseinolytic protease (Clp) system in a zinc-dependent m
50          Plants defective in the chloroplast caseinolytic protease (Clp) system were specifically imp
51            One such complex in plants is the caseinolytic protease (Clp), which plays an essential ro
52 ial agents that act through dysregulation of caseinolytic protease (ClpP).
53 lated by a series of proteases including the caseinolytic protease (CLPP).
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
56 D triggers degradation of the protein by the caseinolytic protease ClpC1-ClpP.
57 to 10-fold up-regulation of AtRH3 in plastid Caseinolytic protease mutants.
58 bstrates into the degradation chamber of the caseinolytic protease P (ClpP) for proteolysis.
59                            The barrel-shaped caseinolytic protease P (ClpP) is a main virulence regul
60                            The mitochondrial caseinolytic protease P (ClpP) plays a central role in m
61                                              Caseinolytic protease P (ClpP) represents a central bact
62  including the mitochondrial matrix protease caseinolytic protease P (ClpP).
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
67                                          The caseinolytic protease subunit P (ClpP) is a serine prote
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
71                            The ATP-dependent caseinolytic protease, ClpP, is highly conserved in bact
72       Here, we study an apicoplast-localized caseinolytic-protease (Clp) system and how it regulates
73                                              Caseinolytic proteases (Clp) are central to bacterial pr
74                                              Caseinolytic proteases (ClpP) from pathogenic bacteria a
75                                              Caseinolytic proteases (ClpPs) are large oligomeric prot
76 ined for the expression of gelatinolytic and caseinolytic proteases as well as for proteinase inhibit