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1 , we have followed the fate of pulse-labeled procathepsin B (ProB, a lysosomal proenyzme) after postp
2 TNFalpha], and IL-6), and catabolic enzymes (procathepsin B and neutrophil elastase) were measured in
3     Therefore, ARF1-dependent trafficking of procathepsin B and the maturation of autophagosomes resu
4                                 Furthermore, procathepsin B could interact with the annexin II tetram
5           Secretion of the cysteine protease procathepsin B from breast fibroblasts may have physiolo
6     We have confirmed that recombinant human procathepsin B interacts with p11 as well as with the an
7 d exocytosis in parallel with insulin, while procathepsin B is efficiently converted to the mature fo
8                                We found that procathepsin B is enriched in Golgi-containing microsome
9 ation-dependent MPRs, the modest fraction of procathepsin B normally remaining within mature secretor
10  tetramer can serve as a binding protein for procathepsin B on the surface of tumor cells, an interac
11 (2), and beta(1) integrin subunits prevented procathepsin B secretion from fibroblasts grown on colla
12                                 In addition, procathepsin B secretion was induced when cells were pla
13                                 Trypsinogen, procathepsin B, and IL-6 concentrations as well as cathe
14                    IL-1beta, TNFalpha, IL-6, procathepsin B, and neutrophil elastase concentrations i
15 sion and secretion of cathepsin B, primarily procathepsin B, was induced by growth on collagen I gels
16  caerulein treatment increased processing of procathepsin B, whereas a known ARF inhibitor brefeldin
17  as a significant export route for lysosomal procathepsin B.
18 screen for proteins that interact with human procathepsin B.
19 r distribution of the cathepsin B precursor, procathepsin B.
20 iminishing the stimulus-dependent release of procathepsin B.
21 rocathepsin K is similar to that observed in procathepsins B and L despite differences in length and
22 int of human cathepsin D was engineered into procathepsin D according to known specificity requiremen
23 oved 6 residues toward the amino terminus of procathepsin D and expressed in Escherichia coli.
24 r the previously described hypersecretion of procathepsin D induced by wortmannin.
25 ot analyses revealed that whereas the 51-kDa procathepsin D is recruited to phagosomes, it is not pro
26                                        Human procathepsin D was expressed in a baculovirus system to
27  mediated through coassociation of VKORC1v2, procathepsin D, and vIL-6 with components of the ER-asso
28  ER-transiting, preproteolytically processed procathepsin D.
29 and lysosomal targeting of newly synthesized procathepsin D.
30                Regulation of human and mouse procathepsin E gene expression was shown not to be influ
31                 Thus the extent to which the procathepsin E gene is expressed in a particular cell ty
32                              Quantitation of procathepsin E mRNA by LightCyclertrade mark technology
33                               [Ser139,Ala163]Procathepsin K (containing mutation C139S,S163A) failed
34    We have determined the structure of human procathepsin K at 2.8 A resolution.
35                             The structure of procathepsin K contributes to an understanding of the mo
36                               [Ser139,Ala163]Procathepsin K could be fully processed to mature enzyme
37 yme by including one equivalent of wild-type procathepsin K in the activation mixture.
38        It is presumed that the activation of procathepsin K in vivo occurs in the bone resorption pit
39                The fold of the propeptide of procathepsin K is similar to that observed in procatheps
40                                     Although procathepsin K is stable and readily detected, the activ
41 structure of the mature enzyme domain within procathepsin K is virtually identical to that of mature
42           Spontaneous in vitro activation of procathepsin K occurred at pH 4 and was catalyzed by exo
43 ts indicated that in vitro activation of the procathepsin K was an autocatalytic process.
44 tures secreted mature cathepsin K as well as procathepsin K, and expressed active cathepsin K in cyto
45 ween the propeptide and the mature enzyme of procathepsin K.
46 tion of a C-terminal epitope tag sequence to procathepsin L also induced misfolding of the proenzyme,
47 at several locations on the surface of mouse procathepsin L and modeling oligosaccharide conformation
48                            Whereas wild-type procathepsin L and mutants bearing carbohydrate at Asn-1
49 biting sequence near the N terminus of mouse procathepsin L can result in glycosylation of a normally
50  and transport kinetics of recombinant human procathepsin L containing one, two, or three glycosylati
51 refore conclude that the carboxy terminus of procathepsin L contains a sequence essential for its sec
52 gged protein did not compete with endogenous procathepsin L for targeting to lysosomes.
53     High-level transient expression of human procathepsin L in mouse NIH 3T3 cells results in the sec
54       At the same time, the endogenous mouse procathepsin L in these nontransformed cells is found in
55 uration was not associated with mutations in procathepsin L mRNA, was not complemented by procathepsi
56                                      But the procathepsin L mutant having phenylalanine in place of T
57 procathepsin L mRNA, was not complemented by procathepsin L overexpression, and did not affect the ma
58                    After several hours, much procathepsin L remains as precursor in a compartment tha
59  may have identified a recognition domain in procathepsin L that is important for its interactions wi
60                       Misfolded mutant mouse procathepsin L was not efficiently targeted to lysosomes
61              Similarly, epitope-tagged mouse procathepsin L was not targeted to lysosomes in homologo
62                             Mutants of human procathepsin L with carboxy-terminus deletions involving
63 gnals (Asn-X-Ser/Thr) into the cDNA of human procathepsin L, a lysosomal acid protease.
64 amino acids Tyr-Asn allowed secretion of the procathepsin L, but the replacement of these two amino a
65 dent lysine-based phosphorylation signals on procathepsin L, which account for the low level of phosp
66 milar treatment did not affect processing of procathepsin L.
67  models, we have compared the itineraries of procathepsins L and B, two closely related members of th
68  report that the expression and secretion of procathepsin-L (pCTS-L) was induced by serum amyloid A (
69             TNF-alpha increased secretion of procathepsin S, but did not affect TIMP-1 and reduced TI
70                                  Recombinant procathepsin V is autocatalytically activated at acidic