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1 und to the glycosaminoglycan (GAG) chains of serglycin.
2 fects of proteases that are complex-bound to serglycin.
3 ked to the chondroitin-sulfate proteoglycan, serglycin.
4 d with the chondroitin-sulfate proteoglycan, serglycin.
5 nogen activator was distributed similarly to serglycin.
10 lacking mouse mast cell protease 6, a major serglycin-associated protease, exhibited similar defects
11 e mast cells underwent apoptotic cell death, serglycin(-/-) cells died predominantly by necrosis.
12 similar defects in apoptosis as observed in serglycin(-/-) cells, indicating that the pro-apoptotic
13 Targets exposed to double-labeled granzyme B-serglycin complexes show solely the uptake of granzyme B
14 molecular interaction of secreted granzyme B-serglycin complexes with target cells remains undefined.
18 the first intron may be related to the high serglycin expression in HL60 relative to HEL or CHRF cel
23 e DNase I-hypersensitive sites (DHSS) of the serglycin gene in resting and phorbol 12-myristate 13-ac
25 ry identified (i) the 25-kDa core protein as serglycin, (ii) the 90-kDa core protein as inter-alpha-i
26 vide direct evidence for a critical role for serglycin in MM pathogenesis and show that targeting ser
28 learn whether the physiologic effector, GrB-serglycin, initiates apoptosis primarily through caspase
30 ndicating that the pro-apoptotic function of serglycin is due to downstream effects of proteases that
31 smembrane domain, flow cytometry showed that serglycin is present on the MM cell surface, and attachm
34 LP2 and IalphaIHC2 with macrophages, whereas serglycin localizes to the underlying glycosaminoglycan-
35 ve high homology with the orthologous murine serglycin locus and are rich in potential transcription
36 e cytosol and that the necrotic phenotype of serglycin(-/-) mast cells was linked to defective degrad
40 n in MM pathogenesis and show that targeting serglycin may provide a novel therapeutic approach for M
42 how the interaction of granzyme B (GrB) with serglycin might influence the apoptotic potential of thi
47 tain regulatory sequences derived from human serglycin, preproapolipoprotein C II, and Egr1 genes.
49 om participating in extracellular processes, serglycin proteoglycan and one of its associated proteas
50 including a single consensus sequence of the serglycin proteoglycan core protein bound heparin strong
55 low mMCP-9 to form multimeric complexes with serglycin proteoglycans and other negatively charged pro
56 Cs) can reversibly alter their expression of serglycin proteoglycans and the homologous granule chyma
57 diators such as bioactive amines, cytokines, serglycin proteoglycans with negatively charged glycosam
58 anule mediators (e.g., neutral proteases and serglycin proteoglycans) and proinflammatory cytokines (
61 s multimeric complexes with the proteoglycan serglycin (SG) in cytotoxic granules, and cytotoxic cell
64 A granule-associated proteoglycan, namely serglycin, that contains chondroitin 4-sulfate (CS) glyc
66 monstrates the exchange of the granzyme from serglycin to immobilized, sulfated glycosaminoglycans.
68 teolysis through a secretory granule-derived serglycin-tryptase axis as a novel principle for histone
69 reover, it was shown that the absence of the serglycin-tryptase axis resulted in altered chromatin co
71 A core protein of the appropriate size for serglycin was detected by analysis of the chondroitinase
72 CD44 is the cell surface-binding partner for serglycin, which therefore may serve as a major ligand f
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