Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.
about
N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21Crystal Structure and Autoactivation Pathway of the Precursor Form of Human Tripeptidyl-peptidase 1, the Enzyme Deficient in Late Infantile Ceroid LipofuscinosisNovel interactions of CLN5 support molecular networking between Neuronal Ceroid Lipofuscinosis proteinsInteractions of the proteins of neuronal ceroid lipofuscinosis: clues to functionA critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosisAlterations in ROS activity and lysosomal pH account for distinct patterns of macroautophagy in LINCL and JNCL fibroblasts.The genetic spectrum of human neuronal ceroid-lipofuscinoses.The intracellular location and function of proteins of neuronal ceroid lipofuscinoses.Proteolytic processing of the neuronal ceroid lipofuscinosis related lysosomal protein CLN5.Tripeptidyl-peptidase I in health and disease.Lysosomal serine protease CLN2 regulates tumor necrosis factor-alpha-mediated apoptosis in a Bid-dependent mannerGlycoMine(struct): a new bioinformatics tool for highly accurate mapping of the human N-linked and O-linked glycoproteomes by incorporating structural features.Analysis of NCL Proteins from an Evolutionary Standpoint.Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses.N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.Propeptides as modulators of functional activity of proteases.Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme.Mannose 6-phosphorylated proteins are required for tumor necrosis factor-induced apoptosis: defective response in I-cell disease fibroblasts.Maturation of human tripeptidyl-peptidase I in vitro.Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I.A zebrafish model of CLN2 disease is deficient in tripeptidyl peptidase 1 and displays progressive neurodegeneration accompanied by a reduction in proliferation.A proteomic network approach across the ALS-FTD disease spectrum resolves clinical phenotypes and genetic vulnerability in human brain.
P2860
Q24308161-4976DF87-BD22-44FD-A841-E0C3C9C70B22Q27653009-E4EA493B-9BA4-4A25-9F3B-84EE476CCAF6Q28115540-1489A541-26B6-44A3-8BC7-2BB75E333095Q28289653-85154C44-7C38-475B-BB85-1F50FCCD416DQ28475003-70CA8085-4CB3-4475-B662-0FFE0E817DFEQ31110961-F5D6694D-F19C-480D-B4B1-5C1DD9F61AD8Q34302797-2A5293C6-2DB4-4B4C-B050-8634ACFAD354Q35681065-20D8FFF8-A945-48B9-8865-618D10FCC203Q36109195-D89A46CD-14C0-423D-A985-6D02EAE8DBD9Q36559721-7CE3A307-16A4-44A8-BD65-81632EE2406AQ37160925-7699100F-9C85-4E3D-88CF-C6B009EFE3E8Q37314730-8414E724-8806-4B6E-A395-54B6DD0C19CAQ37480758-11004D2B-5C89-4E27-A715-6ED8217E3420Q37944570-BACA6192-B7C1-442C-9A6E-14D3274D6198Q38346370-FA2DFF5D-17EB-46B0-88C9-F8FE9ECC59F0Q38472448-478463AD-A0F3-40A9-8ACD-3E875F7C344CQ39026265-D948994F-0AB1-4BEC-9AF1-3203D10586EBQ40510257-D2C9811F-DE50-4107-BA29-E7B2D793EF3EQ44895882-F9B5A178-2616-4B29-A7BF-D549FE78B30DQ45176585-4DF1EB10-93F3-4C4A-9E96-DBCC4E974CF1Q45284367-CED38549-5962-4440-831C-921209F1D16CQ47073900-F81C6AA7-050E-4726-8F48-12F5A5B2978EQ47344945-8394CCE7-F793-41B8-B0F4-7296EAAC0AFF
P2860
Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Biosynthesis, glycosylation, a ...... human tripeptidyl-peptidase I.
@en
type
label
Biosynthesis, glycosylation, a ...... human tripeptidyl-peptidase I.
@en
prefLabel
Biosynthesis, glycosylation, a ...... human tripeptidyl-peptidase I.
@en
P2093
P2860
P356
P1476
Biosynthesis, glycosylation, a ...... human tripeptidyl-peptidase I.
@en
P2093
Adam A Golabek
Elizabeth Kida
Krystyna E Wisniewski
Marius Walus
Pankaj Mehta
Peter Wujek
P2860
P304
P356
10.1074/JBC.M211872200
P407
P577
2002-12-17T00:00:00Z