Multimerization of the protein-tyrosine phosphatase (PTP)-like insulin-dependent diabetes mellitus autoantigens IA-2 and IA-2beta with receptor PTPs (RPTPs). Inhibition of RPTPalpha enzymatic activity
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Structure of the mature ectodomain of the human receptor-type protein-tyrosine phosphatase IA-2Large-scale structural analysis of the classical human protein tyrosine phosphatomeStructural genomics of protein phosphatasesX-ray structure of the mature ectodomain of phogrinDimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilonRegulation of insulin granule turnover in pancreatic beta-cells by cleaved ICA512.Interface analysis of the complex between ERK2 and PTP-SLThe dense core transmembrane vesicle protein IA-2 is a regulator of vesicle number and insulin secretion.Protein-protein interactions in crystals of the human receptor-type protein tyrosine phosphatase ICA512 ectodomain.IA-2beta, but not IA-2, is induced by ghrelin and inhibits glucose-stimulated insulin secretion.Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome"IA-2 modulates dopamine secretion in PC12 cells.Protein tyrosine phosphatases: functional inferences from mouse models and human diseases.Gene silencing of phogrin unveils its essential role in glucose-responsive pancreatic beta-cell growthPathophysiologic changes in IA-2/IA-2β null mice are secondary to alterations in the secretion of hormones and neurotransmitters.Luminal interaction of phogrin with carboxypeptidase E for effective targeting to secretory granules.An extended tyrosine-targeting motif for endocytosis and recycling of the dense-core vesicle membrane protein phogrin.Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum.Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms.Mild impairment of motor nerve repair in mice lacking PTP-BL tyrosine phosphatase activity.Both Intrinsic Substrate Preference and Network Context Contribute to Substrate Selection of Classical Tyrosine Phosphatases.
P2860
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P2860
Multimerization of the protein-tyrosine phosphatase (PTP)-like insulin-dependent diabetes mellitus autoantigens IA-2 and IA-2beta with receptor PTPs (RPTPs). Inhibition of RPTPalpha enzymatic activity
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@ast
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@en
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@nl
type
label
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@ast
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@en
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@nl
prefLabel
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@ast
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@en
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@nl
P2093
P2860
P921
P356
P1476
Multimerization of the protein ...... f RPTPalpha enzymatic activity
@en
P2093
Christophe Blanchetot
Jan Schepens
Jeroen den Hertog
Reiner Lammers
Sabrina Albet
Steffen Gross
P2860
P304
48139-48145
P356
10.1074/JBC.M208228200
P407
P577
2002-10-02T00:00:00Z