Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing - Test2 - elhamkhani - TriplyDB

Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing

Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing

http://www.wikidata.org/entity/Q24676734

about

Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control The conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase mu The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)Dynamic interaction of PTPmu with multiple cadherins in vivo Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.Furin-, ADAM 10-, and gamma-secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of beta-catenin's transcriptional activity Protein tyrosine phosphatases expression during development of mouse superior colliculus Tumor-derived extracellular fragments of receptor protein tyrosine phosphatases (RPTPs) as cancer molecular diagnostic tools alpha-Latrotoxin and its receptors Insecticidal toxins from black widow spider venom BCCIP associates with the receptor protein tyrosine phosphatase PTPmu Protein tyrosine phosphatase kappa and SHP-1 are involved in the regulation of cell-cell contacts at adherens junctions in the exocrine pancreas PTPmu regulates N-cadherin-dependent neurite outgrowth Receptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates the catenin p120(ctn)The transmembrane protein tyrosine phosphatase RPTPsigma modulates signaling of the epidermal growth factor receptor in A431 cells Receptor protein tyrosine phosphatases in nervous system development 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 Modulation of the proteoglycan receptor PTPσ promotes recovery after spinal cord injury Comparative study of protein tyrosine phosphatase-epsilon isoforms: membrane localization confers specificity in cellular signalling Contact inhibition of hepatocyte growth regulated by functional association of the c-Met/hepatocyte growth factor receptor and LAR protein-tyrosine phosphatase LAR receptor protein tyrosine phosphatases in the development and maintenance of excitatory synapses Protein Tyrosine Phosphatase PTPRS Is an Inhibitory Receptor on Human and Murine Plasmacytoid Dendritic Cells Receptor protein tyrosine phosphatase sigma regulates synapse structure, function and plasticity Identification of PTPsigma as an autophagic phosphatase.Macroarray analysis of coelomocyte gene expression in response to LPS in the sea urchin. Identification of unexpected immune diversity in an invertebrate.Mitochondrial uncoupler exerts a synthetic lethal effect against β-catenin mutant tumor cells Receptor protein tyrosine phosphatases are novel components of a polycystin complex The role of a LAR-like receptor tyrosine phosphatase in growth cone collapse and mutual-avoidance by sibling processes.Functional significance of the LAR receptor protein tyrosine phosphatase family in development and diseases.Coordinated action of protein tyrosine phosphatases in insulin signal transduction.Structural basis for extracellular cis and trans RPTPσ signal competition in synaptogenesis.Transmodulation of cell surface regulatory molecules via ectodomain shedding.Identification of protein tyrosine phosphatase receptor gamma extracellular domain (sPTPRG) as a natural soluble protein in plasma.The receptor tyrosine phosphatase Lar regulates adhesion between Drosophila male germline stem cells and the niche Regulation of adherens junction dynamics by phosphorylation switches.Shedding of TNFR1 in regenerative liver can be induced with TNF alpha and PMA SheddomeDB: the ectodomain shedding database for membrane-bound shed markers.

P2860

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P2860

Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing

http://www.wikidata.org/entity/Q24676734

description

1997 nî lūn-bûn

@nan

1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

1997年の論文

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1997年論文

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1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

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1997年論文

@zh-tw

1997年论文

@wuu

name

Cellular redistribution of pro ...... ducible proteolytic processing

@ast

Cellular redistribution of pro ...... ducible proteolytic processing

@en

Cellular redistribution of pro ...... ducible proteolytic processing

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type

label

Cellular redistribution of pro ...... ducible proteolytic processing

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Cellular redistribution of pro ...... ducible proteolytic processing

@en

Cellular redistribution of pro ...... ducible proteolytic processing

@nl

prefLabel

Cellular redistribution of pro ...... ducible proteolytic processing

@ast

Cellular redistribution of pro ...... ducible proteolytic processing

@en

Cellular redistribution of pro ...... ducible proteolytic processing

@nl

P1433

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P1433

Journal of Cell Biology

P1476

Cellular redistribution of pro ...... ducible proteolytic processing

@en

P2093

A Ullrich

http://www.w3.org/2001/XMLSchema#string

B Aicher

http://www.w3.org/2001/XMLSchema#string

J Schilling

http://www.w3.org/2001/XMLSchema#string

M M Lerch

http://www.w3.org/2001/XMLSchema#string

T Müller

http://www.w3.org/2001/XMLSchema#string

P2860

A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen

Structural diversity and evolution of human receptor-like protein tyrosine phosphatases

Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase

Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family

The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1

Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase

Molecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoforms

Association of human protein-tyrosine phosphatase kappa with members of the armadillo family

The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions

Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density

P304

681-96

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scholarly article

P356

10.1083/JCB.138.3.681

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P407

P433

3

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P478

138

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P577

1997-08-11T00:00:00Z

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P5875

13973720

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P698

9245795

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P921

P932

2141638

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