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Receptor protein tyrosine phosphatases are novel components of a polycystin complex

Receptor protein tyrosine phosphatases are novel components of a polycystin complex

http://www.wikidata.org/entity/Q33761927

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A polycystin-centric view of cyst formation and disease: the polycystins revisited OFD1 and flotillins are integral components of a ciliary signaling protein complex organized by polycystins in renal epithelia and odontoblasts The cleaved cytoplasmic tail of polycystin-1 regulates Src-dependent STAT3 activation.Protein phosphatase-1α interacts with and dephosphorylates polycystin-1 A telomerase immortalized human proximal tubule cell line with a truncation mutation (Q4004X) in polycystin-1 Regulation of ciliary motility: conserved protein kinases and phosphatases are targeted and anchored in the ciliary axoneme Identification of protein tyrosine phosphatase receptor gamma extracellular domain (sPTPRG) as a natural soluble protein in plasma.Mutational and functional analysis of the tumor-suppressor PTPRD in human melanoma.Tolvaptan inhibits ERK-dependent cell proliferation, Cl⁻ secretion, and in vitro cyst growth of human ADPKD cells stimulated by vasopressin The extracellular matrix and ciliary signaling Polycystins and partners: proposed role in mechanosensitivity.Therapeutic targets for polycystic kidney disease.

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P2860

Receptor protein tyrosine phosphatases are novel components of a polycystin complex

http://www.wikidata.org/entity/Q33761927

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Receptor protein tyrosine phosphatases are novel components of a polycystin complex

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Receptor protein tyrosine phosphatases are novel components of a polycystin complex

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Receptor protein tyrosine phosphatases are novel components of a polycystin complex

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Receptor protein tyrosine phosphatases are novel components of a polycystin complex

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prefLabel

Receptor protein tyrosine phosphatases are novel components of a polycystin complex

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Receptor protein tyrosine phosphatases are novel components of a polycystin complex

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J.BBADIS.2010.11.006

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Biochimica et Biophysica Acta

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Receptor protein tyrosine phosphatases are novel components of a polycystin complex

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P2093

Andrew Needham

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

Angela Wandinger-Ness

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Catherine A Boucher

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Christopher Ward

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Deborah Hyink

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Elsa Romero

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Heather H Ward

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Katie S Thurston

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Patricia D Wilson

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Richard N Sandford

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P2860

Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene

Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress

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

Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases

PKD1 interacts with PKD2 through a probable coiled-coil domain

The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with multiple cell recognition domains

The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma

The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease.

Furin-, ADAM 10-, and gamma-secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of beta-catenin's transcriptional activity

A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila

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1225-1238

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scholarly article

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10.1016/J.BBADIS.2010.11.006

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