IRS pleckstrin homology domains bind to acidic motifs in proteins. - Wikidata - wikimedia - TriplyDB

IRS pleckstrin homology domains bind to acidic motifs in proteins.

IRS pleckstrin homology domains bind to acidic motifs in proteins.

http://www.wikidata.org/entity/Q33289377

about

Cloning and characterization of PHIP, a novel insulin receptor substrate-1 pleckstrin homology domain interacting protein The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module Signal-dependent membrane targeting by pleckstrin homology (PH) domains Differential binding to and regulation of JAK2 by the SH2 domain and N-terminal region of SH2-bbeta Diacylglycerol kinase delta suppresses ER-to-Golgi traffic via its SAM and PH domains Crystal structure of the pleckstrin homology-phosphotyrosine binding (PH-PTB) targeting region of insulin receptor substrate 1 Insulin receptor substrate 4 associates with the protein IRAS Regulation of insulin receptor substrate 1 pleckstrin homology domain by protein kinase C: role of serine 24 phosphorylation Signal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activity Phosphorylation of Ser24 in the pleckstrin homology domain of insulin receptor substrate-1 by Mouse Pelle-like kinase/interleukin-1 receptor-associated kinase: cross-talk between inflammatory signaling and insulin signaling that may contribute to in Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein co-operative mechanism.Membrane targeting of Grb2-associated binder-1 (Gab1) scaffolding protein through Src myristoylation sequence substitutes for Gab1 pleckstrin homology domain and switches an epidermal growth factor response to an invasive morphogenic program.ClipR-59 interacts with Elmo2 and modulates myoblast fusion.Apoptosis defects and chemotherapy resistance: molecular interaction maps and networks.Interplay between αvβ3 integrin and nucleolin regulates human endothelial and glioma cell migration.Regulating insulin signaling and beta-cell function through IRS proteins.An alignment-free domain architecture similarity search (ADASS) algorithm for inferring homology between multi-domain proteins.Irs2 and Irs4 synergize in non-LepRb neurons to control energy balance and glucose homeostasis.Insulin signaling meets mitochondria in metabolism.Nuclear IRS-1 and cancer IRS2 integrates insulin/IGF1 signalling with metabolism, neurodegeneration and longevity.Phosphotyrosine protein of molecular mass 30 kDa binds specifically to the positively charged region of the pleckstrin N-terminal pleckstrin homology domain.Receptor protein tyrosine phosphatase beta/zeta is a functional binding partner for vascular endothelial growth factor The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing.Nuclear translocation of insulin receptor substrate-1 by the simian virus 40 T antigen and the activated type 1 insulin-like growth factor receptor.Specificity of interleukin-2 receptor gamma chain superfamily cytokines is mediated by insulin receptor substrate-dependent pathway.Acidic motif responsible for plasma membrane association of the voltage-dependent calcium channel beta1b subunit.Insulin induces suppressor of cytokine signaling-3 tyrosine phosphorylation through janus-activated kinase.The insulin receptor substrate (IRS)-1 pleckstrin homology domain functions in downstream signaling.Nuclear translocation of insulin receptor substrate-1 by oncogenes and Igf-I. Effect on ribosomal RNA synthesis.Involvement of insulin-like growth factor-insulin receptor signal pathway in the transgenic mouse model of medulloblastoma.Analysis of insulin receptor substrate signaling dynamics on microstructured surfaces.

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P2860

IRS pleckstrin homology domains bind to acidic motifs in proteins.

http://www.wikidata.org/entity/Q33289377

description

1998 nî lūn-bûn

@nan

1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

1998年の論文

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1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@ast

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@en

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@nl

type

label

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@ast

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@en

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@nl

prefLabel

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@ast

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@en

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@nl

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Journal of Biological Chemistry

P1476

IRS pleckstrin homology domains bind to acidic motifs in proteins.

@en

P2093

Burks DJ

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

Ishibashi O

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

Lowe D

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

Riedel H

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

Towery H

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

Wang J

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White MF

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P2860

Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain

Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor

Disruption of IRS-2 causes type 2 diabetes in mice

A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease

Phosphorylation and activation of p70s6k by PDK1

Characterization of an interaction between insulin receptor substrate 1 and the insulin receptor by using the two-hybrid system

Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin

Solution structure of a pleckstrin-homology domain

The solution structure of the pleckstrin homology domain of mouse Son-of-sevenless 1 (mSos1)

Protein modules and signalling networks

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31061-31067

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10.1074/JBC.273.47.31061

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47

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273

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9813005

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