IRS pleckstrin homology domains bind to acidic motifs in proteins.
about
Cloning and characterization of PHIP, a novel insulin receptor substrate-1 pleckstrin homology domain interacting proteinThe PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding moduleSignal-dependent membrane targeting by pleckstrin homology (PH) domainsDifferential binding to and regulation of JAK2 by the SH2 domain and N-terminal region of SH2-bbetaDiacylglycerol kinase delta suppresses ER-to-Golgi traffic via its SAM and PH domainsCrystal structure of the pleckstrin homology-phosphotyrosine binding (PH-PTB) targeting region of insulin receptor substrate 1Insulin receptor substrate 4 associates with the protein IRASRegulation of insulin receptor substrate 1 pleckstrin homology domain by protein kinase C: role of serine 24 phosphorylationSignal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activityPhosphorylation 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 inSpecificity 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 cancerIRS2 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 factorThe 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.
P2860
Q24290359-B1303AE5-761F-43D8-BFC3-7600F36FDBD8Q24314777-99628657-2BB5-4753-82EB-571E213530E0Q24532099-0AF88604-3C6E-4833-82D8-8E7C890332B0Q24554240-04267B18-F4CB-4EF7-9578-4A776DA41BBDQ24555039-B81359CE-9D8C-4DE0-8D24-CF09D5FFA177Q27619068-CE29FF58-C9EB-47FE-9200-85C9277C6E33Q28209890-DB5C7836-242B-42E6-98B9-8FD231D17C96Q28581138-AAA52526-E6F7-43AD-8AB0-058282790018Q30476276-702D46F8-1521-4D80-A705-6592332AE1B4Q31162696-0427441E-F489-468E-A766-AD4E6B5DE65EQ34402004-E88CA516-879B-477F-A177-009AE1EBA6F1Q34926469-2111B3F6-FE85-42D3-994F-8485C1B76424Q35172911-78416EB1-0F18-445D-9359-2C6D0911AD50Q35743146-2B59FDAE-035C-4805-9A97-93CA11096C8EQ36508636-26D024F7-75EA-436F-AA39-44BA616B111BQ36602630-B8225CF1-675A-4260-AAA7-70169FD01AC2Q36994832-EC86E40A-5B79-4522-9F93-43F2711B6BD8Q37594442-B61C824A-45F7-4472-9932-BA952E0A609AQ37715179-2EEDD965-C332-476C-8455-A78B74E04EBAQ37997745-518FFCC7-15E2-4793-BAEC-24AD115CFFD7Q38247021-B11303DC-760F-4E80-B69A-7127094BDC45Q38321378-41E697B0-9E27-4BF8-A11C-5129CA44836AQ38913862-C523D926-E5A0-4D7B-BE1B-0C21943621E3Q40190294-84FAE28D-965A-4573-9246-E79E92139210Q40725478-BE8DC6EF-8441-40E2-B279-0204DD39F5D6Q40757512-6A3EA1D2-64EA-4FA1-A7A4-5BCA9B44E2E3Q40769994-70C99584-F922-4162-938A-D99576CE6728Q42829419-FD400F7B-CB09-4FF7-897E-05F459B492E3Q42832843-0D386852-A9BF-4C6E-8014-D7096EDE84E1Q44119094-E44EDC0F-3EFD-4E5F-99C9-F9D012FAC00CQ46756214-31778736-8A69-4DF2-A77D-3446BD92E7EAQ50282571-F0F617EA-617D-435F-92F7-B90CFB9CB933
P2860
IRS pleckstrin homology domains bind to acidic motifs in proteins.
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
@ja
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
P2093
P2860
P356
P1476
IRS pleckstrin homology domains bind to acidic motifs in proteins.
@en
P2093
Ishibashi O
P2860
P304
31061-31067
P356
10.1074/JBC.273.47.31061
P407
P577
1998-11-01T00:00:00Z