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Kinase activation through dimerization by human SH2-B

Kinase activation through dimerization by human SH2-B

http://www.wikidata.org/entity/Q24519086

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Molecular basis of signaling specificity of insulin and IGF receptors: neglected corners and recent advances Recent advances in understanding leptin signaling and leptin resistance Regulation of insulin and type 1 insulin-like growth factor signaling and action by the Grb10/14 and SH2B1/B2 adaptor proteins The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14 Chromosome 16p11.2 deletions: another piece in the genetic puzzle of childhood obesity A bipolar clamp mechanism for activation of Jak-family protein tyrosine kinases SH2B1 regulation of energy balance, body weight, and glucose metabolism.The adaptor protein SH2B3 (Lnk) negatively regulates neurite outgrowth of PC12 cells and cortical neurons.Functional characterization of obesity-associated variants involving the α and β isoforms of human SH2B1 Critical role of the Src homology 2 (SH2) domain of neuronal SH2B1 in the regulation of body weight and glucose homeostasis in mice.LNK (SH2B3): paradoxical effects in ovarian cancer.Identification of SH2B2beta as an inhibitor for SH2B1- and SH2B2alpha-promoted Janus kinase-2 activation and insulin signaling Phosphorylation controls a dual-function polybasic nuclear localization sequence in the adapter protein SH2B1β to regulate its cellular function and distribution Adapter protein SH2B1beta binds filamin A to regulate prolactin-dependent cytoskeletal reorganization and cell motility.Phosphorylation of Y372 is critical for Jak2 tyrosine kinase activation Identification of SH2B1β as a focal adhesion protein that regulates focal adhesion size and number.Neuronal SH2B1 is essential for controlling energy and glucose homeostasis.The SH2B1 adaptor protein associates with a proximal region of the erythropoietin receptor.The role of Janus kinases in haemopoiesis and haematological malignancy.Identification of steroid-sensitive gene-1/Ccdc80 as a JAK2-binding protein.JAK2 mutants (e.g., JAK2V617F) and their importance as drug targets in myeloproliferative neoplasms Lnk inhibits myeloproliferative disorder-associated JAK2 mutant, JAK2V617F Adapter protein SH2B1beta cross-links actin filaments and regulates actin cytoskeleton SH2B1 enhances insulin sensitivity by both stimulating the insulin receptor and inhibiting tyrosine dephosphorylation of insulin receptor substrate proteins.The Lnk adaptor protein: a key regulator of normal and pathological hematopoiesis.Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.Binding of SH2-B family members within a potential negative regulatory region maintains JAK2 in an active state The role of LNK/SH2B3 genetic alterations in myeloproliferative neoplasms and other hematological disorders.SH2B1 is critical for the regulation of cardiac remodelling in response to pressure overload.SH2B1--the adaptor protein that could.Gender-specific transcriptomic response to environmental exposure in Flemish adults.Diversity in peptide recognition by the SH2 domain of SH2B1.SH2B binds JAK2 Phosphorylated LEP:LEPR:JAK2 Binds SH2B1 The effect of maternal care on gene expression and DNA methylation in a subsocial bee

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P2860

Kinase activation through dimerization by human SH2-B

http://www.wikidata.org/entity/Q24519086

description

2005 nî lūn-bûn

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2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2005 թվականի ապրիլին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Kinase activation through dimerization by human SH2-B

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Kinase activation through dimerization by human SH2-B

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Kinase activation through dimerization by human SH2-B

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Kinase activation through dimerization by human SH2-B

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type

label

Kinase activation through dimerization by human SH2-B

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Kinase activation through dimerization by human SH2-B

@en

Kinase activation through dimerization by human SH2-B

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Kinase activation through dimerization by human SH2-B

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prefLabel

Kinase activation through dimerization by human SH2-B

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Kinase activation through dimerization by human SH2-B

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Kinase activation through dimerization by human SH2-B

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Kinase activation through dimerization by human SH2-B

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MCB.25.7.2607-2621.2005

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Molecular and Cellular Biology

P1476

Kinase activation through dimerization by human SH2-B

@en

P2093

Eric D Werner

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

J Daniel Frantz

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

Jongsoon Lee

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Lone Hansen

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

Masahiro Nishi

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

Steven E Shoelson

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

P2860

APS, an adaptor protein containing PH and SH2 domains, is associated with the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis

APS, an adaptor protein containing Pleckstrin homology (PH) and Src homology-2 (SH2) domains inhibits the JAK-STAT pathway in collaboration with c-Cbl

PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis

Inhibition of SH2 domain/phosphoprotein association by a nonhydrolyzable phosphonopeptide

Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1

Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor

Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2

SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase

SH2-B is required for both male and female reproduction

APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes

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2607-21

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scholarly article

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10.1128/MCB.25.7.2607-2621.2005

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P433

7

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25

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Sirano Dhe-Paganon

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2005-04-01T00:00:00Z

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15767667

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1061652

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