Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein.
about
Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.Interaction in vitro of the product of the c-Crk-II proto-oncogene with the insulin-like growth factor I receptorInsulin regulates the dynamic balance between Ras and Rap1 signaling by coordinating the assembly states of the Grb2-SOS and CrkII-C3G complexes.Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling.Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contextsThe Role of Crk Adaptor Proteins in T-Cell Adhesion and MigrationThe adaptor protein Crk in immune responseStructural basis for regulation of the Crk signaling protein by a proline switch.Domain organization differences explain Bcr-Abl's preference for CrkL over CrkIISequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinaseRegulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptorPhosphorylation of CrkII adaptor protein at tyrosine 221 by epidermal growth factor receptorXB130: A novel adaptor protein in cancer signal transductionPhosphorylation of c-Crk II on the negative regulatory Tyr222 mediates nerve growth factor-induced cell spreading and morphogenesisRole of CrkII Signaling in RANKL-Induced Osteoclast Differentiation and Function.Cyclophilin A promotes cell migration via the Abl-Crk signaling pathway.Iterative tyrosine phosphorylation controls non-canonical domain utilization in Crk.Models of crk adaptor proteins in cancer.Commentary: The carboxyl-terminal Crk SH3 domain: Regulatory strategies and new perspectives.Functional mechanisms and roles of adaptor proteins in abl-regulated cytoskeletal actin dynamics.Phosphorylation of Crk on tyrosine 251 in the RT loop of the SH3C domain promotes Abl kinase transactivationScintillation proximity assay (SPA) technology to study biomolecular interactions.Proline cis-trans isomerization controls autoinhibition of a signaling protein.Transactivation of Abl by the Crk II adapter protein requires a PNAY sequence in the Crk C-terminal SH3 domain.T cell activation induces direct binding of the Crk adapter protein to the regulatory subunit of phosphatidylinositol 3-kinase (p85) via a complex mechanism involving the Cbl protein.Crk family adaptor proteins trans-activate c-Abl kinase.Activation of the focal adhesion kinase signaling pathway by structural alterations in the carboxyl-terminal region of c-Crk II.c-Crk, a substrate of the insulin-like growth factor-1 receptor tyrosine kinase, functions as an early signal mediator in the adipocyte differentiation process.The kinase-deficient Src acts as a suppressor of the Abl kinase for Cbl phosphorylationInvolvement of the adapter protein CRKL in integrin-mediated adhesion.Structural requirements for function of the Crkl adapter protein in fibroblasts and hematopoietic cells.A potential SH3 domain-binding site in the Crk SH2 domain.Abelson tyrosine kinase facilitates Salmonella enterica serovar Typhimurium entry into epithelial cells.Abl tyrosine kinase promotes dorsal ruffles but restrains lamellipodia extension during cell spreading on fibronectin.Integrin-mediated mechanotransduction pathway of low-intensity continuous ultrasound in human chondrocytesThe non-receptor tyrosine kinase Lyn controls neutrophil adhesion by recruiting the CrkL-C3G complex and activating Rap1 at the leading edgeReal-time fluorescent resonance energy transfer analysis to monitor drug resistance in chronic myelogenous leukemia.Molecular dynamics of the proline switch and its role in Crk signaling.Crk is required for apoptosis in Xenopus egg extracts.Biosensor architectures for high-fidelity reporting of cellular signaling.
P2860
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P2860
Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein.
description
1995 nî lūn-bûn
@nan
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Direct demonstration of an int ...... nteraction in the Crk protein.
@ast
Direct demonstration of an int ...... nteraction in the Crk protein.
@en
type
label
Direct demonstration of an int ...... nteraction in the Crk protein.
@ast
Direct demonstration of an int ...... nteraction in the Crk protein.
@en
prefLabel
Direct demonstration of an int ...... nteraction in the Crk protein.
@ast
Direct demonstration of an int ...... nteraction in the Crk protein.
@en
P2093
P356
P1433
P1476
Direct demonstration of an int ...... nteraction in the Crk protein.
@en
P2093
P2888
P304
P356
10.1038/374477A0
P407
P577
1995-03-01T00:00:00Z
P6179
1027028319