Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets. - Wikidata - wikimedia - TriplyDB

Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets.

Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets.

http://www.wikidata.org/entity/Q30157893

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DOC2B acts as a calcium switch and enhances vesicle fusion ER-bound protein tyrosine phosphatase PTP1B interacts with Src at the plasma membrane/substrate interface Association of Lyn kinase with membrane rafts determines its negative influence on LPS-induced signaling SH3 domain of c-Src governs its dynamics at focal adhesions and the cell membrane.Role of Src kinases in mobilization of glycosylphosphatidylinositol-anchored decay-accelerating factor by Dr fimbria-positive adhering bacteria.Roles for SH2 and SH3 domains in Lyn kinase association with activated FcepsilonRI in RBL mast cells revealed by patterned surface analysis.Microtubule-mediated Src tyrosine kinase trafficking in neuronal growth cones.A role for the juxtamembrane cytoplasm in the molecular dynamics of focal adhesions The reactive oxygen species-Src-Stat3 pathway provokes negative feedback inhibition of apoptosis induced by high-fluence low-power laser irradiation.C-Src and c-Yes are two unlikely partners of spermatogenesis and their roles in blood-testis barrier dynamics.Accurate quantification of diffusion and binding kinetics of non-integral membrane proteins by FRAP.Myristoylation and membrane binding regulate c-Src stability and kinase activity Src mediates cigarette smoke-induced resistance to tyrosine kinase inhibitors in NSCLC cells SH2 Ligand-Like Effects of Second Cytosolic Domain of Na/K-ATPase α1 Subunit on Src Kinase.Focal adhesion kinase-dependent focal adhesion recruitment of SH2 domains directs SRC into focal adhesions to regulate cell adhesion and migration Src-mediated caveolin-1 phosphorylation affects the targeting of active Src to specific membrane sites.The residue at position 5 of the N-terminal region of Src and Fyn modulates their myristoylation, palmitoylation, and membrane interactions.Coated pit-mediated endocytosis of the type I transforming growth factor-β (TGF-β) receptor depends on a di-leucine family signal and is not required for signaling.Protein Interaction and Na/K-ATPase-Mediated Signal Transduction.Presenilin 1 affects focal adhesion site formation and cell force generation via c-Src transcriptional and posttranslational regulation.Molecular aspects of the interaction between Mason-Pfizer monkey virus matrix protein and artificial phospholipid membrane.p63 drives invasion in keratinocytes expressing HPV16 E6/E7 genes through regulation of Src-FAK signalling.Lateral dynamics of proteins with polybasic domain on anionic membranes: a dynamic Monte-Carlo study.Differential regulation of phospholipase C-beta2 activity and membrane interaction by Galphaq, Gbeta1gamma2, and Rac2.Live Cell Imaging of Src/FAK Signaling by FRET.Na/K-ATPase Y260 Phosphorylation-mediated Src Regulation in Control of Aerobic Glycolysis and Tumor Growth

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P2860

Src kinase activity and SH2 domain regulate the dynamics of Src association with lipid and protein targets.

http://www.wikidata.org/entity/Q30157893

description

2007 nî lūn-bûn

@nan

2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Src kinase activity and SH2 do ...... ith lipid and protein targets.

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Src kinase activity and SH2 do ...... ith lipid and protein targets.

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type

label

Src kinase activity and SH2 do ...... ith lipid and protein targets.

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Src kinase activity and SH2 do ...... ith lipid and protein targets.

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prefLabel

Src kinase activity and SH2 do ...... ith lipid and protein targets.

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Src kinase activity and SH2 do ...... ith lipid and protein targets.

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P1433

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P1433

Journal of Cell Biology

P1476

Src kinase activity and SH2 do ...... ith lipid and protein targets.

@en

P2093

G Steven Martin

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

John C Donaldson

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

Orit Gutman

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

Yoav I Henis

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

P2860

Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1

Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal

Newest findings on the oldest oncogene; how activated src does it

Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae

SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange

Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions

Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure

High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides

Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase

P304

675-686

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scholarly article

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10.1083/JCB.200701133

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4

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178

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Dmitry Shvartsman

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2007-08-01T00:00:00Z

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6140266

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17698610

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2064473

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