The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity
about
The Fyn-ADAP Axis: Cytotoxicity Versus Cytokine Production in Killer CellsThe role of the Src homology 3-Src homology 2 interface in the regulation of Src kinasesThe solution structure and intramolecular associations of the Tec kinase SRC homology 3 domainTwo Closely Spaced Tyrosines Regulate NFAT Signaling in B Cells via Syk Association with VavSuperbinder SH2 domains act as antagonists of cell signalingAlternative splicing modulates autoinhibition and SH3 accessibility in the Src kinase Fyn.Quantifying information transfer by protein domains: analysis of the Fyn SH2 domain structureCoevolution of the domains of cytoplasmic tyrosine kinases.SH2 and PTB domains in tyrosine kinase signaling.The autoimmunity-associated BLK haplotype exhibits cis-regulatory effects on mRNA and protein expression that are prominently observed in B cells early in development.Epstein-Barr virus latent membrane protein 2A preferentially signals through the Src family kinase LynAffinity modulation of small-molecule ligands by borrowing endogenous protein surfacesStructural insights into the intertwined dimer of fyn SH2The energetics of phosphate binding to a protein complex.Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.Probing the nature of interactions in SH2 binding interfaces--evidence from electrospray ionization mass spectrometryAdhesion and degranulation promoting adapter protein (ADAP) is a central hub for phosphotyrosine-mediated interactions in T cells.1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.Creation of Phosphotyrosine Superbinders by Directed Evolution of an SH2 Domain.Targeting Lyn tyrosine kinase through protein fusions encompassing motifs of Cbp (Csk-binding protein) and the SOCS box of SOCS1.
P2860
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P2860
The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity
description
1997 nî lūn-bûn
@nan
1997 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
The SH2 domain from the tyrosi ...... bility and binding specificity
@ast
The SH2 domain from the tyrosi ...... bility and binding specificity
@en
The SH2 domain from the tyrosi ...... bility and binding specificity
@nl
type
label
The SH2 domain from the tyrosi ...... bility and binding specificity
@ast
The SH2 domain from the tyrosi ...... bility and binding specificity
@en
The SH2 domain from the tyrosi ...... bility and binding specificity
@nl
prefLabel
The SH2 domain from the tyrosi ...... bility and binding specificity
@ast
The SH2 domain from the tyrosi ...... bility and binding specificity
@en
The SH2 domain from the tyrosi ...... bility and binding specificity
@nl
P2093
P1433
P1476
The SH2 domain from the tyrosi ...... bility and binding specificity
@en
P2093
P304
P356
10.1016/S0969-2126(97)00283-9
P577
1997-10-15T00:00:00Z