Sequence specificity of SHP-1 and SHP-2 Src homology 2 domains. Critical roles of residues beyond the pY+3 position.
about
Simultaneous Binding of Two Peptidyl Ligands by a Src Homology 2 DomainDissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domainsThe language of SH2 domain interactions defines phosphotyrosine-mediated signal transductionSHP-1 and SHP-2 in T cells: two phosphatases functioning at many levelsCompletion of proteomic data sets by Kd measurement using cell-free synthesis of site-specifically labeled proteins.Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft.Defining SH2 domain and PTP specificity by screening combinatorial peptide libraries.Reverse interactomics: decoding protein-protein interactions with combinatorial peptide libraries.On-bead screening of combinatorial libraries: reduction of nonspecific binding by decreasing surface ligand density.Three New Humulane Sesquiterpenes from Cultures of the Fungus Antrodiella albocinnamomea.Regulation of hematopoietic cell function by inhibitory immunoglobulin G receptors and their inositol lipid phosphatase effectors.Targeting protein tyrosine phosphatases for anticancer drug discovery.Signalling by protein phosphatases and drug development: a systems-centred view.Protein tyrosine phosphatases: regulatory mechanisms.Identification of small molecular weight inhibitors of Src homology 2 domain-containing tyrosine phosphatase 2 (SHP-2) via in silico database screening combined with experimental assay.An Efficient Semi-supervised Learning Approach to Predict SH2 Domain Mediated Interactions.Probing SH2-domains using Inhibitor Affinity Purification (IAP).The Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor contains an immunoreceptor tyrosine-based inhibitory motif that activates Shp2.Modulation of SHP-1 phosphatase activity by monovalent and bivalent SH2 phosphopeptide ligands.Two new ylangene-type sesquiterpenoids from cultures of the fungus Postia sp.
P2860
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P2860
Sequence specificity of SHP-1 and SHP-2 Src homology 2 domains. Critical roles of residues beyond the pY+3 position.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2006年の論文
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2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Sequence specificity of SHP-1 ...... dues beyond the pY+3 position.
@ast
Sequence specificity of SHP-1 ...... dues beyond the pY+3 position.
@en
type
label
Sequence specificity of SHP-1 ...... dues beyond the pY+3 position.
@ast
Sequence specificity of SHP-1 ...... dues beyond the pY+3 position.
@en
prefLabel
Sequence specificity of SHP-1 ...... dues beyond the pY+3 position.
@ast
Sequence specificity of SHP-1 ...... dues beyond the pY+3 position.
@en
P2093
P2860
P356
P1476
Sequence specificity of SHP-1 ...... dues beyond the pY+3 position.
@en
P2093
Andreas May
Anne-Sophie Wavreille
Susheela Tridandapani
P2860
P304
20271-20282
P356
10.1074/JBC.M601047200
P407
P577
2006-05-15T00:00:00Z