Binding of a diphosphorylated-ITAM peptide to spleen tyrosine kinase (Syk) induces distal conformational changes: a hydrogen exchange mass spectrometry study.
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3D structure of Syk kinase determined by single-particle electron microscopyBiophysical and mechanistic insights into novel allosteric inhibitor of spleen tyrosine kinase.Integration of phosphoproteomic, chemical, and biological strategies for the functional analysis of targeted protein phosphorylation.DNA as a molecular ruler: interrogation of a tandem SH2 domain with self-assembled, bivalent DNA-peptide complexes.Human spleen tyrosine kinase (Syk) recombinant expression systems for high-throughput assays.Protein flexibility and ligand rigidity: a thermodynamic and kinetic study of ITAM-based ligand binding to Syk tandem SH2.
P2860
Binding of a diphosphorylated-ITAM peptide to spleen tyrosine kinase (Syk) induces distal conformational changes: a hydrogen exchange mass spectrometry study.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
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2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Binding of a diphosphorylated- ...... hange mass spectrometry study.
@ast
Binding of a diphosphorylated- ...... hange mass spectrometry study.
@en
type
label
Binding of a diphosphorylated- ...... hange mass spectrometry study.
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Binding of a diphosphorylated- ...... hange mass spectrometry study.
@en
prefLabel
Binding of a diphosphorylated- ...... hange mass spectrometry study.
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Binding of a diphosphorylated- ...... hange mass spectrometry study.
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P2860
P50
P1476
Binding of a diphosphorylated- ...... change mass spectrometry study
@en
P2093
M Isabel Catalina
Marcel J E Fischer
P2860
P2888
P304
P356
10.1016/J.JASMS.2005.02.011
P577
2005-07-01T00:00:00Z
P5875
P6179
1035180067