Conformational rearrangements upon Syk auto-phosphorylation. - Wikidata - wikimedia - TriplyDB

Conformational rearrangements upon Syk auto-phosphorylation.

Conformational rearrangements upon Syk auto-phosphorylation.

http://www.wikidata.org/entity/Q30490298

about

Serine phosphorylation by SYK is critical for nuclear localization and transcription factor function of Ikaros Biophysical and mechanistic insights into novel allosteric inhibitor of spleen tyrosine kinase.Therapeutic prospect of Syk inhibitors.Autoinhibition and adapter function of Syk.Phosphorylation impact on Spleen Tyrosine kinase conformation by Surface Enhanced Raman Spectroscopy.Molecular mechanism of selective recruitment of Syk kinases by the membrane antigen-receptor complex.Human spleen tyrosine kinase (Syk) recombinant expression systems for high-throughput assays.Differential mast cell outcomes are sensitive to FcεRI-Syk binding kinetics.SYK autophosphorylates

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P2860

Conformational rearrangements upon Syk auto-phosphorylation.

http://www.wikidata.org/entity/Q30490298

description

2009 nî lūn-bûn

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2009 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2009 թվականի մայիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Conformational rearrangements upon Syk auto-phosphorylation.

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Conformational rearrangements upon Syk auto-phosphorylation.

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type

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Conformational rearrangements upon Syk auto-phosphorylation.

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Conformational rearrangements upon Syk auto-phosphorylation.

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prefLabel

Conformational rearrangements upon Syk auto-phosphorylation.

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Conformational rearrangements upon Syk auto-phosphorylation.

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J.BBAPAP.2009.04.010

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Biochimica et Biophysica Acta

P1476

Conformational rearrangements upon Syk auto-phosphorylation.

@en

P2093

Ernesto Arias-Palomo

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

María A Recuero-Checa

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P2860

The Syk tyrosine kinase suppresses malignant growth of human breast cancer cells

Molecular mechanism of the Syk activation switch

Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide

3D structure of Syk kinase determined by single-particle electron microscopy

Crystal structures of c-Src reveal features of its autoinhibitory mechanism

Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem

Structural basis for the inhibition of tyrosine kinase activity of ZAP-70

UCSF Chimera--a visualization system for exploratory research and analysis

EMAN: semiautomated software for high-resolution single-particle reconstructions

Relocation of Syk protein-tyrosine kinase to the actin filament network and subsequent association with Fak

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1211-1217

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scholarly article

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10.1016/J.BBAPAP.2009.04.010

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8

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1794

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Xosé R. Bustelo

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2009-05-03T00:00:00Z

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24396330

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19409513

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phosphorylation

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2746503

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