Src regulated by C-terminal phosphorylation is monomeric - Wikidata - wikimedia - TriplyDB

Src regulated by C-terminal phosphorylation is monomeric

Src regulated by C-terminal phosphorylation is monomeric

http://www.wikidata.org/entity/Q36102407

about

Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering.The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src.Developmentally regulated dual-specificity kinase from peanut that is induced by abiotic stresses.Quadrupole time-of-flight versus triple-quadrupole mass spectrometry for the determination of phosphopeptides by precursor ion scanning.The role of collagen in thrombosis and hemostasis.Junctional adhesion molecule-A suppresses platelet integrin αIIbβ3 signaling by recruiting Csk to the integrin-c-Src complex.An intramolecular association between two domains of the protein kinase Fused is necessary for Hedgehog signaling.Mutational analysis of stress-responsive peanut dual specificity protein kinase. Identification of tyrosine residues involved in regulation of protein kinase activity.

P2860

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P2860

Src regulated by C-terminal phosphorylation is monomeric

http://www.wikidata.org/entity/Q36102407

description

1997 nî lūn-bûn

@nan

1997年の論文

@ja

1997年論文

@yue

1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

1997年论文

@zh

1997年论文

@zh-cn

name

Src regulated by C-terminal phosphorylation is monomeric

@ast

Src regulated by C-terminal phosphorylation is monomeric

@en

type

label

Src regulated by C-terminal phosphorylation is monomeric

@ast

Src regulated by C-terminal phosphorylation is monomeric

@en

prefLabel

Src regulated by C-terminal phosphorylation is monomeric

@ast

Src regulated by C-terminal phosphorylation is monomeric

@en

P1433

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Src regulated by C-terminal phosphorylation is monomeric

@en

P2093

A Weijland

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

G Neubauer

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

J C Williams

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

R K Wierenga

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

S A Courtneidge

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

P2860

Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src

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

c-Abl kinase regulates the protein binding activity of c-Crk

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Structure of the regulatory domains of the Src-family tyrosine kinase Lck

Protein modules and signalling networks

SH2 domains recognize specific phosphopeptide sequences

Sequence requirements for binding of Src family tyrosine kinases to activated growth factor receptors

Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling

P304

3590-3595

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P31

scholarly article

P356

10.1073/PNAS.94.8.3590

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P407

P433

8

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P478

94

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P50

Giulio Superti-Furga

P577

1997-04-01T00:00:00Z

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P5875

14109821

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P698

9108021

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P921

phosphorylation

P932

20484

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