An intramolecular SH3-domain interaction regulates c-Abl activity (Q30176270)

9 June 2017

title

An intramolecular SH3-domain interaction regulates c-Abl activity (English)

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9 June 2017

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9 June 2017

Barilá D

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9 June 2017

language of work or name

English

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publication date

1 March 1998

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9 June 2017

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9 June 2017

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9 June 2017

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9 June 2017

page(s)

280-282

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Activation of the c-Abl tyrosine kinase in the stress response to DMA-damaging agents

9 June 2017

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c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein

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Abl tyrosine kinase in signal transduction and cell-cycle regulation

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Deletion of an N-terminal regulatory domain of the c-abl tyrosine kinase activates its oncogenic potential

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Evidence for regulation of the human ABL tyrosine kinase by a cellular inhibitor

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Structure-function relationships in Src family and related protein tyrosine kinases

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

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Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel p130Cas-related protein, Sin.

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Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity

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Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity

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The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity

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7 January 2021

Identifiers

DOI

10.1038/NG0398-280

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9 June 2017

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