Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL. (Q44373949)

2 December 2017

title

Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL. (English)

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2 December 2017

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3

George Q Daley

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2 December 2017

Mohammad Azam

1

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2 December 2017

Robert R Latek

series ordinal

2

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2 December 2017

publication date

1 March 2003

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2 December 2017

language of work or name

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2 December 2017

volume

112

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2 December 2017

issue

6

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2 December 2017

page(s)

831-843

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An intramolecular SH3-domain interaction regulates c-Abl activity

2 December 2017

cites work

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High frequency of point mutations clustered within the adenosine triphosphate-binding region of BCR/ABL in patients with chronic myeloid leukemia or Ph-positive acute lymphoblastic leukemia who develop imatinib (STI571) resistance

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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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Ph(+) acute lymphoblastic leukemia resistant to the tyrosine kinase inhibitor STI571 has a unique BCR-ABL gene mutation

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Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia

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

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Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation

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7 January 2021

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Identifiers

DOI

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2 December 2017

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