Structural basis for the autoinhibition of c-Abl tyrosine kinase (Q27640773)

8

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Klaus Scheffzek

4

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Oliver Hantschel

2

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Matthew Young

object named as

Matthew A Young

3

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author name string

Bhushan Nagar

1

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Darren Veach

5

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William Bornmann

6

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Bayard Clarkson

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

7

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language of work or name

English

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publication date

21 March 2003

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published in

Cell

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volume

112

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issue

6

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page(s)

859-71

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cites work

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c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines

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A myristoyl/phosphotyrosine switch regulates c-Abl

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The conformational plasticity of protein kinases

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Modular peptide recognition domains in eukaryotic signaling

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En bloc substitution of the Src homology region 2 domain activates the transforming potential of the c-Abl protein tyrosine kinase

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Autoinhibition of c-Abl

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Disabling Abl-perspectives on Abl kinase regulation and cancer therapeutics

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Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor

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Structural mechanism for STI-571 inhibition of abelson tyrosine kinase

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The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions

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

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