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Phosphorylation and structure-based functional studies reveal a positive and a negative role for the...

Phosphorylation and structure-based functional studies reveal a positive and a negative role for the...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_18248468

Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase

About this item

Full title

Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase

Publisher

Basingstoke: Nature Publishing

Journal title

Oncogene, 2001-12, Vol.20 (56), p.8075-8084

Language

English

Formats

Publication information

Publisher

Basingstoke: Nature Publishing

More information

Scope and Contents

Contents

c-Abl is a nuclear and cytoplasmic tyrosine kinase involved in a variety of cellular growth and differentiation processes. In contrast to its oncogenic counterparts, like BCR-Abl, c-Abl is not constitutively tyrosine phosphorylated and its catalytic activity is very low. Here we report tyrosine phosphorylation of endogenous c-Abl and a concomitant...

Alternative Titles

Full title

Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_18248468

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_18248468

Other Identifiers

ISSN

0950-9232

E-ISSN

1476-5594

DOI

10.1038/sj.onc.1205017

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