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Transitions to catalytically inactive conformations in EGFR kinase

Transitions to catalytically inactive conformations in EGFR kinase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1348165425

Transitions to catalytically inactive conformations in EGFR kinase

About this item

Full title

Transitions to catalytically inactive conformations in EGFR kinase

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2013-04, Vol.110 (18), p.7270-7275

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

The epidermal growth factor receptor (EGFR) is a key protein in cellular signaling, and its kinase domain (EGFR kinase) is an intensely pursued target of small-molecule drugs. Although both catalytically active and inactive conformations of EGFR kinase have been resolved crystallographically, experimental characterization of the transitions between...

Alternative Titles

Full title

Transitions to catalytically inactive conformations in EGFR kinase

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_1348165425

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1348165425

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1220843110

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