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Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer

Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5307475

Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer

About this item

Full title

Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2017-02, Vol.114 (6), p.E931-E940

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

The expertise of protein kinases lies in their dynamic structure, wherein they are able to modulate cellular signaling by their phosphotransferase activity. Only a few hundreds of protein kinases regulate key processes in human cells, and protein kinases play a pivotal role in health and disease. The present study dwells on understanding the workin...

Alternative Titles

Full title

Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5307475

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5307475

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1620667114

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