The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
The Structural Basis for Control of Eukaryotic Protein Kinases
Open accessAbstract
Eukaryotic protein kinases are key regulators of cell processes. Comparison of the structures of protein kinase domains, both alone and in complexes, allows generalizations to be made about the mechanisms that regulate protein kinase activation. Protein kinases in the active state adopt a catalytically competent conformation upon binding of both the ATP and peptide substrates that has led to an understanding of the catalytic mechanism. Docking sites remote from the catalytic site are a key feature of several substrate recognition complexes. Mechanisms for kinase activation through phosphorylation, additional domains or subunits, by scaffolding proteins and by kinase dimerization are discussed.
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Cites
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Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
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Structural insights into BMP receptors: Specificity, activation and inhibition
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Metadata
- Authors
- Endicott, J. A., Noble, M. E. M., & Johnson, L. N.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2012-07-07
- Volume
- 81
- Issue
- 1
- Pages
- 587-613
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2159765576
- Cited by
- 427
- References
- 13
- FWCI
- 2.37
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
