The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Multisite protein phosphorylation – from molecular mechanisms to kinetic models
Abstract
Multisite phosphorylation is an important mechanism for fine‐tuned regulation of protein function. Mathematical models developed over recent years have contributed to elucidation of the functional consequences of a variety of molecular mechanisms involved in processing of the phosphorylation sites. Here we review the results of such models, together with salient experimental findings on multisite protein phosphorylation. We discuss how molecular mechanisms that can be distinguished with respect to the order and processivity of phosphorylation, as well as other factors, regulate changes in the sensitivity and kinetics of the response, the synchronization of molecular events, signalling specificity, and other functional implications.
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Cites
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Cited by
Prabakaran, S., Lippens, G., Steen, H., & Gunawardena, J. (2012) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1185 · Cited by 335
Gli Protein Activity Is Controlled by Multisite Phosphorylation in Vertebrate Hedgehog Signaling
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Protein phosphorylation in neurodegeneration: friend or foe?
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Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates
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Neuropharmacological Effects of Quercetin: A Literature-Based Review
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Kinact: a computational approach for predicting activating missense mutations in protein kinases
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Metadata
- Authors
- Salazar, C., & Höfer, T.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2009-05-21
- Volume
- 276
- Issue
- 12
- Pages
- 3177-3198
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1975507400
- Cited by
- 258
- References
- 7
- FWCI
- 6.24
- Type
- journal article
- Language
- en
- Open access
- closed
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