The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Allostery: an illustrated definition for the ‘second secret of life’
Open accessAbstract
Although allosteric regulation is the ‘second secret of life’, the molecular mechanisms that give rise to allostery currently elude understanding. In my opinion, experimental progress is hampered by a commonly used but misleading definition of allostery as protein structural changes that are elicited by the binding of a single ligand. Allostery is more strictly defined in functional terms as a comparison of how one ligand binds in the absence, versus the presence, of a second ligand. Therefore, as each of the two binding events involves two protein complexes, a study of allostery must consider four complexes and not just two. Such a comparison can distinguish allosteric from non-allosteric protein changes, the importance of which is frequently overlooked. When a study of all four complexes is not feasible, an alternative, albeit limited, strategy can identify subsets of allosteric-specific changes.
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Cites
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Cited by
The ensemble nature of allostery
Motlagh, H. N., Wrabl, J. O., Li, J., & Hilser, V. J. (2014) · Nature · doi:10.1038/nature13001 · Cited by 1,247
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A Unified View of “How Allostery Works”
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Novel Allosteric Modulators of G Protein-coupled Receptors
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ASD v3.0: unraveling allosteric regulation with structural mechanisms and biological networks
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Metadata
- Authors
- Fenton, A. W.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 33
- Issue
- 9
- Pages
- 420-425
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2124676068
- Cited by
- 320
- References
- 36
- FWCI
- 0.86
- 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).
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