The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.
Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications
Open accessAbstract
Post-translational modifications (PTMs) produce significant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes. PTMs can induce a range of effects, from local stabilization or destabilization of transient secondary structure to global disorder-to-order transitions, potentially driving complete state changes between intrinsically disordered and folded states or dispersed monomeric and phase-separated states. Here, we discuss diverse biological processes that are dependent on PTM regulation of IDPs. We also present recent tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanisms.
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Metadata
- Authors
- Bah, A., & Forman-Kay, J. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-03
- Volume
- 291
- Issue
- 13
- Pages
- 6696-6705
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2300545781
- Cited by
- 566
- References
- 95
- FWCI
- 20.62
- Type
- journal article
- Language
- en
- Open access
- hybrid
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