The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Native State Proline Isomerization: An Intrinsic Molecular Switch
Abstract
Exquisite control of biological function is achieved via tight regulation of the catalytic and binding activities of cellular proteins. The mechanistic details of protein regulation vary from targeted chemical modification of amino acid side chains (1) to the quite drastic global unfolding of an entire polypeptide chain (2). Peptidyl prolyl cis/trans isomerization is emerging as a potentially general mechanism for the control of protein function (3). While most structures of native, folded proteins reveal peptidyl-prolyl imide bonds that adopt either the cis or trans conformation, there are a growing number of folded proteins that exhibit conformational heterogeneity about one or more peptidyl-prolyl bonds. Unlike covalent modification or global unfolding, proline isomerization is an intrinsic conformational exchange process that has the potential to direct ligand recognition and to control protein activity within the confines of the native state.
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Cites
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Self-citation
Cited by
The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682
Folding versus aggregation: Polypeptide conformations on competing pathways
Jahn, T. R., & Radford, S. E. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.05.015 · Cited by 428
Histones: At the Crossroads of Peptide and Protein Chemistry
Müller, M. M., & Muir, T. W. (2015) · Chemical Reviews · doi:10.1021/cr5003529 · Cited by 247
Bedir, M., Outwin, E., Colnaghi, R., Bassett, L., Abramowicz, I., & O’Driscoll, M. (2024) · EMBO Reports · doi:10.1038/s44319-024-00184-9 · Cited by 6
Metadata
- Authors
- Andreotti, A. H.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-07-24
- Volume
- 42
- Issue
- 32
- Pages
- 9515-9524
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2057451487
- Cited by
- 270
- References
- 17
- FWCI
- 4.29
- Type
- journal article
- Language
- en
- Open access
- closed
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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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