The DOI matches its Crossref record; 438 of the 439 references it cites were found in a registry or an index.
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Abstract
Regulation, recognition and cell signaling involve the coordinated actions of many players. To achieve this coordination, each participant must have a valid identification (ID) that is easily recognized by the others. For proteins, these IDs are often within intrinsically disordered (also ID) regions. The functions of a set of well-characterized ID regions from a diversity of proteins are presented herein to support this view. These examples include both more recently described signaling proteins, such as p53, alpha-synuclein, HMGA, the Rieske protein, estrogen receptor alpha, chaperones, GCN4, Arf, Hdm2, FlgM, measles virus nucleoprotein, RNase E, glycogen synthase kinase 3beta, p21(Waf1/Cip1/Sdi1), caldesmon, calmodulin, BRCA1 and several other intriguing proteins, as well as historical prototypes for signaling, regulation, control and molecular recognition, such as the lac repressor, the voltage gated potassium channel, RNA polymerase and the S15 peptide associating with the RNA polymerase S-protein. The frequent occurrence and the common use of ID regions in important protein functions raise the possibility that the relationship between amino acid sequence, disordered ensemble and function might be the dominant paradigm for the molecular recognition that serves as the basis for signaling and regulation by protein molecules.
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“Collectively, these abilities clearly indicate that the activity of ERs relies on intrinsic disorder [17].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [17]
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Cited by
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Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept
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Self-citation
Metadata
- Authors
- Uversky, V. N., Oldfield, C. J., & Dunker, A. K.
- Affiliations
- Russian Academy of Sciences (RU)
- Molecular Kinetics (United States) (US)
- Corresponding author
- Uversky, Vladimir N.
- Venue
- Journal of Molecular Recognition
- Publisher
- Wiley
- Published
- 2005
- Volume
- 18
- Issue
- 5
- Pages
- 343-384
- ISSN
- 0952-3499 (ISSN-L)
- 1099-1352
- OpenAlex
- W2162720882
- Cited by
- 847
- References
- 439
- Citations by year
- 2026: 15 · 2025: 14 · 2024: 23 · 2023: 28 · 2022: 31 · 2021: 27 · 2020: 37 · 2019: 48 · 2018: 33 · 2017: 46 · 2016: 38 · 2015: 47 · 2014: 53 · 2013: 55 · 2012: 56
- FWCI
- 3.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Recognition (publishedVersion)
- PubMed (publishedVersion)
- Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
- Funders
- U.S. National Library of Medicine (R01LM007688, 1 R01 LM007688-0A1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- intrinsically disordered regions, protein recognition, signal transduction, protein regulation, molecular recognition, p53, alpha-synuclein, HMGA, estrogen receptor alpha, molecular chaperones, GCN4, ARF, MDM2, measles virus nucleoprotein, RNase E, glycogen synthase kinase-3β, p21, caldesmon, calmodulin, BRCA1, lac repressor, voltage-gated potassium channels, RNA polymerase, S protein, sequence-function relationships
- MeSH terms
- Animals, Antigens, Humans, Nucleic Acids, Protein Conformation, Proteins, Signal Transduction, Protein Folding, Molecular Chaperones
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