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Intrinsic Disorder and Protein Function
Abstract
0196237 to Z.O. and A.K.D and by NIH-1R01-LM06916 to A.K.D. and Z.O. Key words: native protein, random coil, molten globule, intrinsic disorder, protein structurefunction, genomics, proteomics, and bioinformatics Abbreviations: circular dichroism (CD), limited proteolysis (LP), nuclear magnetic resonance
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“Many IDPs/IDRs are capable of at least partial ordering upon interaction with specific partners [7–18].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [9]
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“The interest in understanding the functions of intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs), such as the UD of SFKs, has exploded in recent years as the sheer abundance and relevance of IDPs and IDRs in the eukaryotic proteome has become apparent (Dunker et al., 2002; Wright and…”
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Intrinsic Disorder and Prote in Modifications: Building an SVM Predictor for Methylation
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Self-citationControl of DNA Damage Bypass by Ubiquitylation of PCNA
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Order, Disorder, and Flexibility
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Metadata
- Authors
- Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z.
- Affiliations
- Washington State University (US)
- School of Molecular Biosciences, Washington State University, Pullman, Washington 99164 and Center for Information Science and Technology, Temple University, Philadelphia, Pennsylvania 19122
- Corresponding author
- Dunker, A. Keith
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-05-01
- Volume
- 41
- Issue
- 21
- Pages
- 6573-6582
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2073745520
- Cited by
- 1,731
- References
- 89
- Citations by year
- 2026: 16 · 2025: 33 · 2024: 40 · 2023: 39 · 2022: 64 · 2021: 52 · 2020: 70 · 2019: 71 · 2018: 60 · 2017: 69 · 2016: 89 · 2015: 78 · 2014: 97 · 2013: 96 · 2012: 109
- FWCI
- 25.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. National Library of Medicine (1R01-LM06916, R01LM006916)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- intrinsic disorder, protein function, random coil, molten globule, protein structure-function relationship, native proteins, limited proteolysis, circular dichroism, nuclear magnetic resonance
- MeSH terms
- Apoproteins, Cytochrome c Group, DNA Helicases, Glycoproteins, Proteins, Structure-Activity Relationship, Molecular Structure, Protein Folding, Molecular Chaperones, Computational Biology, Cytochromes c, Clusterin
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