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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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“Intrinsically disordered proteins are abundant in nature and responsible for a plethora of cellular functions (Dunker et al., 2002; Habchi et al., 2014).”
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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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