Intrinsic Disorder and Protein Function

Dunker, A. Keith; Brown, Celeste J.; Lawson, J. David; Iakoucheva, Lilia M.; Obradović, Zoran

doi:10.1021/bi012159+

Cited by 1,731Protein Structure and DynamicsEnzyme Structure and FunctionProtein Interaction Studies and Fluorescence Analysis

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Intrinsic Disorder and Protein Function

Dunker, A. Keith, Brown, Celeste J., Lawson, J. David, Iakoucheva, Lilia M., Obradović, Zoran·2002·Biochemistry

DOI 10.1021/bi012159+

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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.
“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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Functional anthology of intrinsic disorder. III. Ligands, postranslational modifications and diseases associated with long disordered regions
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Self-citation

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
ORCID: Dunker, A. Keith
Brown, Celeste J.
Lawson, J. David
Iakoucheva, Lilia M.
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
DOI: 10.1021/bi012159+
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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Intrinsic Disorder and Protein Function

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