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Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTPathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human DiseasesVladimir N. Uversky*†‡§, Vrushank Davé∥⊥, Lilia M. Iakoucheva#, Prerna Malaney∥, Steven J. Metallo▽, Ravi Ramesh Pathak∥, and Andreas C. Joerger*▲View Author Information∥ †Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute and ∥Department of Pathology and Cell Biology, Morsani College of Medicine, University of South Florida, Tampa, Florida 33612, United States‡ Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia§ Department of Biological Sciences, Faculty of Science, King Abdulaziz University, Jeddah 22254, Saudi Arabia⊥ Department of Molecular Oncology, H. Lee Moffitt Cancer Center and Research Institute, Tampa, Florida 33612, United States# Department of Psychiatry, University of California San Diego, La Jolla, California 92093, United States▽ Department of Chemistry, Georgetown University, Washington, District of Columbia 20057, United States▲ Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom*Phone 1-813-974-5816; fax 1-813-974-7357; e-mail [email protected]*Phone +44-1223-267290; e-mail [email protected]Cite this: Chem. Rev. 2014, 114, 13, 6844–6879Publication Date (Web):May 15, 2014Publication History Received15 December 2013Published online15 May 2014Published inissue 9 July 2014https://pubs.acs.org/doi/10.1021/cr400713rhttps://doi.org/10.1021/cr400713rreview-articleACS PublicationsCopyright © 2014 American Chemical SocietyRequest reuse permissionsArticle Views3882Altmetric-Citations215LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Cancer,Diseases and disorders,Genetics,Peptides and proteins,Post-translational modification Get e-Alerts
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“Therefore, IDPs have also become the focus of studies of molecular mechanisms of amyloid aggregation, characterized by conformational transitions from intrinsic disorder in the soluble monomeric/oligomeric form to ordered self-assembled amyloid fibrils of the same proteins.262–263”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [263]
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Cites
MUSCLE: multiple sequence alignment with high accuracy and high throughput
Edgar, R. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh340 · Cited by 44,662
A method and server for predicting damaging missense mutations.
Adzhubei, I. A., Schmidt, S., Peshkin, L., Ramensky, V. E., Gerasimova, A., Bork, P., Kondrashov, A. S., & Sunyaev, S. R. (2010) · Nature Methods · doi:10.1038/nmeth0410-248 · Cited by 13,194
Jalview Version 2—a multiple sequence alignment editor and analysis workbench
Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M. E., & Barton, G. J. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp033 · Cited by 10,349
Kumar, P., Henikoff, S., & Ng, P. C. (2009) · Nature Protocols · doi:10.1038/nprot.2009.86 · Cited by 6,521
Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138
Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2
Amir, R. E., Van den Veyver, I. B., Wan, M., Tran, C. Q., Francke, U., & Zoghbi, H. Y. (1999) · Nature Genetics · doi:10.1038/13810 · Cited by 4,990
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Dang, C. V. (2012) · Cell · doi:10.1016/j.cell.2012.03.003 · Cited by 3,390
Goh, K.-I., Cusick, M. E., Valle, D., Childs, B., Vidal, M., & Barabási, A.-L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701361104 · Cited by 3,242
Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
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2 of the 379 references couldn’t be matched to a known paper.
Research works printed but not linked: 13
- Dunker A. K., 2000, Genome Inf. Ser., 11, 161
- Sette C., 2013, Int. J. Cell. Biol., 458727
- Wang J. Z., 2013, J. Alzheimer’s Dis., 33, S123
- Li S., 2010, Pac. Symp. Biocomput., 337
- Tan C. S., 2009, Sci. Signal., 2, ra39
- Uversky V. N., 2012, eLS (Encyclopedia of Life Sciences)
- Meek D. W., 2009, Cold Spring Harbor Perspect. Biol., 1, a000950
- Andreeva A., 2012, Methods Mol. Biol., 857, 1
- Chang Y. S., 2013, Proc. Natl. Acad. Sci. U.S.A., 110, E3445
- Fata J. E., 2012, Int. J. Cell. Biol., 2012, 379685
- Singh G., 2011, Curr. Cancer Drug Targets, 11, 536, 10.2174/156800911795655930 · DOI
- Fry D. C., 2013, Med. Chem. Lett., 4, 95
- Yuan, X.; Cai, C.; Chen, S.; Chen, S.; Yu, Z.; Bal, S. P.Oncogene 2013, in press
Cited by
Sorted by citations
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Uversky, V. N. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.10.015 · Cited by 707
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Self-citationWei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions
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Metadata
- Authors
- Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C.
- Affiliations
- Russian Academy of Sciences (RU)
- Moffitt Cancer Center (US)
- University of California San Diego (US)
- University of South Florida (US)
- Georgetown University (US)
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Uversky, Vladimir N.
- Joerger, Andreas C.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-05-15
- Volume
- 114
- Issue
- 13
- Pages
- 6844-6879
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- PMC
- PMC4100540
- OpenAlex
- W2086189298
- Cited by
- 288
- References
- 379
- Citations by year
- 2026: 13 · 2025: 24 · 2024: 16 · 2023: 21 · 2022: 20 · 2021: 13 · 2020: 30 · 2019: 31 · 2018: 26 · 2017: 26 · 2016: 37 · 2015: 24 · 2014: 7
- FWCI
- 2.98
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Chemical Reviews (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
- Funders
- National Cancer Institute (P50CA119997)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- intrinsically disordered proteins, protein misfolding, protein aggregation, human disease, neurodegenerative diseases, protein structure-function relationship
- MeSH terms
- Disease, Humans, Mutation, Protein Unfolding, Intrinsically Disordered Proteins
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