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Short Communication Section: Biochemistry

The Intrinsically Disordered Protein: A Literature Landscape

Author(s): Mouna Choura*, Faiçal Brini and Ahmed Rebaï

Volume 2, Issue 3, 2022

Published on: 28 March, 2022

Page: [183 - 188] Pages: 6

DOI: 10.2174/2210298102666220307111220

Abstract

Background: Intrinsically disordered proteins (IDPs) are proteins that lack a predetermined 3D structure and play key cellular functions. IDPs are often involved in diseases and have been shown to be attractive targets for drug development. The IDPs have been intensively investigated, revealing important results.

Objective: This study aimed to evaluate the latest research bibliography since 2010, including the latest findings, major contributors, institutions, and journals.

Methods: The bibliographic data were retrieved from PubMed from 2010 to 2020. The data collected were then analysed by VOSviewer software (version 1.6.11).

Results: In this study, 4590 publications were retrieved for analysis. They have been published in 579 journals. Over 9683 organisations have contributed to IDP publications, with United States of America and Russia being in the first place. Human proteins are most studied for their IDP features and mainly in the context of diseases and drug design.

Conclusion: This bibliometric study reveals that the trend of publications is increasing year by year. USA and Russia have contributed the most to the IDP research field. Moreover, it suggests that IDP research remains a challenging issue that is still open for original contributions and original applications.

Keywords: Bibliometric, bibliography, intrinsically disordered proteins, organisations, 3D structures, drug development, proteins.

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Graphical Abstract

[1]
Uversky, V.N.; Dunker, A.K. Understanding protein non-folding. Biochim. Biophys. Acta, 2010, 1804(6), 1231-1264.
[http://dx.doi.org/10.1016/j.bbapap.2010.01.017] [PMID: 20117254]
[2]
Tompa, P. Unstructural biology coming of age. Curr. Opin. Struct. Biol., 2011, 21(3), 419-425.
[http://dx.doi.org/10.1016/j.sbi.2011.03.012] [PMID: 21514142]
[3]
Uversky, V.N.; Davé, V.; Iakoucheva, L.M.; Malaney, P.; Metallo, S.J.; Pathak, R.R.; Joerger, A.C. Pathological unfoldomics of uncon-trolled chaos: Intrinsically disordered proteins and human diseases. Chem. Rev., 2014, 114(13), 6844-6879.
[http://dx.doi.org/10.1021/cr400713r] [PMID: 24830552]
[4]
Uversky, V.N.; Oldfield, C.J.; Dunker, A.K. Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu. Rev. Biophys., 2008, 37(1), 215-246.
[http://dx.doi.org/10.1146/annurev.biophys.37.032807.125924] [PMID: 18573080]
[5]
Habchi, J.; Tompa, P.; Longhi, S.; Uversky, V.N. Introduction to Intrinsically Disordered Proteins (IDPs). Chem. Rev., 2014, 114(13), 6561-6588.
[http://dx.doi.org/10.1021/cr400514h] [PMID: 24739139]
[6]
Dunker, A.K.; Uversky, V.N. Drugs for ‘protein clouds’: Targeting intrinsically disordered transcription factors. Curr. Opin. Pharmacol., 2010, 10(6), 782-788.
[http://dx.doi.org/10.1016/j.coph.2010.09.005] [PMID: 20889377]
[7]
Yan, J.; Dunker, A.K.; Uversky, V.N.; Kurgan, L. Molecular recognition features (MoRFs) in three domains of life. Mol. Biosyst., 2016, 12(3), 697-710.
[http://dx.doi.org/10.1039/C5MB00640F] [PMID: 26651072]
[8]
Macossay-Castillo, M.; Kosol, S.; Tompa, P.; Pancsa, R. Synonymous constraint elements show a tendency to encode intrinsically disor-dered protein segments. PLOS Comput. Biol., 2014, 10(5), e1003607.
[http://dx.doi.org/10.1371/journal.pcbi.1003607] [PMID: 24809503]
[9]
Piovesan, D.; Tabaro, F.; Paladin, L.; Necci, M.; Micetic, I.; Camilloni, C.; Davey, N.; Dosztányi, Z.; Mészáros, B.; Monzon, A.M.; Parisi, G.; Schad, E.; Sormanni, P.; Tompa, P.; Vendruscolo, M.; Vranken, W.F.; Tosatto, S.C.E. MobiDB 3.0: More annotations for intrinsic dis-order, conformational diversity and interactions in proteins. Nucleic Acids Res., 2018, 46(D1), D471-D476.
[http://dx.doi.org/10.1093/nar/gkx1071] [PMID: 29136219]
[10]
Cedeño, C.; Raveh-Hamit, H.; Dinnyés, A.; Tompa, P. Towards understanding protein disorder in-cell. Adv. Exp. Med. Biol., 2015, 870, 319-334.
[http://dx.doi.org/10.1007/978-3-319-20164-1_10] [PMID: 26387107]
[11]
Uversky, V.N. Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders. Front. Aging Neurosci., 2015, 7, 18.
[http://dx.doi.org/10.3389/fnagi.2015.00018] [PMID: 25784874]
[12]
Metallo, S.J. Intrinsically disordered proteins are potential drug targets. Curr. Opin. Chem. Biol., 2010, 14(4), 481-488.
[http://dx.doi.org/10.1016/j.cbpa.2010.06.169] [PMID: 20598937]
[13]
Wang, J.; Cao, Z.; Zhao, L.; Li, S.; Wang, J. Novel strategies for drug discovery based on Intrinsically Disordered Proteins (IDPs). Int. J. Mol. Sci., 2011, 12(5), 3205-3219.
[http://dx.doi.org/10.3390/ijms12053205] [PMID: 21686180]
[14]
Oates, M.E.; Romero, P.; Ishida, T.; Ghalwash, M.; Mizianty, M.J.; Xue, B.; Dosztányi, Z.; Uversky, V.N.; Obradovic, Z.; Kurgan, L.; Dunker, A.K.; Gough, J.D. 2P2: Database of disordered protein predictions. Nucleic Acids Res., 2013, 41(Database issue), D508-D516.
[PMID: 23203878]

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