The DOI matches its Crossref record; 74 of the 75 references it cites were found in a registry or an index.
Allosteric post-translational modification codes
Abstract
Post-translational modifications (PTMs) have been recognized to impact protein function in two ways: (i) orthosterically, via direct recognition by protein domains or through interference with binding; and (ii) allosterically, via conformational changes induced at the functional sites. Because different chemical types of PTMs elicit different structural alterations, the effects of combinatorial codes of PTMs are vastly larger than previously believed. Combined with orthosteric PTMs, the impact of PTMs on cellular regulation is immense. From an evolutionary standpoint, harnessing this immense, yet highly specific, PTM code is an extremely efficient vehicle that can save a cell several-fold in gene number and speed up its response to environmental change.
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In the citing paper
“A post-translational modification (PTM) can bias the conformational distribution, increasing the population time of a cluster favored for binding a specific partner77.”
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 [77]
In the citing paper
“Combinations of PTMs can constitute an allosteric code.77”
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 [77]
Citations
Cites
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Is allostery an intrinsic property of all dynamic proteins?
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Self-citationPost-translational modifications in signal integration
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Cited by
Sorted by citations
Allostery in Disease and in Drug Discovery
Nussinov, R., & Tsai, C. (2013) · Cell · doi:10.1016/j.cell.2013.03.034 · Cited by 769
Self-citationWei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Self-citationThe Role of Protein Loops and Linkers in Conformational Dynamics and Allostery
Papaleo, E., Saladino, G., Lambrughi, M., Lindorff‐Larsen, K., Gervasio, F. L., & Nussinov, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00623 · Cited by 434
Self-citationProtein Language: Post-Translational Modifications Talking to Each Other.
Vu, L. D., Gevaert, K., & Smet, I. D. (2018) · Trends in Plant Science · doi:10.1016/j.tplants.2018.09.004 · Cited by 340
Pejaver, V., Hsu, W., Xin, F., Dunker, A. K., Uversky, V. N., & Radivojac, P. (2014) · Protein Science · doi:10.1002/pro.2494 · Cited by 349
Self-citation
Metadata
- Authors
- Nussinov, R., Tsai, C.-J., Xin, F., & Radivojac, P.
- Affiliations
- National Institutes of Health (US)
- Frederick National Laboratory for Cancer Research (US)
- Indiana University Bloomington (US)
- Corresponding author
- Nussinov, Ruth
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2012-10
- Volume
- 37
- Issue
- 10
- Pages
- 447-455
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W1995254028
- Cited by
- 211
- References
- 75
- Citations by year
- 2026: 5 · 2025: 25 · 2024: 8 · 2023: 8 · 2022: 19 · 2021: 16 · 2020: 18 · 2019: 17 · 2018: 13 · 2017: 10 · 2016: 13 · 2015: 13 · 2014: 25 · 2013: 18 · 2012: 3
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Korea Agency for Infrastructure Technology Advancement
- National Institutes of Health
- U.S. Public Health Service (HHSN261200800001E)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- post-translational modification, allosteric regulation, protein conformational change, protein domains, cell regulation
- MeSH terms
- Allosteric Regulation, Humans, Models, Molecular, Protein Processing, Post-Translational, Proteins
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