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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HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153
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Chromatin remodelling during development
Ho, L., & Crabtree, G. R. (2010) · Nature · doi:10.1038/nature08911 · Cited by 1,114
Nonproteolytic Functions of Ubiquitin in Cell Signaling
Chen, Z. J., & Sun, L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.014 · Cited by 948
Is allostery an intrinsic property of all dynamic proteins?
Gunasekaran, K., Ma, B., & Nussinov, R. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20232 · Cited by 896
Self-citationPost-translational modifications in signal integration
Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876
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1 of the 75 references couldn’t be matched to a known paper.
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Chen, J., Qi, Y., Duan, Y., Duan, M., & Yang, M. (2020) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25960 · Cited by 1
Reconstitution of retrotranslocation by the Hrd1 ubiquitin ligase with purified components
Vasic, V. (2020) · doi:10.53846/goediss-7915 · Cited by 1
Tarbox, H. E., Branch, A., & Fried, S. D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.20.614172 · Cited by 1
Tuning cell motility : roles of nestin and vimentin in cancer cell invasion
Hyder, C. L. (2014)
Jiang, W., Zhang, P., Yang, P. H., Kang, N., Liu, J., Aihemaiti, Y., & Tu, H. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3940631
Tamar Schlick, A. (2014) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718240466.793494108
Mollapour, M. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737482045.793572272
Cheng, F., & Eriksson, J. (2014) · Wiley eBooks · doi:10.1002/9780470015902.a0001259.pub2
Decoding Allostery: How Interactions Lock S100B Conformations and What K55A Mutation Teaches Us
Samanta, R., Zhuang, X., Gondolesi, M., Varney, K. M., Weber, D. J., & Matysiak, S. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02475
Protein Neddylation Beyond Tumor Cells is a Vital Modulator of Anticancer Immunity
Xu, M., Liu, W., Liu, F., & Xie, P. (2026) · Phenomics · doi:10.1007/s43657-025-00233-w
BindingDB Entry 50018463: Allosteric inhibitors of the STAT3 signaling pathway.
BindingDB (2024) · UC San Diego · doi:10.7270/q2m90dwx
BindingDB (2023) · UC San Diego · doi:10.7270/q2b85d0b
BindingDB (2021) · UC San Diego · doi:10.7270/q2c53q9m
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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