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Uncovering post-translational modification-associated protein–protein interactions
Open accessAbstract
In living systems, the chemical space and functional repertoire of proteins are dramatically expanded through the post-translational modification (PTM) of various amino acid residues. These modifications frequently trigger unique protein-protein interactions (PPIs) - for example with reader proteins that directly bind the modified amino acid residue - which leads to downstream functional outcomes. The modification of a protein can also perturb its PPI network indirectly, for example, through altering its conformation or subcellular localization. Uncovering the network of unique PTM-triggered PPIs is essential to fully understand the roles of an ever-expanding list of PTMs in our biology. In this review, we discuss established strategies and current challenges associated with this endeavor.
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“PPIs are highly specific (especially PPIs dependent on acetylated isoforms [17]) and are thus attractive, albeit challenging, therapeutic targets[18].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [17]
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Metadata
- Authors
- Wang, S., Osgood, A. O., & Chatterjee, A.
- Affiliations
- Boston College (US)
- Corresponding author
- Chatterjee, Abhishek
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2022-06
- Volume
- 74
- Pages
- 102352
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC9464464
- OpenAlex
- W4220699331
- Cited by
- 153
- References
- 87
- Citations by year
- 2026: 44 · 2025: 54 · 2024: 28 · 2023: 24 · 2022: 3
- FWCI
- 3.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (am, 294 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Current Opinion in Structural Biology (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R35GM136437)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- post-translational modification, protein-protein interaction, protein-protein interaction network, protein conformation, subcellular localization
- MeSH terms
- Amino Acids, Protein Processing, Post-Translational, Proteins
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