The DOI matches its Crossref record; 629 of the 629 references it cites were found in a registry or an index.
Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
Open accessAbstract
Post-translational acetylation of lysine residues has emerged as a key regulatory mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique modification of histones, acetylation marks are now found on thousands of nonhistone proteins located in virtually every cellular compartment. Here we summarize key findings in the field of protein acetylation over the past 20 years with a focus on recent discoveries in nuclear, cytoplasmic, and mitochondrial compartments. Collectively, these findings have elevated protein acetylation as a major post-translational modification, underscoring its physiological relevance in gene regulation, cell signaling, metabolism, and disease.
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1 retracted
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Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Metabolism of Amino Acids in Cancer
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Metadata
- Authors
- Ali, I., Conrad, R. J., Verdin, E., & Ott, M.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2018-02-06
- Volume
- 118
- Issue
- 3
- Pages
- 1216-1252
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2786527187
- Cited by
- 366
- References
- 629
- FWCI
- 2.86
- Type
- journal article
- Language
- en
- Open access
- green
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- Ali, I., Conrad, R. J., Verdin, E., & Ott, M. (2018). Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.7b00181
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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