The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications
Abstract
The diversity of distinct covalent forms of proteins (the proteome) greatly exceeds the number of proteins predicted by DNA coding capacities owing to directed posttranslational modifications. Enzymes dedicated to such protein modifications include 500 human protein kinases, 150 protein phosphatases, and 500 proteases. The major types of protein covalent modifications, such as phosphorylation, acetylation, glycosylation, methylation, and ubiquitylation, can be classified according to the type of amino acid side chain modified, the category of the modifying enzyme, and the extent of reversibility. Chemical events such as protein splicing, green fluorescent protein maturation, and proteasome autoactivations also represent posttranslational modifications. An understanding of the scope and pattern of the many posttranslational modifications in eukaryotic cells provides insight into the function and dynamics of proteome compositions.
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Identification of lysine succinylation as a new post-translational modification
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Metadata
- Authors
- Walsh, C. T., Garneau‐Tsodikova, S., & Gatto, G. J.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2005-11-16
- Volume
- 44
- Issue
- 45
- Pages
- 7342-7372
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2028161249
- Cited by
- 1,604
- References
- 12
- FWCI
- 8.39
- Type
- journal article
- Language
- en
- Open access
- closed
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