The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Nonenzymatic Deamidation of Asparaginyl and Glutaminyl Residues in Protein
Abstract
Some asparagine and glutamine residues in proteins undergo deamidation to aspartate and glutamate with rates that depend upon the sequence and higher-order structure of the protein. Functional groups within the protein can catalyze this reaction, acting as general acids, bases, or stabilizers of the transition state. Information from specific proteins that deamidate and analysis of protein sequence and structure data bases suggest that asparagine and glutamine lability has been a selective pressure in the evolution of protein sequence and folding. Asparagine and glutamine deamidation can affect protein structure and function in natural and engineered mutant sequences, and may play a role in the regulation of protein folding, protein breakdown, and aging.
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Cites
Sickle Cell Anemia, a Molecular Disease
Pauling, L., Itano, H. A., Singer, S. J., & Wells, I. C. (1949) · Science · doi:10.1126/science.110.2865.543 · Cited by 2,319
Cited by
Food protein functionality: A comprehensive approach
Foegeding, E. A., & Davis, J. P. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.05.008 · Cited by 486
Mass spectrometry approaches to glycomic and glycoproteomic analyses
Ruhaak, L. R., Xu, G., Li, Q., Goonatilleke, E., & Lebrilla, C. B. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00732 · Cited by 395
Proteins in Art, Archaeology, and Paleontology: From Detection to Identification
Dallongeville, S., Garnier, N., Rolando, C., & Tokarski, C. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00037 · Cited by 172
Ferrari (1998) · doi:10.1002/(sici)1097-0290(19981205)60:5<589::aid-bit9>3.0.co;2-k
Metadata
- Authors
- Tonie Wright, H., & Urry, D. W.
- Venue
- Critical Reviews in Biochemistry and Molecular Biology
- Publisher
- Informa UK Limited
- Published
- 1991-01
- Volume
- 26
- Issue
- 1
- Pages
- 1-52
- ISSN
- 0045-6411 (ISSN-L)
- 1040-9238
- 1549-7798
- OpenAlex
- W2101971141
- Cited by
- 414
- References
- 1
- FWCI
- 1.75
- Type
- journal article
- Language
- en
- Open access
- closed
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- Tonie Wright, H., & Urry, D. W. (1991). Nonenzymatic Deamidation of Asparaginyl and Glutaminyl Residues in Protein. Critical Reviews in Biochemistry and Molecular Biology. https://doi.org/10.3109/10409239109081719
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
