The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The structures of type I polyketide synthases
Abstract
With the recent structural characterization of each of the component enzymes of type I polyketide synthases, scientists are coming tantalizingly close to elucidating the overall architectures and mechanisms of these enormous molecular factories. This review highlights not only what has been revealed about the structures and activities of each of the domains but also the mysteries that remain to be solved.
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Citations
Cites
Structural mechanism for statin inhibition of HMG-CoA reductase
Istvan, E. S., & Deisenhofer, J. (2001) · Science · doi:10.1126/science.1059344 · Cited by 1,644
Cited by
Assessing and harnessing updated polyketide synthase modules through combinatorial engineering
Ray, K. A., Lutgens, J. D., Bista, R., Zhang, J., Desai, R. R., Hirsch, M., Miyazawa, T., Cordova, A., & Keatinge-Clay, A. T. (2024) · Nature Communications · doi:10.1038/s41467-024-50844-6 · Cited by 28
Self-citationExpanding catalytic versatility of modular polyketide synthases for alcohol biosynthesis
Yao, S., Xie, S., Liu, R.-Z., Huang, Z., & Zhang, L. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01883-7 · Cited by 14
Metadata
- Authors
- Keatinge-Clay, A. T.
- Venue
- Natural Product Reports
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2012
- Volume
- 29
- Issue
- 10
- Pages
- 1050
- ISSN
- 0265-0568 (ISSN-L)
- 1460-4752
- OpenAlex
- W2091007201
- Cited by
- 344
- References
- 1
- FWCI
- 15.28
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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