ArticleCell chemical biology2016
The Structural Relationship between Iterative and Modular PKSs.
Article in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Serendipity and the Slime Mold: A Visual Survey of High-Molecular-Weight Protein Assemblies Reveals the Structure of the Polyketide Synthase Pks16.Molecular & cellular proteomics : MCP · 2026Article
- Solution structure of the type I polyketide synthase Pks13 from Mycobacterium tuberculosis.BMC biology · 2022Article
- Protein-protein interactions in "cis-AT" polyketide synthases.Natural product reports · 2018Review
- The Uncommon Enzymology of Cis-Acyltransferase Assembly Lines.Chemical reviews · 2017Review
- Towards Precision Engineering of Canonical Polyketide Synthase Domains: Recent Advances and Future Prospects.Molecules (Basel, Switzerland) · 2017Review
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1 author.
Funding
Abstract
Recent work has characterized the architecture of a highly-reducing iterative polyketide synthase (PKS), the mycocerosic acid synthase (MAS) (Herbst et al., 2016). Beyond sharing a structural similarity with the mammalian fatty acid synthase (FAS), the authors argue that the MAS architecture is representative of some PKS modules.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.