ArticleJournal of the American Chemical Society2020
Antibody Probes of Module 1 of the 6-Deoxyerythronolide B Synthase Reveal an Extended Conformation During Ketoreduction.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed.
- Structural basis for intermodular communication in assembly-line polyketide biosynthesis.Nature chemical biology · 2025Article
- Architecture of full-length type I modular polyketide synthases revealed by X-ray crystallography, cryo-electron microscopy, and AlphaFold2.Natural product reports · 2024Review
- Structure and Mechanisms of Assembly-Line Polyketide Synthases.Annual review of biochemistry · 2024Review
- Adaptable SEC-SAXS data collection for higher quality structure analysis in solution.Protein science : a publication of the Protein Society · 2024Article
- Discovery and Characterization of Antibody Probes of Module 2 of the 6-Deoxyerythronolide B Synthase.Biochemistry · 2023Article
- Enzymology of assembly line synthesis by modular polyketide synthases.Nature chemical biology · 2023Review
- Fragment antigen binding domains (FSynthetic and systems biotechnology · 2022Article
- Article
- Mapping the catalytic conformations of an assembly-line polyketide synthase module.Science (New York, N.Y.) · 2021Article
- Modular polyketide synthase contains two reaction chambers that operate asynchronously.Science (New York, N.Y.) · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The 6-deoxyerythronolide B synthase (DEBS) is a prototypical assembly line polyketide synthase (PKS) that synthesizes the macrocyclic core of the antibiotic erythromycin. Each of its six multidomain modules presumably sample distinct conformations, as biosynthetic intermediates tethered to their acyl carrier proteins interact with multiple active sites during the courses of their catalytic cycles. The spatiotemporal details underlying these protein dynamics remain elusive. Here, we investigate one aspect of this conformational flexibility using two domain-specific monoclonal antibody fragments (F
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Registered trials
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