Evidence map›Paper›PMID 27960309›Full record

ArticleJournal of the American Chemical Society2016

Vinylogous Dehydration by a Polyketide Dehydratase Domain in Curacin Biosynthesis.

William D Fiers, Greg J Dodge, David H Sherman, Janet L Smith, Courtney C Aldrich

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.

  1. Pooled it
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  4. Structure of a modular polyketide synthase reducing region.Structure (London, England : 1993) · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

William D FiersDepartment of Medicinal Chemistry, College of Pharmacy, University of Minnesota , Minneapolis, Minnesota 55455, United States.
Greg J DodgeDepartment of Biological Chemistry and Life Sciences Institute, University of Michigan , Ann Arbor, Michigan 48109, United States.
David H ShermanDepartment of Medicinal Chemistry and Life Sciences Institute, University of Michigan , Ann Arbor, Michigan 48109, United States.
Janet L SmithDepartment of Biological Chemistry and Life Sciences Institute, University of Michigan , Ann Arbor, Michigan 48109, United States.
Courtney C AldrichDepartment of Medicinal Chemistry, College of Pharmacy, University of Minnesota , Minneapolis, Minnesota 55455, United States.
University of Michigan–Ann Arbor · USUniversity of Minnesota · US

Funding

Women's CancerP30CA077598 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI Douglas Yee · 1998 to 2026
$100.4M
Structural basis of specificity in affinity-labeled polyketide synthase didomainsR01GM081544 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 2009 to 2012
$1.9M
Silicon Mechanics Compute ClusterS10OD020011 · OD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SKINIOTIS, GEORGIOS · 2015 to 2015
$490k
NCI NIH HHS P30 CA077598NIGMS NIH HHS R01 GM081544NIH HHS S10 OD020011
6 · The paper itself

Abstract

Polyketide synthase (PKS) enzymes continue to hold great promise as synthetic biology platforms for the production of novel therapeutic agents, biofuels, and commodity chemicals. Dehydratase (DH) catalytic domains play an important role during polyketide biosynthesis through the dehydration of the nascent polyketide intermediate to provide olefins. Our understanding of the detailed mechanistic and structural underpinning of DH domains that control substrate specificity and selectivity remains limited, thus hindering our efforts to rationally re-engineer PKSs. The curacin pathway houses a rare plurality of possible double bond permutations containing conjugated olefins as well as both cis- and trans-olefins, providing an unrivaled model system for polyketide dehydration. All four DH domains implicated in curacin biosynthesis were characterized in vitro using synthetic substrates, and activity was measured by LC-MS/MS analysis. These studies resulted in complete kinetic characterization of the all-trans-trienoate-forming CurK-DH, whose k

Indexed as

Alcohol OxidoreductasesBacterial ProteinsCyanobacteriaCyclopropanesDehydrationMolecular ConformationProtein DomainsThiazolesAlcohol OxidoreductasesBacterial Proteinscuracin ACyclopropanespolyketide synthase ketoreductaseThiazoles

Identifiers

PMID27960309
PMCPMC5590676
OpenAlexW2549770330

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.