Evidence map›Paper›PMID 32883882›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

A kinetic rationale for functional redundancy in fatty acid biosynthesis.

Sophia Ruppe, Kathryn Mains, Jerome M Fox

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. A Hidden Binding Pocket in the β- ketoacyl-ACP Synthase FabB.bioRxiv : the preprint server for biology · 2026
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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

3 authors at 1 institution in 1 country.

Sophia RuppeDepartment of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, CO 80303.ORCID 0000-0003-0743-8796
Kathryn MainsDepartment of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, CO 80303.ORCID 0000-0002-3623-1383
Jerome M FoxDepartment of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, CO 80303 jerome.fox@colorado.edu.ORCID 0000-0002-3739-1899
University of Colorado Boulder · US

Funding

Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
NIGMS NIH HHS T32 GM065103
6 · The paper itself

Abstract

Cells build fatty acids with biocatalytic assembly lines in which a subset of enzymes often exhibit overlapping activities (e.g., two enzymes catalyze one or more identical reactions). Although the discrete enzymes that make up fatty acid pathways are well characterized, the importance of catalytic overlap between them is poorly understood. We developed a detailed kinetic model of the fatty acid synthase (FAS) of

Indexed as

Models, BiologicalBiochemical PhenomenaEscherichia coli ProteinsFatty AcidsFatty Acid Synthase, Type IIKineticsMetabolic Networks and PathwaysEscherichia coli ProteinsFatty AcidsFatty Acid Synthase, Type IIbiocatalytic networksenzyme cascadesfatty acid synthesiskinetic modeloleochemicals

Identifiers

PMID32883882
PMCPMC7519226
OpenAlexW3081574745

What OpenQuestion holds

Textmetadata
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.