Evidence map›Paper›PMID 35876515›Full record

ArticleJournal of bacteriology2022

Escherichia coli YigI is a Conserved Gammaproteobacterial Acyl-CoA Thioesterase Permitting Metabolism of Unusual Fatty Acid Substrates.

Michael Schmidt, Theresa Proctor, Rucheng Diao, Lydia Freddolino

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of bacteriology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 42% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Deciphering the proteome ofComputational and structural biotechnology journal · 2025
    Article
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

4 authors at 1 institution in 1 country.

Michael SchmidtDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, USA.
Theresa ProctorPost-baccalaureate Research Education Program (PREP), University of Michigan Medical School, Ann Arbor, Michigan, USA.
Rucheng DiaoDepartment of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, Michigan, USA.
Lydia FreddolinoDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan, USA.ORCID 0000-0002-5821-4226
University of Michigan · US

Funding

University of Michigan Postbaccalaureate Research Education Program (UM PREP)R25GM086262 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ALLEN, BENJAMIN · 2009 to 2024
$6.1M
HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) R01 AI13467801NIGMS NIH HHS R25 GM086262
6 · The paper itself

Abstract

Thioesterases play a critical role in metabolism, membrane biosynthesis, and overall homeostasis for all domains of life. In this present study, we characterize a putative thioesterase from Escherichia coli MG1655 and define its role as a cytosolic enzyme. Building on structure-guided functional predictions, we show that YigI is a medium- to long-chain acyl-CoA thioesterase that is involved in the degradation of conjugated linoleic acid (CLA)

Indexed as

Escherichia coliFatty AcidsAcyl Coenzyme AThiolester HydrolasesAcyl Coenzyme AFatty AcidsThiolester HydrolasesEscherichia coliesterasepoorly annotated proteinsprotein function predictionthioesterase

Identifiers

PMID35876515
PMCPMC9380530
OpenAlexW4287377794

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.