Evidence map›Paper›PMID 31746669›Full record

ArticleMolecular biology of the cell2020

Dysregulation of very-long-chain fatty acid metabolism causes membrane saturation and induction of the unfolded protein response.

Yagmur Micoogullari, Sankha S Basu, Jessie Ang, Nina Weisshaar, Nicholas D Schmitt, Walid M Abdelmoula, Begona Lopez, Jeffrey N Agar, Nathalie Agar, John Hanna

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 14% 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, 40 citations in OpenAlex.

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  20. Lipids Composition in Plant Membranes.Cell biochemistry and biophysics · 2020
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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

10 authors at 2 institutions in 1 country.

Yagmur MicoogullariDepartment of Pathology and.
Sankha S BasuDepartment of Neurosurgery, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Jessie AngDepartment of Pathology and.
Nina WeisshaarDepartment of Pathology and.
Nicholas D SchmittDepartment of Chemistry and Chemical Biology and.
Walid M AbdelmoulaDepartment of Neurosurgery, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Begona LopezDepartment of Neurosurgery, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
Jeffrey N AgarDepartment of Chemistry and Chemical Biology and.
Nathalie AgarDepartment of Neurosurgery, Harvard Medical School and Brigham and Women's Hospital, Boston, MA 02115.
John HannaDepartment of Pathology and.
Brigham and Women's Hospital · USNortheastern University · US

Funding

VASCULAR, PULMONARY AND RENAL INJURYT32HL007627 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI GIMBRONE, MICHAEL A, MITCHELL, RICHARD N · 1985 to 2019
$12.7M
New Ubiquitin-Proteasome System Components that Protect against ProteotoxicityDP5OD019800 · OD · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2014 to 2018
$2.2M
NHLBI NIH HHS T32 HL007627NIH HHS DP5 OD019800
6 · The paper itself

Abstract

The unfolded protein response (UPR) senses defects in the endoplasmic reticulum (ER) and orchestrates a complex program of adaptive cellular remodeling. Increasing evidence suggests an important relationship between lipid homeostasis and the UPR. Defects in the ER membrane induce the UPR, and the UPR in turn controls the expression of some lipid metabolic genes. Among lipid species, the very-long-chain fatty acids (VLCFAs) are relatively rare and poorly understood. Here, we show that loss of the VLCFA-coenzyme A synthetase Fat1, which is essential for VLCFA utilization, results in ER stress with compensatory UPR induction. Comprehensive lipidomic analyses revealed a dramatic increase in membrane saturation in the

Indexed as

Coenzyme A LigasesEndoplasmic ReticulumEndoplasmic Reticulum StressFatty AcidsFatty Acid Transport ProteinsHomeostasisLipid MetabolismLipidsMembranesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUnfolded Protein ResponseCoenzyme A LigasesFAT1 protein, S cerevisiaeFatty AcidsFatty Acid Transport ProteinsLipidsSaccharomyces cerevisiae Proteins

Identifiers

PMID31746669
PMCPMC6938273
OpenAlexW2989581073

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.