Evidence map›Paper›PMID 34010015›Full record

ArticleMolecular biology of the cell2021

Peroxisomes exhibit compromised structure and matrix protein content in SARS-CoV-2-infected cells.

Barbara Knoblach, Ray Ishida, Tom C Hobman, Richard A Rachubinski

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

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  10. The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024
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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

4 authors at 1 institution in 1 country.

Barbara KnoblachDepartment of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Ray IshidaDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Tom C HobmanDepartment of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Richard A RachubinskiDepartment of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
University of Alberta · CA

Funding

CIHR OV3-172302
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel coronavirus that has triggered global health and economic crises. Here we report the effects of SARS-CoV-2 infection on peroxisomes of human cell lines Huh-7 and SK-N-SH. Peroxisomes undergo dramatic changes in morphology in SARS-CoV-2-infected cells. Rearrangement of peroxisomal membranes is followed by redistribution of peroxisomal matrix proteins to the cytosol, resulting in a dramatic decrease in the number of mature peroxisomes. The SARS-CoV-2 ORF14 protein was shown to interact physically with human PEX14, a peroxisomal membrane protein required for matrix protein import and peroxisome biogenesis. Given the important roles of peroxisomes in innate immunity, SARS-CoV-2 may directly target peroxisomes, resulting in loss of peroxisome structural integrity, matrix protein content and ability to function in antiviral signaling.

Indexed as

AnimalsCell LineCell MembraneChlorocebus aethiopsCoronavirus Nucleocapsid ProteinsExtracellular Matrix ProteinsHumansMembrane ProteinsPeroxisomesPhosphoproteinsRepressor ProteinsSARS-CoV-2Vero CellsCoronavirus Nucleocapsid ProteinsExtracellular Matrix ProteinsMembrane Proteinsnucleocapsid phosphoprotein, SARS-CoV-2PEX14 protein, humanPhosphoproteinsRepressor Proteins

Identifiers

PMID34010015
PMCPMC8351553
OpenAlexW3160915383

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.