Evidence map›Paper›PMID 29545371›Full record

ArticleThe Journal of cell biology2018

Romo1 is a mitochondrial nonselective cation channel with viroporin-like characteristics.

Gi Young Lee, Deok-Gyun You, Hye-Ra Lee, Sun Wook Hwang, C Justin Lee, Young Do Yoo

Abstract read
In one paragraph

Article in The Journal of cell biology, 2018. 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
2.0field-weighted citation impact, top 13% 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, 45 citations in OpenAlex.

  1. Article
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  3. [ROMO1 Promotes the Repair of Radiation-induced Skin Injury by Regulating Mitochondrial Function and Keratinocyte Proliferation].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 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

6 authors at 1 institution in 1 country.

Gi Young LeeLaboratory of Molecular Cell Biology, Graduate School of Medicine, Korea University College of Medicine, Korea University, Seoul, Republic of Korea.
Deok-Gyun YouLaboratory of Molecular Cell Biology, Graduate School of Medicine, Korea University College of Medicine, Korea University, Seoul, Republic of Korea.
Hye-Ra LeeLaboratory of Molecular Cell Biology, Graduate School of Medicine, Korea University College of Medicine, Korea University, Seoul, Republic of Korea.
Sun Wook HwangDepartment of Biomedical Sciences, Korea University College of Medicine, Korea University, Seoul, Republic of Korea.
C Justin LeeCenter for Neuroscience and Functional Connectomics, Korea Institute of Science and Technology, Seoul, Republic of Korea.
Young Do YooLaboratory of Molecular Cell Biology, Graduate School of Medicine, Korea University College of Medicine, Korea University, Seoul, Republic of Korea ydy1130@korea.ac.kr.ORCID 0000-0001-7636-4677
Korea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reactive oxygen species (ROS) modulator 1 (Romo1) is a nuclear-encoded mitochondrial inner membrane protein known to regulate mitochondrial ROS production and to act as an essential redox sensor in mitochondrial dynamics. Although its physiological roles have been studied for a decade, the biophysical mechanisms that explain these activities of Romo1 are unclear. In this study, we report that Romo1 is a unique mitochondrial ion channel that differs from currently identified eukaryotic ion channels. Romo1 is a highly conserved protein with structural features of class II viroporins, which are virus-encoded nonselective cation channels. Indeed, Romo1 forms a nonselective cation channel with its amphipathic helical transmembrane domain necessary for pore-forming activity. Notably, channel activity was specifically inhibited by Fe

Indexed as

Amino Acid SequenceCationsCell MembraneCell Membrane PermeabilityConserved SequenceHEK293 CellsHuman Immunodeficiency Virus ProteinsHumansIon ChannelsIronMembrane ProteinsMitochondriaMitochondrial ProteinsModels, MolecularProtein MultimerizationProtein Structure, SecondaryCationsHuman Immunodeficiency Virus ProteinsIon ChannelsIronMembrane ProteinsMitochondrial ProteinsROMO1 protein, humanViral Regulatory and Accessory ProteinsViroporin Proteinsvpu protein, Human immunodeficiency virus 1

Identifiers

PMID29545371
PMCPMC5987721
OpenAlexW2791402143

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.