Evidence map›Paper›PMID 34024890›Full record

ArticleJournal of microbiology and biotechnology2021

Mitochondrial Targeting Domain Homologs Induce Necrotic Cell Death Via Mitochondrial and Endoplasmic Reticulum Disruption.

Junghee Park, Ji-Hye Han, Seung-Hyun Myung, Hea-Jong Chung, Jae-Il Park, Ju-Yeon Cho, Tae-Hyoung Kim

Open access · bronzeAbstract read
In one paragraph

Article in Journal of microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 96% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

7 authors at 3 institutions in 1 country.

Junghee ParkDepartment of Biochemistry and Molecular Biology, Chosun University School of Medicine, Gwangju 61452, Republic of Korea.
Ji-Hye HanDepartment of Biochemistry and Molecular Biology, Chosun University School of Medicine, Gwangju 61452, Republic of Korea.
Seung-Hyun MyungDepartment of Biochemistry and Molecular Biology, Chosun University School of Medicine, Gwangju 61452, Republic of Korea.
Hea-Jong ChungGwangju Center, Korea Basic Science Institute, Gwangju 61168, Republic of Korea.
Jae-Il ParkGwangju Center, Korea Basic Science Institute, Gwangju 61168, Republic of Korea.
Ju-Yeon ChoDepartment of Medicine, Chosun University Hospital, Gwangju 61453, Republic of Korea.
Tae-Hyoung KimDepartment of Biochemistry and Molecular Biology, Chosun University School of Medicine, Gwangju 61452, Republic of Korea.
Chosun University · KRKorea Basic Science Institute · KRChosun University Hospital · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial targeting domain (MTD) of Noxa contributes to its mitochondrial localization and to apoptosis induction. As a peptide, MTD fused with octa-arginine (R8), a CPP, induces necrosis related to intracellular calcium influx and destruction of mitochondria and endoplasmic reticulum. We searched for homologs of MTD, and compared their cell killing capability when fused with R8. Three of the seven peptides triggered cell death with similar mechanisms. The comparative analysis of peptide sequences showed that four amino acid sites of MTD are critical in regulating necrosis, suggesting the potential to generate artificial, adjustable cytotoxic peptides, which could be effective medicines for many diseases. Thus, homologs functionality could hint to the functions of their belonging proteins.

Indexed as

Amino Acid SequenceApoptosis Regulatory ProteinsCalciumCell DeathCell SurvivalEndoplasmic ReticulumHeLa CellsHumansMitochondriaNecrosisOligopeptidesProtein DomainsReactive Oxygen SpeciesSequence AlignmentApoptosis Regulatory ProteinsCalciumocta-arginine peptideOligopeptidesReactive Oxygen SpeciesmitochondriaMTDMTD homologsnecrotic cell death

Identifiers

PMID34024890
PMCPMC9705834
OpenAlexW3164693017

What OpenQuestion holds

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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.