Bisindolylpyrrole Induces a Cpr3- and Porin1/2-Dependent Transition in Yeast Mitochondrial Permeability in a Low Conductance State via the AACs-Associated Pore.

Masami Koushi, Rei Asakai

Open access · goldAbstract read

In one paragraph

Article in International journal of molecular sciences, 2021. 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

0.1field-weighted citation impact, top 58% 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, 1 citations in OpenAlex.

Mitochondrial Research: Yeast and Human Cells as Models.International journal of molecular sciences · 2022
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

2 authors at 1 institution in 1 country.

Masami KoushiDepartment of Morphophysiology, Faculty of Pharmaceutical Sciences, Josai International University, 1 Gumyo, Togane, Chiba 283-8555, Japan.

Rei AsakaiDepartment of Morphophysiology, Faculty of Pharmaceutical Sciences, Josai International University, 1 Gumyo, Togane, Chiba 283-8555, Japan.ORCID 0000-0002-1018-7556

Josai International University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although the mitochondrial permeability transition pore (PTP) is presumably formed by either ATP synthase or the ATP/ADP carrier (AAC), little is known about their differential roles in PTP activation. We explored the role of AAC and ATP synthase in PTP formation in

Indexed as

CyclophilinsDose-Response Relationship, DrugMembrane Potential, MitochondrialMitochondriaMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesPermeabilityPorinsProtein MultimerizationPyrrolesSaccharomyces cerevisiaeYeastsCyclophilinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesPorinsPyrrolesADP/ATP carrierbisindolylpyrrolemitochondrial permeability transition poreSaccharomyces cerevisiae

Identifiers

PMID33530556

DOI10.3390/ijms22031212

PMCPMC7865566

OpenAlexW3126107564

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.