Evidence map›Paper›PMID 30647902›Full record

ReviewF1000Research2018

Recent insights into the structure and function of Mitofusins in mitochondrial fusion.

Mickael M Cohen, David Tareste

Open access · goldAbstract readReview
In one paragraph

Review in F1000Research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

24 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
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  11. Mitochondrial dynamics proteins as emerging drug targets.Trends in pharmacological sciences · 2023
    Review
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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

2 authors at 2 institutions in 1 country.

Mickael M CohenSorbonne Université, CNRS UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Paris, France.
David TaresteUniversité Paris Descartes, Sorbonne Paris Cité, INSERM ERL U950, Trafic Membranaire dans le Cerveau Normal et Pathologique, Paris, France.ORCID 0000-0002-8744-7598
Centre National de la Recherche Scientifique · FRDélégation Paris 5 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria undergo frequent fusion and fission events to adapt their morphology to cellular needs. Homotypic docking and fusion of outer mitochondrial membranes are controlled by Mitofusins, a set of large membrane-anchored GTPase proteins belonging to the dynamin superfamily. Mitofusins include, in addition to their GTPase and transmembrane domains, two heptad repeat domains, HR1 and HR2. All four regions are crucial for Mitofusin function, but their precise contribution to mitochondrial docking and fusion events has remained elusive until very recently. In this commentary, we first give an overview of the established strategies employed by various protein machineries distinct from Mitofusins to mediate membrane fusion. We then present recent structure-function data on Mitofusins that provide important novel insights into their mode of action in mitochondrial fusion.

Indexed as

GTP PhosphohydrolasesMitochondrial DynamicsMitochondrial Membrane Transport ProteinsAnimalsHumansMembrane FusionMitochondrial MembranesGTP PhosphohydrolasesMfn1 protein, humanMitochondrial Membrane Transport ProteinsAmphipathic HelixAtlastinCoiled-coilFusionGTPaseHemagglutininHeptad RepeatLipidsMembraneMitochondriaMitofusinSNARE

Identifiers

PMID30647902
PMCPMC6317495
OpenAlexW2907940778

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.