Evidence map›Paper›PMID 30030361›Full record

ReviewEssays in biochemistry2018

Assembly of mammalian oxidative phosphorylation complexes I-V and supercomplexes.

Alba Signes, Erika Fernandez-Vizarra

Open access · hybridAbstract readReview
In one paragraph

Review in Essays in biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
158citing papers in PubMed, 1 pooled it
10.9field-weighted citation impact, top 1% 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

158 citing papers in PubMed, 1 synthesis or guideline pooled it, 279 citations in OpenAlex.

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98 more citing papers are in PubMed but not listed here.

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.

Alba SignesMRC-Mitochondrial Biology Unit, University of Cambridge, Hills Road, Cambridge CB2 0XY, U.K.
Erika Fernandez-VizarraMRC-Mitochondrial Biology Unit, University of Cambridge, Hills Road, Cambridge CB2 0XY, U.K. emfvb2@mrc-mbu.cam.ac.uk.
MRC Mitochondrial Biology Unit · GB

Funding

Medical Research Council MC_UP_1002/1Medical Research Council QQR 2015-2020
6 · The paper itself

Abstract

The assembly of the five oxidative phosphorylation system (OXPHOS) complexes in the inner mitochondrial membrane is an intricate process. The human enzymes comprise core proteins, performing the catalytic activities, and a large number of 'supernumerary' subunits that play essential roles in assembly, regulation and stability. The correct addition of prosthetic groups as well as chaperoning and incorporation of the structural components require a large number of factors, many of which have been found mutated in cases of mitochondrial disease. Nowadays, the mechanisms of assembly for each of the individual complexes are almost completely understood and the knowledge about the assembly factors involved is constantly increasing. On the other hand, it is now well established that complexes I, III and IV interact with each other, forming the so-called respiratory supercomplexes or 'respirasomes', although the pathways that lead to their formation are still not completely clear. This review is a summary of our current knowledge concerning the assembly of complexes I-V and of the supercomplexes.

Indexed as

Oxidative PhosphorylationAnimalsElectron TransportHumansMammalsMitochondriaMultienzyme ComplexesMultienzyme Complexesatp synthaseelectron transport chainmitochondriaoxidative phosphorylationrespiratory chain complex assembly

Identifiers

PMID30030361
PMCPMC6056720
OpenAlexW2884533811

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.