Evidence map›Paper›PMID 33753518›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase and interact with assembly factors for complex I.

Joe Carroll, Jiuya He, Shujing Ding, Ian M Fearnley, John E Walker

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

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  15. Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024
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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

5 authors at 1 institution in 1 country.

Joe CarrollMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0003-0530-7194
Jiuya HeMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0002-8602-1202
Shujing DingMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
Ian M FearnleyMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0002-8510-1219
John E WalkerMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom john.walker@mrc-mbu.cam.ac.uk.ORCID 0000-0001-7929-2162
University of Cambridge · GB

Funding

Medical Research Council MC_EX_MR/M009858/1Medical Research Council MC_UU_00015/8Medical Research Council MR/M009858/1
6 · The paper itself

Abstract

Human mitochondrial ATP synthase is a molecular machine with a rotary action bound in the inner organellar membranes. Turning of the rotor, driven by a proton motive force, provides energy to make ATP from ADP and phosphate. Among the 29 component proteins of 18 kinds, ATP6 and ATP8 are mitochondrial gene products, and the rest are nuclear gene products that are imported into the organelle. The ATP synthase is assembled from them via intermediate modules representing the main structural elements of the enzyme. One such module is the c

Indexed as

Catalytic DomainElectron Transport Complex IGene DeletionHEK293 CellsHumansMembrane ProteinsMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesProton-Motive ForceRotationElectron Transport Complex IMembrane ProteinsMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesTMEM70 protein, humanassemblyATP synthasehuman mitochondriaTMEM242TMEM70

Identifiers

PMID33753518
PMCPMC8020751
OpenAlexW3137671608

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.