Evidence map›Paper›PMID 31787485›Full record

ReviewTrends in biochemical sciences2020

The SLC25 Mitochondrial Carrier Family: Structure and Mechanism.

Jonathan J Ruprecht, Edmund R S Kunji

Open access · hybridAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 255 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
255citing papers in PubMed, 1 pooled it
14.2field-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

255 citing papers in PubMed, 1 synthesis or guideline pooled it, 398 citations in OpenAlex.

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  20. Proteomic profiling of metabolizing enzymes and transporters in 2 layers of Caucasian human skin.Drug metabolism and disposition: the biological fate of chemicals · 2026
    Article

195 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 2 institutions in 1 country.

Jonathan J RuprechtMedical Research Council (MRC) Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, CB2 0XY, UK.
Edmund R S KunjiMedical Research Council (MRC) Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, CB2 0XY, UK. Electronic address: ek@mrc-mbu.cam.ac.uk.
Medical Research Council · GBUniversity of Cambridge · GB

Funding

Medical Research Council MC_UU_00015/1Medical Research Council MC_UU_00015/7
6 · The paper itself

Abstract

Members of the mitochondrial carrier family (SLC25) provide the transport steps for amino acids, carboxylic acids, fatty acids, cofactors, inorganic ions, and nucleotides across the mitochondrial inner membrane and are crucial for many cellular processes. Here, we use new insights into the transport mechanism of the mitochondrial ADP/ATP carrier to examine the structure and function of other mitochondrial carriers. They all have a single substrate-binding site and two gates, which are present on either side of the membrane and involve salt-bridge networks. Transport is likely to occur by a common mechanism, in which the coordinated movement of six structural elements leads to the alternating opening and closing of the matrix or cytoplasmic side of the carriers.

Indexed as

AnimalsBiological TransportCytoplasmHumansMitochondriaMitochondrial ADP, ATP TranslocasesMitochondrial ADP, ATP Translocasesadenine nucleotide translocaseenergeticsmitochondrial transportsalt-bridge networkstransport mechanismuncoupling protein

Identifiers

PMID31787485
PMCPMC7611774
OpenAlexW2990776892

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.