Evidence map›Paper›PMID 32722450›Full record

ReviewBiomolecules2020

On the Detection and Functional Significance of the Protein-Protein Interactions of Mitochondrial Transport Proteins.

Youjun Zhang, Alisdair R Fernie

Abstract readReview
In one paragraph

Review in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Structures ofScience (New York, N.Y.) · 2022
    Article
  5. Review
  6. Review
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.

Youjun ZhangCenter of Plant Systems Biology and Biotechnology, 4000 Plovdiv, Bulgaria.ORCID 0000-0003-1052-0256
Alisdair R FernieCenter of Plant Systems Biology and Biotechnology, 4000 Plovdiv, Bulgaria.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein assemblies are highly prevalent in all living cells. Considerable evidence has recently accumulated suggesting that particularly transient association/dissociation of proteins represent an important means of regulation of metabolism. This is true not only in the cytosol and organelle matrices, but also at membrane surfaces where, for example, receptor complexes, as well as those of key metabolic pathways, are common. Transporters also frequently come up in lists of interacting proteins, for example, binding proteins that catalyze the production of their substrates or that act as relays within signal transduction cascades. In this review, we provide an update of technologies that are used in the study of such interactions with mitochondrial transport proteins, highlighting the difficulties that arise in their use for membrane proteins and discussing our current understanding of the biological function of such interactions.

Indexed as

Protein Interaction MappingProtein Interaction MapsAnimalsCarrier ProteinsHumansMitochondriaMitochondrial ProteinsCarrier ProteinsMitochondrial Proteinsinner mitochondrial membranemitochondrial carrier familyprotein–protein interaction

Identifiers

PMID32722450
PMCPMC7464641

What OpenQuestion holds

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LicenceCC BY
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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.