Evidence map›Paper›PMID 11768756›Full record

ArticleJournal of bioenergetics and biomembranes2000

Cloning and characterization of a 35-kDa mouse mitochondrial outer membrane protein MOM35 with high homology to Tom40.

I L Rivera, G C Shore, E Schleiff

Abstract read
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In one paragraph

Article in Journal of bioenergetics and biomembranes, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

3 authors.

I L RiveraDepartment of Biochemistry, McGill University, Montreal Quebec, Canada.
G C Shore
E Schleiff

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have cloned a 35-kDa protein from a mouse cDNA library with a 25% overall amino acid identity to yTom40 and 27% identity to nTom40. This homolog toTom40 was named MOM35. It contains two possible start codons 36 amino acids apart from each other. Both the long and the short version of MOM35 can be imported in vitro into mouse mitochondria. The identified protein is imported into the outer mitochondrial membrane and comprises a trypsin-resistance pattern similar to that of nTom40. Tom40 of N. crassa, S. cerevisiae, and the protein identified herein contains a highly conserved region with possible physiological importance. Subsequent investigation has revealed that this region interacts specifically in vitro with preproteins proposed to be imported by a Tom40-dependent pathway.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBinding SitesCloning, MolecularDNA PrimersGene LibraryIntracellular MembranesMembrane ProteinsMembrane Transport ProteinsMiceMitochondria, HeartMitochondrial Membrane Transport ProteinsMitochondrial ProteinsMolecular Sequence DataNeurospora crassaDNA PrimersMembrane ProteinsMembrane Transport ProteinsMitochondrial Membrane Transport Proteinsmitochondrial outer membrane protein 35-kDa, mouseMitochondrial ProteinsProtein PrecursorsSaccharomyces cerevisiae ProteinsTom40 protein, S cerevisiaeTrypsin

Identifiers

PMID11768756

What OpenQuestion holds

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Registered trials

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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.