Evidence map›Paper›PMID 23438732›Full record

ArticleMolecular & cellular proteomics : MCP2013

Predicting physical interactions between protein complexes.

Trevor Clancy, Einar Andreas Rødland, Ståle Nygard, Eivind Hovig

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
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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

4 authors.

Trevor ClancyDepartment of Tumor Biology, Institute for Cancer Research, The Norwegian Radium Hospital and Oslo University Hospital, Oslo, Norway. trevor.clancy@rr-research.no
Einar Andreas Rødland
Ståle Nygard
Eivind Hovig

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein complexes enact most biochemical functions in the cell. Dynamic interactions between protein complexes are frequent in many cellular processes. As they are often of a transient nature, they may be difficult to detect using current genome-wide screens. Here, we describe a method to computationally predict physical interactions between protein complexes, applied to both humans and yeast. We integrated manually curated protein complexes and physical protein interaction networks, and we designed a statistical method to identify pairs of protein complexes where the number of protein interactions between a complex pair is due to an actual physical interaction between the complexes. An evaluation against manually curated physical complex-complex interactions in yeast revealed that 50% of these interactions could be predicted in this manner. A community network analysis of the highest scoring pairs revealed a biologically sensible organization of physical complex-complex interactions in the cell. Such analyses of proteomes may serve as a guide to the discovery of novel functional cellular relationships.

Indexed as

AlgorithmsProtein Interaction MapsDatabases, ProteinHumansLikelihood FunctionsProtein BindingProtein Interaction MappingProtein MultimerizationProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID23438732
PMCPMC3675826

What OpenQuestion holds

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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.