Evidence map›Paper›PMID 14525624›Full record

ArticleBMC evolutionary biology2003

Apparent dependence of protein evolutionary rate on number of interactions is linked to biases in protein-protein interactions data sets.

Jesse D Bloom, Christoph Adami

Open access · goldAbstract read
In one paragraph

Article in BMC evolutionary biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

64 citing papers in PubMed, 139 citations in OpenAlex.

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  16. Hsp90 promotes kinase evolution.Molecular biology and evolution · 2015
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4 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Jesse D BloomDepartment of Chemistry and Digital Life Laboratory, 210-41, California Institute of Technology, Pasadena, CA 91125, USA. bloom@caltech.edu
Christoph Adami
California Institute of Technology · USJet Propulsion Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSeveral studies have suggested that proteins that interact with more partners evolve more slowly. The strength and validity of this association has been called into question. Here we investigate how biases in high-throughput protein-protein interaction studies could lead to a spurious correlation.

resultsWe examined the correlation between evolutionary rate and the number of protein-protein interactions for sets of interactions determined by seven different high-throughput methods in Saccharomyces cerevisiae. Some methods have been shown to be biased towards counting more interactions for abundant proteins, a fact that could be important since abundant proteins are known to evolve more slowly. We show that the apparent tendency for interactive proteins to evolve more slowly varies directly with the bias towards counting more interactions for abundant proteins. Interactions studies with no bias show no correlation between evolutionary rate and the number of interactions, and the one study biased towards counting fewer interactions for abundant proteins actually suggests that interactive proteins evolve more rapidly. In all cases, controlling for protein abundance significantly decreases the observed correlation between interactions and evolutionary rate. Finally, we disprove the hypothesis that small data set size accounts for the failure of some interactions studies to show a correlation between evolutionary rate and the number of interactions.

conclusionsThe only correlation supported by a careful analysis of the data is between evolutionary rate and protein abundance. The reported correlation between evolutionary rate and protein-protein interactions cannot be separated from the biases of some protein-protein interactions studies to count more interactions for abundant proteins.

Indexed as

Biological EvolutionBacterial ProteinsComputational BiologyGene Expression ProfilingMacromolecular SubstancesOligonucleotide Array Sequence AnalysisProteinsResearch DesignSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesBacterial ProteinsMacromolecular SubstancesProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID14525624
PMCPMC270031
OpenAlexW1918164078

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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.