Evidence map›Paper›PMID 17937820›Full record

ArticleBMC bioinformatics2007

On the detection of functionally coherent groups of protein domains with an extension to protein annotation.

William A McLaughlin, Ken Chen, Tingjun Hou, Wei Wang

Open access · goldAbstract read
In one paragraph

Article in BMC bioinformatics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.1field-weighted citation impact, top 45% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

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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 at 2 institutions in 1 country.

William A McLaughlinDepartment of Chemistry and Biochemistry, Center for Theoretical Biological Physics, University of California, San Diego, 9500 Gilman Drive La Jolla, CA 92093-0359, USA. wimclaug@ucsd.edu
Ken Chen
Tingjun Hou
Wei Wang
Center for Theoretical Biological Physics · USUniversity of California, San Diego · US

Funding

HEMOGLOBIN AND BLOOD PROTEIN CHEMISTRYT32DK007233 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1986 to 2012
$4.6M
NIDDK NIH HHS 5 T32DK07233NIDDK NIH HHS T32 DK007233
6 · The paper itself

Abstract

backgroundProtein domains coordinate to perform multifaceted cellular functions, and domain combinations serve as the functional building blocks of the cell. The available methods to identify functional domain combinations are limited in their scope, e.g. to the identification of combinations falling within individual proteins or within specific regions in a translated genome. Further effort is needed to identify groups of domains that span across two or more proteins and are linked by a cooperative function. Such functional domain combinations can be useful for protein annotation.

resultsUsing a new computational method, we have identified 114 groups of domains, referred to as domain assembly units (DASSEM units), in the proteome of budding yeast Saccharomyces cerevisiae. The units participate in many important cellular processes such as transcription regulation, translation initiation, and mRNA splicing. Within the units the domains were found to function in a cooperative manner; and each domain contributed to a different aspect of the unit's overall function. The member domains of DASSEM units were found to be significantly enriched among proteins contained in transcription modules, defined as genes sharing similar expression profiles and presumably similar functions. The observation further confirmed the functional coherence of DASSEM units. The functional linkages of units were found in both functionally characterized and uncharacterized proteins, which enabled the assessment of protein function based on domain composition.

conclusionA new computational method was developed to identify groups of domains that are linked by a common function in the proteome of Saccharomyces cerevisiae. These groups can either lie within individual proteins or span across different proteins. We propose that the functional linkages among the domains within the DASSEM units can be used as a non-homology based tool to annotate uncharacterized proteins.

Indexed as

AlgorithmsAmino Acid MotifsDatabases, GeneticDatabases, ProteinForecastingPattern Recognition, AutomatedProtein BindingProtein ConformationProtein Interaction MappingProteinsProtein Structure, TertiaryProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Analysis, ProteinProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID17937820
PMCPMC2151957
OpenAlexW2155870664

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.