Evidence map›Paper›PMID 17880712›Full record

ArticleBMC bioinformatics2007

A machine learning approach for the identification of odorant binding proteins from sequence-derived properties.

Ganesan Pugalenthi, Ke Tang, P N Suganthan, G Archunan, R Sowdhamini

Abstract 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

11 citing papers in PubMed.

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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

5 authors.

Ganesan PugalenthiSchool of Electrical and Electronic Engineering, Nanyang Technological University, 639798, Singapore. ganesan@ntu.edu.sg
Ke Tang
P N Suganthan
G Archunan
R Sowdhamini

Funding

Wellcome Trust
6 · The paper itself

Abstract

backgroundOdorant binding proteins (OBPs) are believed to shuttle odorants from the environment to the underlying odorant receptors, for which they could potentially serve as odorant presenters. Although several sequence based search methods have been exploited for protein family prediction, less effort has been devoted to the prediction of OBPs from sequence data and this area is more challenging due to poor sequence identity between these proteins.

resultsIn this paper, we propose a new algorithm that uses Regularized Least Squares Classifier (RLSC) in conjunction with multiple physicochemical properties of amino acids to predict odorant-binding proteins. The algorithm was applied to the dataset derived from Pfam and GenDiS database and we obtained overall prediction accuracy of 97.7% (94.5% and 98.4% for positive and negative classes respectively).

conclusionOur study suggests that RLSC is potentially useful for predicting the odorant binding proteins from sequence-derived properties irrespective of sequence similarity. Our method predicts 92.8% of 56 odorant binding proteins non-homologous to any protein in the swissprot database and 97.1% of the 414 independent dataset proteins, suggesting the usefulness of RLSC method for facilitating the prediction of odorant binding proteins from sequence information.

Indexed as

AlgorithmsArtificial IntelligenceModels, ChemicalAmino Acid SequenceBinding SitesComputer SimulationMolecular Sequence DataPattern Recognition, AutomatedProtein BindingProtein Interaction MappingReceptors, OdorantSequence Analysis, Proteinodorant-binding proteinReceptors, Odorant

Identifiers

PMID17880712
PMCPMC2216042

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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.