Evidence map›Paper›PMID 24872686›Full record

ArticleInternational journal of nanomedicine2014

An ensemble method approach to investigate kinase-specific phosphorylation sites.

Sutapa Datta, Subhasis Mukhopadhyay

Abstract read
In one paragraph

Article in International journal of nanomedicine, 2014. 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
–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

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3 · Its place in the literature

Who cites it

3 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

2 authors.

Sutapa DattaDepartment of Biophysics, Molecular Biology and Bioinformatics and Distributed Information Centre for Bioinformatics, University of Calcutta, West Bengal, India.
Subhasis MukhopadhyayDepartment of Biophysics, Molecular Biology and Bioinformatics and Distributed Information Centre for Bioinformatics, University of Calcutta, West Bengal, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphorylation is one of the most significant and well-studied post-translational modifications, and it plays an important role in various cellular processes. It has made a considerable impact in understanding the protein functions which are involved in revealing signal transductions and various diseases. The identification of kinase-specific phosphorylation sites has an important role in elucidating the mechanism of phosphorylation; however, experimental techniques for identifying phosphorylation sites are labor intensive and expensive. An exponentially increasing number of protein sequences generated by various laboratories across the globe require computer-aided procedures for reliably and quickly identifying the phosphorylation sites, opening a new horizon for in silico analysis. In this regard, we have introduced a novel ensemble method where we have selected three classifiers (least square support vector machine, multilayer perceptron, and k-Nearest Neighbor) and three different feature encoding parameters (dipeptide composition, physicochemical properties of amino acids, and protein-protein similarity score). Each of these classifiers is trained on each of the three different parameter systems. The final results of the ensemble method are obtained by fusing the results of all the classifiers by a weighted voting algorithm. Extensive experiments reveal that our proposed method can successfully predict phosphorylation sites in a kinase-specific manner and performs significantly better when compared with other existing phosphorylation site prediction methods.

Indexed as

AlgorithmsAmino AcidsAmino Acid SequenceEnzyme ActivationMolecular Sequence DataPattern Recognition, AutomatedPhosphatesPhosphorylationPhosphotransferasesProtein Interaction MappingSequence Analysis, ProteinSubstrate SpecificityAmino AcidsPhosphatesPhosphotransferasescell signalingphosphatepost-translational modification

Identifiers

PMID24872686
PMCPMC4026567

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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.