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Motif-All: discovering all phosphorylation motifs

BACKGROUND: Phosphorylation motifs represent common patterns around the phosphorylation site. The discovery of such kinds of motifs reveals the underlying regulation mechanism and facilitates the prediction of unknown phosphorylation event. To date, people have gathered large amounts of phosphorylat...

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Autores principales: He, Zengyou, Yang, Can, Guo, Guangyu, Li, Ning, Yu, Weichuan
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044277/
https://www.ncbi.nlm.nih.gov/pubmed/21342552
http://dx.doi.org/10.1186/1471-2105-12-S1-S22
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author He, Zengyou
Yang, Can
Guo, Guangyu
Li, Ning
Yu, Weichuan
author_facet He, Zengyou
Yang, Can
Guo, Guangyu
Li, Ning
Yu, Weichuan
author_sort He, Zengyou
collection PubMed
description BACKGROUND: Phosphorylation motifs represent common patterns around the phosphorylation site. The discovery of such kinds of motifs reveals the underlying regulation mechanism and facilitates the prediction of unknown phosphorylation event. To date, people have gathered large amounts of phosphorylation data, making it possible to perform substrate-driven motif discovery using data mining techniques. RESULTS: We describe an algorithm called Motif-All that is able to efficiently identify all statistically significant motifs. The proposed method explores a support constraint to reduce search space and avoid generating random artifacts. As the number of phosphorylated peptides are far less than that of unphosphorylated ones, we divide the mining process into two stages: The first step generates candidates from the set of phosphorylated sequences using only support constraint and the second step tests the statistical significance of each candidate using the odds ratio derived from the whole data set. Experimental results on real data show that Motif-All outperforms current algorithms in terms of both effectiveness and efficiency. CONCLUSIONS: Motif-All is a useful tool for discovering statistically significant phosphorylation motifs. Source codes and data sets are available at: http://bioinformatics.ust.hk/MotifAll.rar.
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spelling pubmed-30442772011-02-25 Motif-All: discovering all phosphorylation motifs He, Zengyou Yang, Can Guo, Guangyu Li, Ning Yu, Weichuan BMC Bioinformatics Research BACKGROUND: Phosphorylation motifs represent common patterns around the phosphorylation site. The discovery of such kinds of motifs reveals the underlying regulation mechanism and facilitates the prediction of unknown phosphorylation event. To date, people have gathered large amounts of phosphorylation data, making it possible to perform substrate-driven motif discovery using data mining techniques. RESULTS: We describe an algorithm called Motif-All that is able to efficiently identify all statistically significant motifs. The proposed method explores a support constraint to reduce search space and avoid generating random artifacts. As the number of phosphorylated peptides are far less than that of unphosphorylated ones, we divide the mining process into two stages: The first step generates candidates from the set of phosphorylated sequences using only support constraint and the second step tests the statistical significance of each candidate using the odds ratio derived from the whole data set. Experimental results on real data show that Motif-All outperforms current algorithms in terms of both effectiveness and efficiency. CONCLUSIONS: Motif-All is a useful tool for discovering statistically significant phosphorylation motifs. Source codes and data sets are available at: http://bioinformatics.ust.hk/MotifAll.rar. BioMed Central 2011-02-15 /pmc/articles/PMC3044277/ /pubmed/21342552 http://dx.doi.org/10.1186/1471-2105-12-S1-S22 Text en Copyright ©2011 He et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
He, Zengyou
Yang, Can
Guo, Guangyu
Li, Ning
Yu, Weichuan
Motif-All: discovering all phosphorylation motifs
title Motif-All: discovering all phosphorylation motifs
title_full Motif-All: discovering all phosphorylation motifs
title_fullStr Motif-All: discovering all phosphorylation motifs
title_full_unstemmed Motif-All: discovering all phosphorylation motifs
title_short Motif-All: discovering all phosphorylation motifs
title_sort motif-all: discovering all phosphorylation motifs
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044277/
https://www.ncbi.nlm.nih.gov/pubmed/21342552
http://dx.doi.org/10.1186/1471-2105-12-S1-S22
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