Literature DB >> 21551145

Exploiting maximal dependence decomposition to identify conserved motifs from a group of aligned signal sequences.

Tzong-Yi Lee1, Zong-Qing Lin, Sheng-Jen Hsieh, Neil Arvin Bretaña, Cheng-Tsung Lu.   

Abstract

UNLABELLED: Bioinformatics research often requires conservative analyses of a group of sequences associated with a specific biological function (e.g. transcription factor binding sites, micro RNA target sites or protein post-translational modification sites). Due to the difficulty in exploring conserved motifs on a large-scale sequence data involved with various signals, a new method, MDDLogo, is developed. MDDLogo applies maximal dependence decomposition (MDD) to cluster a group of aligned signal sequences into subgroups containing statistically significant motifs. In order to extract motifs that contain a conserved biochemical property of amino acids in protein sequences, the set of 20 amino acids is further categorized according to their physicochemical properties, e.g. hydrophobicity, charge or molecular size. MDDLogo has been demonstrated to accurately identify the kinase-specific substrate motifs in 1221 human phosphorylation sites associated with seven well-known kinase families from Phospho.ELM. Moreover, in a set of plant phosphorylation data-lacking kinase information, MDDLogo has been applied to help in the investigation of substrate motifs of potential kinases and in the improvement of the identification of plant phosphorylation sites with various substrate specificities. In this study, MDDLogo is comparable with another well-known motif discover tool, Motif-X. CONTACT: francis@saturn.yzu.edu.tw

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Year:  2011        PMID: 21551145     DOI: 10.1093/bioinformatics/btr291

Source DB:  PubMed          Journal:  Bioinformatics        ISSN: 1367-4803            Impact factor:   6.937


  39 in total

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3.  EuLoc: a web-server for accurately predict protein subcellular localization in eukaryotes by incorporating various features of sequence segments into the general form of Chou's PseAAC.

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4.  BioSeq-Analysis2.0: an updated platform for analyzing DNA, RNA and protein sequences at sequence level and residue level based on machine learning approaches.

Authors:  Bin Liu; Xin Gao; Hanyu Zhang
Journal:  Nucleic Acids Res       Date:  2019-11-18       Impact factor: 16.971

5.  LncRNA-Encoded Short Peptides Identification Using Feature Subset Recombination and Ensemble Learning.

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Journal:  Interdiscip Sci       Date:  2021-07-25       Impact factor: 2.233

6.  SNOSite: exploiting maximal dependence decomposition to identify cysteine S-nitrosylation with substrate site specificity.

Authors:  Tzong-Yi Lee; Yi-Ju Chen; Tsung-Cheng Lu; Hsien-Da Huang; Yu-Ju Chen
Journal:  PLoS One       Date:  2011-07-15       Impact factor: 3.240

7.  Investigation and identification of protein γ-glutamyl carboxylation sites.

Authors:  Tzong-Yi Lee; Cheng-Tsung Lu; Shu-An Chen; Neil Arvin Bretaña; Tzu-Hsiu Cheng; Min-Gang Su; Kai-Yao Huang
Journal:  BMC Bioinformatics       Date:  2011-11-30       Impact factor: 3.169

8.  PlantPhos: using maximal dependence decomposition to identify plant phosphorylation sites with substrate site specificity.

Authors:  Tzong-Yi Lee; Neil Arvin Bretaña; Cheng-Tsung Lu
Journal:  BMC Bioinformatics       Date:  2011-06-26       Impact factor: 3.169

9.  Identifying protein phosphorylation sites with kinase substrate specificity on human viruses.

Authors:  Neil Arvin Bretaña; Cheng-Tsung Lu; Chiu-Yun Chiang; Min-Gang Su; Kai-Yao Huang; Tzong-Yi Lee; Shun-Long Weng
Journal:  PLoS One       Date:  2012-07-23       Impact factor: 3.240

10.  DbPTM 3.0: an informative resource for investigating substrate site specificity and functional association of protein post-translational modifications.

Authors:  Cheng-Tsung Lu; Kai-Yao Huang; Min-Gang Su; Tzong-Yi Lee; Neil Arvin Bretaña; Wen-Chi Chang; Yi-Ju Chen; Yu-Ju Chen; Hsien-Da Huang
Journal:  Nucleic Acids Res       Date:  2012-11-27       Impact factor: 16.971

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