Literature DB >> 15022646

Reduced bio basis function neural network for identification of protein phosphorylation sites: comparison with pattern recognition algorithms.

Emily A Berry1, Andrew R Dalby, Zheng Rong Yang.   

Abstract

Protein phosphorylation is a post-translational modification performed by a group of enzymes known as the protein kinases or phosphotransferases (Enzyme Commission classification 2.7). It is essential to the correct functioning of both proteins and cells, being involved with enzyme control, cell signalling and apoptosis. The major problem when attempting prediction of these sites is the broad substrate specificity of the enzymes. This study employs back-propagation neural networks (BPNNs), the decision tree algorithm C4.5 and the reduced bio-basis function neural network (rBBFNN) to predict phosphorylation sites. The aim is to compare prediction efficiency of the three algorithms for this problem, and examine knowledge extraction capability. All three algorithms are effective for phosphorylation site prediction. Results indicate that rBBFNN is the fastest and most sensitive of the algorithms. BPNN has the highest area under the ROC curve and is therefore the most robust, and C4.5 has the highest prediction accuracy. C4.5 also reveals the amino acid 2 residues upstream from the phosporylation site is important for serine/threonine phosphorylation, whilst the amino acid 3 residues upstream is important for tyrosine phosphorylation.

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Year:  2004        PMID: 15022646     DOI: 10.1016/j.compbiolchem.2003.11.005

Source DB:  PubMed          Journal:  Comput Biol Chem        ISSN: 1476-9271            Impact factor:   2.877


  9 in total

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Journal:  Bioinformatics       Date:  2005-03-29       Impact factor: 6.937

Review 2.  Peptide bioinformatics: peptide classification using peptide machines.

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Journal:  Methods Mol Biol       Date:  2008

3.  Prediction of human disease-associated phosphorylation sites with combined feature selection approach and support vector machine.

Authors:  Xiaoyi Xu; Ao Li; Minghui Wang
Journal:  IET Syst Biol       Date:  2015-08       Impact factor: 1.615

4.  dbPTM: an information repository of protein post-translational modification.

Authors:  Tzong-Yi Lee; Hsien-Da Huang; Jui-Hung Hung; Hsi-Yuan Huang; Yuh-Shyong Yang; Tzu-Hao Wang
Journal:  Nucleic Acids Res       Date:  2006-01-01       Impact factor: 16.971

5.  KinasePhos: a web tool for identifying protein kinase-specific phosphorylation sites.

Authors:  Hsien-Da Huang; Tzong-Yi Lee; Shih-Wei Tzeng; Jorng-Tzong Horng
Journal:  Nucleic Acids Res       Date:  2005-07-01       Impact factor: 16.971

6.  Characterizing the microenvironment surrounding phosphorylated protein sites.

Authors:  Shi Cai Fan; Xue Gong Zhang
Journal:  Genomics Proteomics Bioinformatics       Date:  2005-11       Impact factor: 7.691

7.  KinasePhos 2.0: a web server for identifying protein kinase-specific phosphorylation sites based on sequences and coupling patterns.

Authors:  Yung-Hao Wong; Tzong-Yi Lee; Han-Kuen Liang; Chia-Mao Huang; Ting-Yuan Wang; Yi-Huan Yang; Chia-Huei Chu; Hsien-Da Huang; Ming-Tat Ko; Jenn-Kang Hwang
Journal:  Nucleic Acids Res       Date:  2007-05-21       Impact factor: 16.971

8.  Meta-prediction of phosphorylation sites with weighted voting and restricted grid search parameter selection.

Authors:  Ji Wan; Shuli Kang; Chuanning Tang; Jianhua Yan; Yongliang Ren; Jie Liu; Xiaolian Gao; Arindam Banerjee; Lynda B M Ellis; Tongbin Li
Journal:  Nucleic Acids Res       Date:  2008-01-30       Impact factor: 16.971

9.  The PROSECCO server for chemical shift predictions in ordered and disordered proteins.

Authors:  Máximo Sanz-Hernández; Alfonso De Simone
Journal:  J Biomol NMR       Date:  2017-11-08       Impact factor: 2.835

  9 in total

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