Literature DB >> 16731044

Predicting O-glycosylation sites in mammalian proteins by using SVMs.

Sujun Li1, Boshu Liu, Rong Zeng, Yudong Cai, Yixue Li.   

Abstract

O-glycosylation is one of the most important, frequent and complex post-translational modifications. This modification can activate and affect protein functions. Here, we present three support vector machines models based on physical properties, 0/1 system, and the system combining the above two features. The prediction accuracies of the three models have reached 0.82, 0.85 and 0.85, respectively. The accuracies of the three SVMs methods were evaluated by 'leave-one-out' cross validation. This approach provides a useful tool to help identify the O-glycosylation sites in mammalian proteins. An online prediction web server is available at http://www.biosino.org/Oglyc.

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Year:  2006        PMID: 16731044     DOI: 10.1016/j.compbiolchem.2006.02.002

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


  23 in total

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3.  A novel model to predict O-glycosylation sites using a highly unbalanced dataset.

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4.  Incorporating post-translational modifications and unnatural amino acids into high-throughput modeling of protein structures.

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Authors:  Matthew J Troese; Madhubanti Sarkar; Nathan L Galloway; Rachael J Thomas; Sarah A Kearns; Dexter V Reneer; Tian Yang; Jason A Carlyon
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Journal:  Sci Rep       Date:  2018-10-19       Impact factor: 4.379

9.  Prediction of pharmacological and xenobiotic responses to drugs based on time course gene expression profiles.

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10.  Critical role of glycosylation in determining the length and structure of T cell epitopes.

Authors:  Tamás G Szabó; Robin Palotai; Péter Antal; Itay Tokatly; László Tóthfalusi; Ole Lund; György Nagy; András Falus; Edit I Buzás
Journal:  Immunome Res       Date:  2009-09-24
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