Title |
Characterization and identification of protein O-GlcNAcylation sites with substrate specificity
|
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Published in |
BMC Bioinformatics, December 2014
|
DOI | 10.1186/1471-2105-15-s16-s1 |
Pubmed ID | |
Authors |
Hsin-Yi Wu, Cheng-Tsung Lu, Hui-Ju Kao, Yi-Ju Chen, Yu-Ju Chen, Tzong-Yi Lee |
Abstract |
Protein O-GlcNAcylation, involving the attachment of single N-acetylglucosamine (GlcNAc) to the hydroxyl group of serine or threonine residues. Elucidation of O-GlcNAcylation sites on proteins is required in order to decipher its crucial roles in regulating cellular processes and aid in drug design. With an increasing number of O-GlcNAcylation sites identified by mass spectrometry (MS)-based proteomics, several methods have been proposed for the computational identification of O-GlcNAcylation sites. However, no development that focuses on the investigation of O-GlcNAcylated substrate motifs has existed. Thus, we were motivated to design a new method for the identification of protein O-GlcNAcylation sites with the consideration of substrate site specificity. |
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Unknown | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 24 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 8 | 33% |
Student > Master | 4 | 17% |
Student > Ph. D. Student | 4 | 17% |
Student > Bachelor | 2 | 8% |
Student > Postgraduate | 2 | 8% |
Other | 3 | 13% |
Unknown | 1 | 4% |
Readers by discipline | Count | As % |
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Agricultural and Biological Sciences | 6 | 25% |
Computer Science | 3 | 13% |
Medicine and Dentistry | 2 | 8% |
Nursing and Health Professions | 1 | 4% |
Other | 3 | 13% |
Unknown | 2 | 8% |