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mUbiSiDa: A Comprehensive Database for Protein Ubiquitination Sites in Mammals

Overview of attention for article published in PLOS ONE, January 2014
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Title
mUbiSiDa: A Comprehensive Database for Protein Ubiquitination Sites in Mammals
Published in
PLOS ONE, January 2014
DOI 10.1371/journal.pone.0085744
Pubmed ID
Authors

Tong Chen, Tao Zhou, Bing He, Haiyan Yu, Xuejiang Guo, Xiaofeng Song, Jiahao Sha

Abstract

Protein ubiquitination is one of the important post-translational modifications by attaching ubiquitin to specific lysine (K) residues in target proteins, and plays important regulatory roles in many cell processes. Recent studies indicated that abnormal protein ubiquitination have been implicated in many diseases by degradation of many key regulatory proteins including tumor suppressor, oncoprotein, and cell cycle regulator. The detailed information of protein ubiquitination sites is useful for scientists to investigate the mechanism of many cell activities and related diseases.

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The data shown below were compiled from readership statistics for 53 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 53 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 18 34%
Researcher 8 15%
Student > Master 4 8%
Professor > Associate Professor 3 6%
Student > Bachelor 3 6%
Other 5 9%
Unknown 12 23%
Readers by discipline Count As %
Agricultural and Biological Sciences 17 32%
Biochemistry, Genetics and Molecular Biology 16 30%
Chemistry 4 8%
Engineering 2 4%
Medicine and Dentistry 1 2%
Other 1 2%
Unknown 12 23%