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The multiple roles of histidine in protein interactions

Overview of attention for article published in BMC Chemistry, March 2013
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Title
The multiple roles of histidine in protein interactions
Published in
BMC Chemistry, March 2013
DOI 10.1186/1752-153x-7-44
Pubmed ID
Authors

Si-Ming Liao, Qi-Shi Du, Jian-Zong Meng, Zong-Wen Pang, Ri-Bo Huang

Abstract

Among the 20 natural amino acids histidine is the most active and versatile member that plays the multiple roles in protein interactions, often the key residue in enzyme catalytic reactions. A theoretical and comprehensive study on the structural features and interaction properties of histidine is certainly helpful.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 528 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 4 <1%
United Kingdom 2 <1%
Colombia 1 <1%
Malaysia 1 <1%
Russia 1 <1%
Poland 1 <1%
Unknown 518 98%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 135 26%
Student > Bachelor 76 14%
Researcher 61 12%
Student > Master 57 11%
Student > Doctoral Student 25 5%
Other 50 9%
Unknown 124 23%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 120 23%
Chemistry 103 20%
Agricultural and Biological Sciences 82 16%
Pharmacology, Toxicology and Pharmaceutical Science 17 3%
Engineering 12 2%
Other 56 11%
Unknown 138 26%