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High resolution structure of cleaved Serpin 42 Da from Drosophila melanogaster

Overview of attention for article published in BMC Molecular and Cell Biology, April 2014
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Title
High resolution structure of cleaved Serpin 42 Da from Drosophila melanogaster
Published in
BMC Molecular and Cell Biology, April 2014
DOI 10.1186/1472-6807-14-14
Pubmed ID
Authors

Andrew M Ellisdon, Qingwei Zhang, Michelle A Henstridge, Travis K Johnson, Coral G Warr, Ruby HP Law, James C Whisstock

Abstract

The Drosophila melanogaster Serpin 42 Da gene (previously Serpin 4) encodes a serine protease inhibitor that is capable of remarkable functional diversity through the alternative splicing of four different reactive centre loop exons. Eight protein isoforms of Serpin 42 Da have been identified to date, targeting the protease inhibitor to both different proteases and cellular locations. Biochemical and genetic studies suggest that Serpin 42 Da inhibits target proteases through the classical serpin 'suicide' inhibition mechanism, however the crystal structure of a representative Serpin 42 Da isoform remains to be determined.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 20 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 5%
Ireland 1 5%
Unknown 18 90%

Demographic breakdown

Readers by professional status Count As %
Researcher 5 25%
Student > Bachelor 3 15%
Student > Master 2 10%
Lecturer 1 5%
Other 1 5%
Other 4 20%
Unknown 4 20%
Readers by discipline Count As %
Agricultural and Biological Sciences 6 30%
Biochemistry, Genetics and Molecular Biology 3 15%
Computer Science 2 10%
Nursing and Health Professions 1 5%
Medicine and Dentistry 1 5%
Other 1 5%
Unknown 6 30%