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Protein dynamics and conformational selection in bidirectional signal transduction

Overview of attention for article published in BMC Biology, January 2012
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Title
Protein dynamics and conformational selection in bidirectional signal transduction
Published in
BMC Biology, January 2012
DOI 10.1186/1741-7007-10-2
Pubmed ID
Authors

Ruth Nussinov, Buyong Ma

Abstract

Protein conformational dynamics simultaneously allow promiscuity and specificity in binding. The multiple conformations of the free EphA4 ligand-binding domain observed in two new EphA4 crystal structures provide a unique insight into the conformational dynamics of EphA4 and its signaling pathways. The heterogeneous ensemble and loop dynamics explain how the EphA4 receptor is able to bind multiple A- and B-ephrin ligands and small molecules via conformational selection, which helps to fine-tune cellular signal response in both receptor and ligand cells.

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Mendeley readers

The data shown below were compiled from readership statistics for 65 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 2 3%
Chile 1 2%
Australia 1 2%
Turkey 1 2%
Israel 1 2%
Singapore 1 2%
Argentina 1 2%
United States 1 2%
Unknown 56 86%

Demographic breakdown

Readers by professional status Count As %
Researcher 14 22%
Student > Ph. D. Student 13 20%
Student > Master 8 12%
Professor 5 8%
Student > Bachelor 5 8%
Other 15 23%
Unknown 5 8%
Readers by discipline Count As %
Agricultural and Biological Sciences 24 37%
Biochemistry, Genetics and Molecular Biology 10 15%
Chemistry 9 14%
Physics and Astronomy 3 5%
Computer Science 3 5%
Other 9 14%
Unknown 7 11%