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Molecular dissection of Wnt3a-Frizzled8 interaction reveals essential and modulatory determinants of Wnt signaling activity

Overview of attention for article published in BMC Biology, May 2014
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Title
Molecular dissection of Wnt3a-Frizzled8 interaction reveals essential and modulatory determinants of Wnt signaling activity
Published in
BMC Biology, May 2014
DOI 10.1186/1741-7007-12-44
Pubmed ID
Authors

Sumit Kumar, Mihaela Žigman, Trushar R Patel, Benjamin Trageser, Julia Christina Gross, Karolin Rahm, Michael Boutros, Dietmar Gradl, Herbert Steinbeisser, Thomas Holstein, Jörg Stetefeld, Suat Özbek

Abstract

Wnt proteins are a family of secreted signaling molecules that regulate key developmental processes in metazoans. The molecular basis of Wnt binding to Frizzled and LRP5/6 co-receptors has long been unknown due to the lack of structural data on Wnt ligands. Only recently, the crystal structure of the Wnt8-Frizzled8-cysteine-rich-domain (CRD) complex was solved, but the significance of interaction sites that influence Wnt signaling has not been assessed.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 63 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Germany 2 3%
Unknown 61 97%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 16 25%
Researcher 10 16%
Student > Bachelor 8 13%
Student > Master 8 13%
Student > Doctoral Student 4 6%
Other 9 14%
Unknown 8 13%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 30 48%
Agricultural and Biological Sciences 15 24%
Medicine and Dentistry 3 5%
Chemistry 3 5%
Neuroscience 2 3%
Other 2 3%
Unknown 8 13%