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Macromolecular juggling by ubiquitylation enzymes

Overview of attention for article published in BMC Biology, June 2013
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Title
Macromolecular juggling by ubiquitylation enzymes
Published in
BMC Biology, June 2013
DOI 10.1186/1741-7007-11-65
Pubmed ID
Authors

Sonja Lorenz, Aaron J Cantor, Michael Rape, John Kuriyan

Abstract

The posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins is accomplished by the sequential action of E1, E2, and E3 enzymes. Members of the E1 and E3 enzyme families can undergo particularly large conformational changes during their catalytic cycles, involving the remodeling of domain interfaces. This enables the efficient, directed and regulated handover of ubiquitin from one carrier to the next one. We review some of these conformational transformations, as revealed by crystallographic studies.

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Mendeley readers

The data shown below were compiled from readership statistics for 83 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 1%
Netherlands 1 1%
India 1 1%
Unknown 80 96%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 24 29%
Researcher 14 17%
Student > Master 8 10%
Student > Bachelor 5 6%
Other 4 5%
Other 13 16%
Unknown 15 18%
Readers by discipline Count As %
Agricultural and Biological Sciences 28 34%
Biochemistry, Genetics and Molecular Biology 22 27%
Chemistry 11 13%
Nursing and Health Professions 1 1%
Unspecified 1 1%
Other 4 5%
Unknown 16 19%