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Crystal Structure of the PIM2 Kinase in Complex with an Organoruthenium Inhibitor

Overview of attention for article published in PLOS ONE, October 2009
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Title
Crystal Structure of the PIM2 Kinase in Complex with an Organoruthenium Inhibitor
Published in
PLOS ONE, October 2009
DOI 10.1371/journal.pone.0007112
Pubmed ID
Authors

Alex N. Bullock, Santina Russo, Ann Amos, Nicholas Pagano, Howard Bregman, Judit É. Debreczeni, Wen Hwa Lee, Frank von Delft, Eric Meggers, Stefan Knapp

Abstract

The serine/threonine kinase PIM2 is highly expressed in human leukemia and lymphomas and has been shown to positively regulate survival and proliferation of tumor cells. Its diverse ATP site makes PIM2 a promising target for the development of anticancer agents. To date our knowledge of catalytic domain structures of the PIM kinase family is limited to PIM1 which has been extensively studied and which shares about 50% sequence identity with PIM2.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 74 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 1 1%
Greece 1 1%
Germany 1 1%
Canada 1 1%
Unknown 70 95%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 17 23%
Researcher 12 16%
Student > Bachelor 9 12%
Other 8 11%
Student > Master 8 11%
Other 8 11%
Unknown 12 16%
Readers by discipline Count As %
Chemistry 20 27%
Agricultural and Biological Sciences 17 23%
Biochemistry, Genetics and Molecular Biology 8 11%
Medicine and Dentistry 6 8%
Pharmacology, Toxicology and Pharmaceutical Science 3 4%
Other 3 4%
Unknown 17 23%