- Abstract:
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BACKGROUND: 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. PRINCIPAL FINDINGS: Here we deter...
Expand abstract - Publication status:
- Published
- Files:
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(pdf, 732.5kb)
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- Publisher copy:
- 10.1371/journal.pone.0007112
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- Publisher:
- Public Library of Science Publisher's website
- Journal:
- PloS one Journal website
- Volume:
- 4
- Issue:
- 10
- Pages:
- Article: e7112
- Publication date:
- 2009
- DOI:
- EISSN:
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1932-6203
- ISSN:
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1932-6203
- URN:
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uuid:75641f80-06c0-4e70-925f-48b0614b6a27
- Source identifiers:
-
34939
- Local pid:
- pubs:34939
- Language:
- English
- Keywords:
- Copyright holder:
- Bullock et al.
- Copyright date:
- 2009
- Notes:
- Copyright 2009 Bullock et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Journal article
Crystal structure of the PIM2 kinase in complex with an organoruthenium inhibitor.
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Canadian Institutes for Health Research
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Canadian Foundation for Innovation
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Ontario Genomics Institute
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GlaxoSmithKline
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Karolinska Institutet
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