Linked Life Data

20939820

Source:http://linkedlifedata.com/resource/pubmed/id/20939820

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2010-12-14
pubmed:abstractText
The Pim (provirus insertion site of Moloney murine leukemia virus) family of serine/threonine protein kinases possesses the fundamental characteristics critical for the biology of eukaryotes, in particular, survival and malignant transformation of cells. The members of this protein family (Pim-1 to Pim-3) are aberrantly expressed in human tumors, most frequently in prostate cancer and hematological malignancies. Therefore, Pim proteins are widely considered as attractive targets in cancer chemotherapy. Growing knowledge of mechanisms of Pim-mediated anti-apoptosis and transformation, as well as rapid progress in the design of Pim-modulating compounds dictate the need for an in-depth analysis of the chemistry of inhibitors and the modes of their interaction with these protein kinases. This review summarizes recent advances in understanding the molecular events regulated by Pim proteins. In addition, we focus on the non-patent literature (mostly since 2005) that demonstrates a diversity of chemical classes of small molecular weight Pim inhibitors. The X-ray co-crystal structures of complexes Pim:inhibitor provide evidence for SAR data important for the choice of synthetic routes, optimization of lead compounds and testing chemical libraries. We also discuss a cell-based test system useful for rapid and inexpensive pre-screening of compounds capable of preventing Pim-mediated phosphorylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1875-533X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4114-33
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Fighting tumor cell survival: advances in the design and evaluation of Pim inhibitors.
pubmed:affiliation
Clermont Université, Université Blaise Pascal, Laboratoire SEESIB, BP 10448, F-63000 Clermont-Ferrand, France. Fabrice.ANIZON@univ-bpclermont.fr
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't