Title : Structural analysis of PIM1 kinase complexes with ATP-competitive inhibitors.

Pub. Date : 2017 Oct 17

PMID : 29042609






6 Functional Relationships(s)
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1 Structural analysis of PIM1 kinase complexes with ATP-competitive inhibitors. Adenosine Triphosphate Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens
2 Several studies demonstrated that inhibition of PIM1 activity is an attractive strategy in fighting overexpressing cancers, while distinct structural features of ATP binding pocket make PIM1 an inviting target for the design of selective inhibitors. Adenosine Triphosphate Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens
3 To facilitate development of specific PIM1 inhibitors, in this study we report three crystal structures of ATP-competitive inhibitors at the ATP binding pocket of PIM1. Adenosine Triphosphate Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens
4 To facilitate development of specific PIM1 inhibitors, in this study we report three crystal structures of ATP-competitive inhibitors at the ATP binding pocket of PIM1. Adenosine Triphosphate Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens
5 To facilitate development of specific PIM1 inhibitors, in this study we report three crystal structures of ATP-competitive inhibitors at the ATP binding pocket of PIM1. Adenosine Triphosphate Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens
6 To facilitate development of specific PIM1 inhibitors, in this study we report three crystal structures of ATP-competitive inhibitors at the ATP binding pocket of PIM1. Adenosine Triphosphate Pim-1 proto-oncogene, serine/threonine kinase Homo sapiens