Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase. - Wikidata - wikimedia - TriplyDB

Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase.

Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase.

http://www.wikidata.org/entity/Q45138630

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Crystal structure of the PIM2 kinase in complex with an organoruthenium inhibitor Structural and functional diversity of the microbial kinome Proto-oncogene, Pim-3 with serine/threonine kinase activity, is aberrantly expressed in human colon cancer cells and can prevent Bad-mediated apoptosis 14-3-3 Binding to Pim-phosphorylated Ser166 and Ser186 of human Mdm2--Potential interplay with the PKB/Akt pathway and p14(ARF)PIM serine/threonine kinases in the pathogenesis and therapy of hematologic malignancies and solid cancers Cryptic promoter activity in the DNA sequence corresponding to the pim-1 5'-UTR Evolution of CASK into a Mg2+-sensitive kinase Targeting the Pim kinases in multiple myeloma Design principles underpinning the regulatory diversity of protein kinases Pim Kinases Promote Migration and Metastatic Growth of Prostate Cancer Xenografts Tricyclic Benzo[cd]azulenes selectively inhibit activities of Pim kinases and restrict growth of Epstein-Barr virus-transformed cells Flexibility of the P-loop of Pim-1 kinase: observation of a novel conformation induced by interaction with an inhibitor 7,8-Dichloro-1-oxo-β-carbolines as a Versatile Scaffold for the Development of Potent and Selective Kinase Inhibitors with Unusual Binding Modes Crystal Structure of Pim1 Kinase in Complex with a Pyrido[4,3-D]Pyrimidine Derivative Suggests a Unique Binding Mode Non-ATP-Mimetic Organometallic Protein Kinase Inhibitor Structure Guided Optimization, in Vitro Activity, and in Vivo Activity of Pan-PIM Kinase Inhibitors PIM1 kinase phosphorylates the human transcription factor FOXP3 at serine 422 to negatively regulate its activity under inflammation Targeting Pim kinases for cancer treatment: opportunities and challenges The PIM kinases in hematological cancers PIM1 kinase as a target for cancer therapy Pim kinase inhibitors: a survey of the patent literature Small molecule inhibitors of PIM1 kinase: July 2009 to February 2013 patent update Conservation, variability and the modeling of active protein kinases Accelerated evolution of PAK3- and PIM1-like kinase gene families in the zebra finch, Taeniopygia guttata Pim3 negatively regulates glucose-stimulated insulin secretion Pim-selective inhibitor DHPCC-9 reveals Pim kinases as potent stimulators of cancer cell migration and invasion Pim1 promotes human prostate cancer cell tumorigenicity and c-MYC transcriptional activity.Synthesis and evaluation of novel inhibitors of Pim-1 and Pim-2 protein kinases.In vitro evaluation of dihydropyridine-3-carbonitriles as potential cytotoxic agents through PIM-1 protein kinase inhibition.Pathophysiological roles of Pim-3 kinase in pancreatic cancer development and progression.Regulation of Skp2 levels by the Pim-1 protein kinase Pim-1 knockdown potentiates paclitaxel-induced apoptosis in human hormone-refractory prostate cancers through inhibition of NHEJ DNA repair.Pim-1 kinase is a target of miR-486-5p and eukaryotic translation initiation factor 4E, and plays a critical role in lung cancer.The oncogenic kinase Pim-1 is modulated by K-Ras signaling and mediates transformed growth and radioresistance in human pancreatic ductal adenocarcinoma cells.Pim1 kinase is upregulated in glioblastoma multiforme and mediates tumor cell survival.Pim-1 kinase phosphorylates and stabilizes 130 kDa FLT3 and promotes aberrant STAT5 signaling in acute myeloid leukemia with FLT3 internal tandem duplication Pim1 kinase is required to maintain tumorigenicity in MYC-expressing prostate cancer cells.Differential regulation of androgen receptor by PIM-1 kinases via phosphorylation-dependent recruitment of distinct ubiquitin E3 ligases.The survival kinases Akt and Pim as potential pharmacological targets.Control of Pim2 kinase stability and expression in transformed human haematopoietic cells

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P2860

Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase.

http://www.wikidata.org/entity/Q45138630

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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Structural basis of constituti ...... ng mode of human Pim-1 kinase.

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Structural basis of constituti ...... ng mode of human Pim-1 kinase.

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type

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Structural basis of constituti ...... ng mode of human Pim-1 kinase.

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Structural basis of constituti ...... ng mode of human Pim-1 kinase.

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Structural basis of constituti ...... ng mode of human Pim-1 kinase.

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Structural basis of constituti ...... ng mode of human Pim-1 kinase.

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Journal of Biological Chemistry

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Structural basis of constituti ...... ng mode of human Pim-1 kinase.

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P2093

Andre White

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Anthony Kronkaitis

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Bennett Farmer

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Charline Peng

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Eugene R Hickey

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Joey Studts

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Jun Li

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Kevin Barringer

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Kevin C Qian

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Lian Wang

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P2860

The protein kinase complement of the human genome

STAT5 as a molecular regulator of proliferation, differentiation and apoptosis in hematopoietic cells.

Mice deficient for all PIM kinases display reduced body size and impaired responses to hematopoietic growth factors

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

The 1.7 A crystal structure of human cell cycle checkpoint kinase Chk1: implications for Chk1 regulation

Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product

A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility

The conformational plasticity of protein kinases

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