BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo. - Test2 - elhamkhani - TriplyDB

BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo.

BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo.

http://www.wikidata.org/entity/Q34575151

about

Polo-like kinase-1 controls Aurora A destruction by activating APC/C-Cdh1 Computational analysis of phosphopeptide binding to the polo-box domain of the mitotic kinase PLK1 using molecular dynamics simulation Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells Polo-like kinase is required for synaptonemal complex disassembly and phosphorylation in mouse spermatocytes The novel mouse Polo-like kinase 5 responds to DNA damage and localizes in the nucleolus Pharmacological inhibition of BMK1 suppresses tumor growth through promyelocytic leukemia protein Phosphorylation by polo-like kinase 1 induces the tumor-suppressing activity of FADD Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4 triggers centriole duplication Polo-like kinase 1 is involved in hepatitis C virus replication by hyperphosphorylating NS5A Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a phosphatase-independent manner Plk1-dependent recruitment of gamma-tubulin complexes to mitotic centrosomes involves multiple PCM components A genome-wide RNAi screen identifies multiple synthetic lethal interactions with the Ras oncogene A panel of isogenic human cancer cells suggests a therapeutic approach for cancers with inactivated p53 Targeting protein serine/threonine phosphatases for drug development PLK-1 Targeted Inhibitors and Their Potential against Tumorigenesis Putting a bit into the polo-box domain of polo-like kinase 1 Volasertib for AML: clinical use and patient consideration Polo-like kinase 1, on the rise from cell cycle regulation to prostate cancer development Discovery and development of the Polo-like kinase inhibitor volasertib in cancer therapy Molecular dynamics of PLK1 during mitosis A high-content small molecule screen identifies sensitivity of glioblastoma stem cells to inhibition of polo-like kinase 1 The Plk1 inhibitor BI 2536 temporarily arrests primary cardiac fibroblasts in mitosis and generates aneuploidy in vitro Plk1 inhibition causes post-mitotic DNA damage and senescence in a range of human tumor cell lines PP2A-twins is antagonized by greatwall and collaborates with polo for cell cycle progression and centrosome attachment to nuclei in drosophila embryos Small-molecule kinase inhibitors provide insight into Mps1 cell cycle function Acetyl-lysine Binding Site of Bromodomain-Containing Protein 4 (BRD4) Interacts with Diverse Kinase Inhibitors Dual kinase-bromodomain inhibitors for rationally designed polypharmacology Selective and brain-permeable polo-like kinase-2 (Plk-2) inhibitors that reduce α-synuclein phosphorylation in rat brain PLK1, A Potential Target for Cancer Therapy Polo-like kinase 1 licenses CENP-A deposition at centromeres Current prospects for RNA interference-based therapies A mitotic phosphorylation feedback network connects Cdk1, Plk1, 53BP1, and Chk2 to inactivate the G(2)/M DNA damage checkpoint A series of beta-carboline derivatives inhibit the kinase activity of PLKs A simple high-content cell cycle assay reveals frequent discrepancies between cell number and ATP and MTS proliferation assays Targeting Echinococcus multilocularis stem cells by inhibition of the Polo-like kinase EmPlk1 Robust Classification of Small-Molecule Mechanism of Action Using a Minimalist High-Content Microscopy Screen and Multidimensional Phenotypic Trajectory Analysis Structure-Bioactivity Relationship for Benzimidazole Thiophene Inhibitors of Polo-Like Kinase 1 (PLK1), a Potential Drug Target in Schistosoma mansoni Identification of Polo-like kinase 1 interaction inhibitors using a novel cell-based assay Drug Discovery Targeting Bromodomain-Containing Protein 4.

P2860

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P2860

BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo.

http://www.wikidata.org/entity/Q34575151

description

2007 nî lūn-bûn

@nan

2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի փետրվարին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

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BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

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BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

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type

label

BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

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BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

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BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

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prefLabel

BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

@ast

BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

@en

BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo.

@nl

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J.CUB.2006.12.037

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Current Biology

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BI 2536, a potent and selectiv ...... inhibits tumor growth in vivo

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Anke Baum

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Günther R Adolf

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Jan-Michael Peters

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Jens Quant

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Norbert Kraut

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316-322

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10.1016/J.CUB.2006.12.037

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4

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17

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Mark Petronczki

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2007-02-08T00:00:00Z

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6512960

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