Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3 - Test2 - elhamkhani - TriplyDB

Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

http://www.wikidata.org/entity/Q27652994

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Structure of anticancer ruthenium half-sandwich complex bound to glycogen synthase kinase 3β Structurally Sophisticated Octahedral Metal Complexes as Highly Selective Protein Kinase Inhibitors An Organometallic Inhibitor for the Human Repair Enzyme 7,8-Dihydro-8-oxoguanosine Triphosphatase PIM1 kinase as a target for cancer therapy Insights into protein kinase regulation and inhibition by large scale structural comparison Allosteric regulation of glycogen synthase kinase 3β: a theoretical study.Small-Molecule Inhibitors of GSK-3: Structural Insights and Their Application to Alzheimer's Disease Models GSK3β inhibition blocks melanoma cell/host interactions by downregulating N-cadherin expression and decreasing FAK phosphorylation.Application of metal coordination chemistry to explore and manipulate cell biology.From imide to lactam metallo-pyridocarbazoles: distinct scaffolds for the design of selective protein kinase inhibitors.Marine pyrrolocarbazoles and analogues: synthesis and kinase inhibition.Tuning heavy metal compounds for anti-tumor activity: is diversity the key to ruthenium's success?Anticancer metallodrug research analytically painting the "omics" picture--current developments and future trends.The induction of mitochondria-mediated apoptosis in cancer cells by ruthenium(II) asymmetric complexes.New organometallic imines of rhenium(i) as potential ligands of GSK-3β: synthesis, characterization and biological studies.Organoruthenium antagonists of human A₃ adenosine receptors.Assessing protein-ligand docking for the binding of organometallic compounds to proteins.Pharmacophore Modeling, Ensemble Docking, Virtual Screening, and Biological Evaluation on Glycogen Synthase Kinase-3β.Metal complexes as "protein surface mimetics".Role of bridging water molecules in GSK3β-inhibitor complexes: insights from QM/MM, MD, and molecular docking studies.Synthesis and evaluation of metallocene containing methylidene-1,3-dihydro-2H-indol-2-ones as kinase inhibitors.Metal Compounds as Kinase and Phosphatase Inhibitors in Drug Development: The Role of the Metal and Ligands

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P2860

Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

http://www.wikidata.org/entity/Q27652994

description

2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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Extremely Tight Binding of a Ruthenium Complex to Glycogen Synthase Kinase 3

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G Ekin Atilla-Gokcumen

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Jasna Maksimoska

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Nicholas Pagano

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P2860

Structural insights and biological effects of glycogen synthase kinase 3-specific inhibitor AR-A014418

Structural characterization of the GSK-3beta active site using selective and non-selective ATP-mimetic inhibitors

GSK-3-selective inhibitors derived from Tyrian purple indirubins

Novel bis(indolyl)maleimide pyridinophanes that are potent, selective inhibitors of glycogen synthase kinase-3

Ruthenium half-sandwich complexes as protein kinase inhibitors: derivatization of the pyridocarbazole pharmacophore ligand

Structure-Based Design of an Organoruthenium Phosphatidyl-inositol-3-kinase Inhibitor Reveals a Switch Governing Lipid Kinase Potency and Selectivity

Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction

Ruthenium half-sandwich complexes bound to protein kinase Pim-1

Exploring biologically relevant chemical space with metal complexes

Ruthenium half-sandwich complexes as protein kinase inhibitors: an N-succinimidyl ester for rapid derivatizations of the cyclopentadienyl moiety.

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2933-6

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10.1002/CBIC.200800489

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18

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9

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Panagis Filippakopoulos

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2008-12-15T00:00:00Z

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19035373

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4094351

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