The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors - sprookjes - yvandenbroek - TriplyDB

The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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Protein crystallization screens developed at the MRC Laboratory of Molecular Biology PI3K isoform-selective inhibitors: next-generation targeted cancer therapies Idelalisib: First-in-Class PI3K Delta Inhibitor for the Treatment of Chronic Lymphocytic Leukemia, Small Lymphocytic Leukemia, and Follicular Lymphoma Phosphoinositides: tiny lipids with giant impact on cell regulation Shaping Development of Autophagy Inhibitors with the Structure of the Lipid Kinase Vps34 Structure of Lipid Kinase p110β/p85β Elucidates an Unusual SH2-Domain-Mediated Inhibitory Mechanism Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases A highly potent and selective Vps34 inhibitor alters vesicle trafficking and autophagy Discovery and SAR of Novel 2,3-Dihydroimidazo[1,2-c]quinazoline PI3K Inhibitors: Identification of Copanlisib (BAY 80-6946)The function of phosphatidylinositol 5-phosphate 4-kinase γ (PI5P4Kγ) explored using a specific inhibitor that targets the PI5P-binding site Signaling by the phosphoinositide 3-kinase family in immune cells Dynamic steps in receptor tyrosine kinase mediated activation of class IA phosphoinositide 3-kinases (PI3K) captured by H/D exchange (HDX-MS).Alternative splicing promotes tumour aggressiveness and drug resistance in African American prostate cancer.Puquitinib, a novel orally available PI3Kδ inhibitor, exhibits potent antitumor efficacy against acute myeloid leukemia Probing the probes: fitness factors for small molecule tools.Ras/Raf/MEK/ERK and PI3K/PTEN/Akt/mTOR cascade inhibitors: how mutations can result in therapy resistance and how to overcome resistance.A biochemical mechanism for the oncogenic potential of the p110beta catalytic subunit of phosphoinositide 3-kinase.Dominant-activating germline mutations in the gene encoding the PI(3)K catalytic subunit p110δ result in T cell senescence and human immunodeficiency Simultaneous targeting of PI3Kδ and a PI3Kδ-dependent MEK1/2-Erk1/2 pathway for therapy in pediatric B-cell acute lymphoblastic leukemia.Nuclear but not cytosolic phosphoinositide 3-kinase beta has an essential function in cell survival Dynamics of the phosphoinositide 3-kinase p110δ interaction with p85α and membranes reveals aspects of regulation distinct from p110α Dual inhibition of allosteric mitogen-activated protein kinase (MEK) and phosphatidylinositol 3-kinase (PI3K) oncogenic targets with a bifunctional inhibitor Structural, biochemical, and biophysical characterization of idelalisib binding to phosphoinositide 3-kinase δ Thiazolidinedione-based PI3Kα inhibitors: an analysis of biochemical and virtual screening methods.Germline recessive mutations in PI4KA are associated with perisylvian polymicrogyria, cerebellar hypoplasia and arthrogryposis The p110δ subunit of PI3K regulates bone marrow-derived eosinophil trafficking and airway eosinophilia in allergen-challenged mice.Taxifolin suppresses UV-induced skin carcinogenesis by targeting EGFR and PI3K.The Therapeutic Potential for PI3K Inhibitors in Autoimmune Rheumatic Diseases Definition of the binding mode of a new class of phosphoinositide 3-kinase α-selective inhibitors using in vitro mutagenesis of non-conserved amino acids and kinetic analysis.Identification of mammalian target of rapamycin as a direct target of fenretinide both in vitro and in vivo.Discovery of Bifunctional Oncogenic Target Inhibitors against Allosteric Mitogen-Activated Protein Kinase (MEK1) and Phosphatidylinositol 3-Kinase (PI3K)[18F]-FLT positron emission tomography can be used to image the response of sensitive tumors to PI3-kinase inhibition with the novel agent GDC-0941.Discovery of the novel mTOR inhibitor and its antitumor activities in vitro and in vivo.L-Aminoacyl-triazine derivatives are isoform-selective PI3Kβ inhibitors that target non-conserved Asp862 of PI3Kβ Phosphoinositide 3-kinase p110δ promotes lumen formation through the enhancement of apico-basal polarity and basal membrane organization.Potential role of PI3K inhibitors in the treatment of breast cancer.Progress in the preclinical discovery and clinical development of class I and dual class I/IV phosphoinositide 3-kinase (PI3K) inhibitors.Selective PI3Kδ inhibitors, a review of the patent literature.Identifying and testing potential new anti-asthma agents.Structure, function and inhibition of the phosphoinositide 3-kinase p110α enzyme.

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

http://www.wikidata.org/entity/Q27659013

description

2010 nî lūn-bûn

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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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Nature Chemical Biology

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The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

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Alex Berndt

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Benjamin T Houseman

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Christian Rommel

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Daniel D Le

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Fabrice Gorrec

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Jeffrey P Shaw

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Kevan M Shokat

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Matthias K Schwarz

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Olusegun Williams

http://www.w3.org/2001/XMLSchema#string

Pascale Gaillard

http://www.w3.org/2001/XMLSchema#string

P2860

PI3K delta and PI3K gamma: partners in crime in inflammation in rheumatoid arthritis and beyond?

P110delta, a novel phosphoinositide 3-kinase in leukocytes

p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes

Isoform selective phosphoinositide 3-kinase gamma and delta inhibitors and their therapeutic potential

A pharmacological map of the PI3-K family defines a role for p110alpha in insulin signaling

AKT/PKB signaling: navigating downstream

Structural Determinants of Phosphoinositide 3-Kinase Inhibition by Wortmannin, LY294002, Quercetin, Myricetin, and Staurosporine

Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase gamma

Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit

The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations

P2888

P304

117-24

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scholarly article

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5082104

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10.1038/NCHEMBIO.293

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2

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6

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Joseph I Pacold

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2010-02-01T00:00:00Z

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232785814

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1011080093

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20081827

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P932

2880452

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