NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses - Wikidata - wikimedia - TriplyDB

NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses

NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses

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The X-ray Structure of RU486 Bound to the Progesterone Receptor in a Destabilized Agonistic Conformation Coupling of receptor conformation and ligand orientation determine graded activity Structural and mechanistic insights into bisphenols action provide guidelines for risk assessment and discovery of bisphenol A substitutes Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases Development of Selective Estrogen Receptor Modulator (SERM)-Like Activity Through an Indirect Mechanism of Estrogen Receptor Antagonism: Defining the Binding Mode of 7-Oxabicyclo[2.2.1]hept-5-ene Scaffold Core Ligands X-ray Structures of Progesterone Receptor Ligand Binding Domain in Its Agonist State Reveal Differing Mechanisms for Mixed Profiles of 11 -Substituted Steroids Resveratrol modulates the inflammatory response via an estrogen receptor-signal integration network Unprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits ESR1 ligand-binding domain mutations in hormone-resistant breast cancer.Antiestrogens: structure-activity relationships and use in breast cancer treatment Predictive features of ligand-specific signaling through the estrogen receptor Monitoring a coordinated exchange process in a four-component biological interaction system: development of a time-resolved terbium-based one-donor/three-acceptor multicolor FRET system Diosgenin relieves goiter via the inhibition of thyrocyte proliferation in a mouse model of Graves' disease.Estradiol inhibits ongoing autoimmune neuroinflammation and NFkappaB-dependent CCL2 expression in reactive astrocytes The atypical ubiquitin ligase RNF31 stabilizes estrogen receptor α and modulates estrogen-stimulated breast cancer cell proliferation Effects of 7-O substitutions on estrogenic and anti-estrogenic activities of daidzein analogues in MCF-7 breast cancer cells.Versatility or promiscuity: the estrogen receptors, control of ligand selectivity and an update on subtype selective ligands.The selective estrogen receptor downregulator GDC-0810 is efficacious in diverse models of ER+ breast cancer.Competitive molecular docking approach for predicting estrogen receptor subtype α agonists and antagonists.Structural and functional profiling of environmental ligands for estrogen receptors.The 2010 Philip S. Portoghese Medicinal Chemistry Lectureship: addressing the "core issue" in the design of estrogen receptor ligands Estrogen receptor mutations and their role in breast cancer progression Identification and structure-activity relationships of a novel series of estrogen receptor ligands based on 7-thiabicyclo[2.2.1]hept-2-ene-7-oxide.Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.Exploring Flexibility of Progesterone Receptor Ligand Binding Domain Using Molecular Dynamics.Bicyclic core estrogens as full antagonists: synthesis, biological evaluation and structure-activity relationships of estrogen receptor ligands based on bridged oxabicyclic core arylsulfonamides.Small molecule modulation of nuclear receptor conformational dynamics: implications for function and drug discovery Systematic Prioritization of Druggable Mutations in ∼5000 Genomes Across 16 Cancer Types Using a Structural Genomics-based Approach Dual suppression of estrogenic and inflammatory activities for targeting of endometriosis Estrogen receptor alpha somatic mutations Y537S and D538G confer breast cancer endocrine resistance by stabilizing the activating function-2 binding conformation.ESR1 mutations—a mechanism for acquired endocrine resistance in breast cancer.Stapled Peptides with γ-Methylated Hydrocarbon Chains for the Estrogen Receptor/Coactivator Interaction.Nonclassical SNAPFL analogue as a Cy5 resonance energy transfer partner Full antagonism of the estrogen receptor without a prototypical ligand side chain.Triaryl-substituted Schiff bases are high-affinity subtype-selective ligands for the estrogen receptor.Exploring the Structural Compliancy versus Specificity of the Estrogen Receptor Using Isomeric Three-Dimensional Ligands.The nuclear receptor signalling scaffold: insights from full-length structures.Oxabicycloheptene Sulfonate Protects Against β-Amyloid-induced Toxicity by Activation of PI3K/Akt and ERK Signaling Pathways Via GPER1 in C6 Cells.Activating ESR1 Mutations Differentially Affect the Efficacy of ER Antagonists.The Evolving Role of the Estrogen Receptor Mutations in Endocrine Therapy-Resistant Breast Cancer.

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NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses

http://www.wikidata.org/entity/Q27650089

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2008 nî lūn-bûn

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2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2008 թվականի ապրիլին 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年论文

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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NFκB selectivity of estrogen r ...... tive crystallographic analyses

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Nature Chemical Biology

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NFkappaB selectivity of estrog ...... tive crystallographic analyses

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Andrzej Joachmiak

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Geoffrey L Greene

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Jason Nowak

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John A Katzenellenbogen

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John B Bruning

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Johnnie B Hahm

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Kendall W Nettles

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Kristen Kulp

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Richard B Hochberg

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Younchang Kim

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P2860

CBP Is a dosage-dependent regulator of nuclear factor-kappaB suppression by the estrogen receptor

The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain

Structural insights into the mode of action of a pure antiestrogen

Structural plasticity in the oestrogen receptor ligand-binding domain

Elemental isomerism: a boron-nitrogen surrogate for a carbon-carbon double bond increases the chemical diversity of estrogen receptor ligands

Partial agonists activate PPARgamma using a helix 12 independent mechanism

Structure and specificity of nuclear receptor-coactivator interactions

The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen

A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site

Hormone-PAMAM dendrimer conjugates: polymer dynamics and tether structure affect ligand access to receptors.

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241-247

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2140775

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10.1038/NCHEMBIO.76

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4

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4

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Sanjeev Kumar Sharma

Benita Katzenellenbogen

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2008-03-16T00:00:00Z

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5507297

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1025380413

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2659626

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