Structural plasticity in the oestrogen receptor ligand-binding domain - Wikidata - wikimedia - TriplyDB

Structural plasticity in the oestrogen receptor ligand-binding domain

Structural plasticity in the oestrogen receptor ligand-binding domain

http://www.wikidata.org/entity/Q27644641

about

3D models of MBP, a biologically active metabolite of bisphenol A, in human estrogen receptor α and estrogen receptor β Identification of xenoestrogens in food additives by an integrated in silico and in vitro approach Doubling the Size of the Glucocorticoid Receptor Ligand Binding Pocket by Deacylcortivazol NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses The Structural Basis of Gas-Responsive Transcription by the Human Nuclear Hormone Receptor REV-ERBβ Coupling of receptor conformation and ligand orientation determine graded activity Structure of Estradiol Metal Chelate and Estrogen Receptor Complex: The Basis for Designing a New Class of Selective Estrogen Receptor Modulators Ligand-binding dynamics rewire cellular signaling via estrogen receptor-α Deciphering Modern Glucocorticoid Cross-pharmacology Using Ancestral Corticosteroid Receptors 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 Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics.Screening Chemicals for Receptor-Mediated Toxicological and Pharmacological Endpoints: Using Public Data to Build Screening Tools within a KNIME Workflow.Estrogen Receptor-Targeted Contrast Agents for Molecular Magnetic Resonance Imaging of Breast Cancer Hormonal Status.Dual RXR Agonists and RAR Antagonists Based on the Stilbene Retinoid Scaffold.Potential activity of fevicordin-A from Phaleria macrocarpa (Scheff) Boerl. seeds as estrogen receptor antagonist based on cytotoxicity and molecular modelling studies.Synthesis and functional analysis of novel bivalent estrogens.Probing the topological tolerance of multimeric protein interactions: evaluation of an estrogen/synthetic ligand for FK506 binding protein conjugate.Versatility or promiscuity: the estrogen receptors, control of ligand selectivity and an update on subtype selective ligands.Structural and functional insights into nuclear receptor signaling.Histone deacetylase inhibitors equipped with estrogen receptor modulation activity.Competitive molecular docking approach for predicting estrogen receptor subtype α agonists and antagonists.Behavior of solvent-exposed hydrophobic groove in the anti-apoptotic Bcl-XL protein: clues for its ability to bind diverse BH3 ligands from MD simulations.Virtual screening of the estrogen receptor.Structural and functional profiling of environmental ligands for estrogen receptors.Multiple-targeting and conformational selection in the estrogen receptor: computation and experiment.The 2010 Philip S. Portoghese Medicinal Chemistry Lectureship: addressing the "core issue" in the design of estrogen receptor ligands Steroidal bivalent ligands for the estrogen receptor: design, synthesis, characterization and binding affinities.Structural and functional analysis of domains of the progesterone receptor.Synthesis and evaluation of 17α-E-20-(heteroaryl)norpregn-1,3,5(10),20 tetraene-3,17β-diols [17α-(heteroaryl)vinyl estradiols] as ligands for the estrogen receptor-α ligand binding domain (ERα-LBD).Targeting the estrogen receptor with metal-carbonyl derivatives of estradiol 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.Synthesis and evaluation of 17α-(dimethylphenyl)vinyl estradiols as probes of the estrogen receptor-α ligand binding domain.Synergistic activation of human pregnane X receptor by binary cocktails of pharmaceutical and environmental compounds.Tetradian oscillation of estrogen receptor α is necessary to prevent liver lipid deposition.Structure-Based Understanding of Binding Affinity and Mode of Estrogen Receptor α Agonists and Antagonists Origin of an ancient hormone/receptor couple revealed by resurrection of an ancestral estrogen Selective Human Estrogen Receptor Partial Agonists (ShERPAs) for Tamoxifen-Resistant Breast Cancer Neural-Network Scoring Functions Identify Structurally Novel Estrogen-Receptor Ligands.The natural estrogenic compound diarylheptanoid (D3): in vitro mechanisms of action and in vivo uterine responses via estrogen receptor α Nonsteroidal bivalent estrogen ligands: an application of the bivalent concept to the estrogen receptor.

P2860

Q21560757-C80234B2-26AC-4874-BF44-79F4AA4C8DB4 Q24656051-64F3937F-9C75-411D-BBDA-ED9F5DA05B53 Q27649439-545351D4-579A-4790-87F3-93113D6B0650 Q27650089-7F55D04D-B2EF-4D60-B5A7-EEE9D0B5F694 Q27653944-C742B3A0-B09F-40B3-BBA4-7A2CAEA9C2AE Q27664921-EBF85536-F43C-43C9-8703-DA89F84F987A Q27667460-B8F93963-B63F-47D5-894C-668821047A9B Q27677013-9EC116CA-6DDC-4F2D-A42D-69983B526849 Q27678139-DE517EF0-DD10-49CE-8754-7E50E6365352 Q27678627-9C85898D-398B-4C5E-AFCD-E814B40D4E2B Q30418832-84DF48C7-B8B9-41AC-B47C-3222D500072F Q30489654-7B80CF3D-9D32-450D-83C0-09BC3563B641 Q31097623-A46F47B6-CA51-4F47-97B8-6D6509C4F452 Q33636514-E036B634-25E1-4221-9D81-8E013881FABB Q33755530-E4E2A9B2-A699-4397-9B6B-A026B4DE2245 Q34170273-44F44157-F797-4F2F-8806-2B8C9577747E Q34257756-D7380FE4-3490-4D6C-9F3F-95EEDF65B66F Q34347992-DCBCCF53-95E9-4090-ADB7-1297478E0688 Q34348135-90BEC3C0-37DC-41B5-B736-AA96E9F64F25 Q34352264-8E96A3A3-7F83-4999-AF2F-2C9BCB2FD796 Q34607003-8678CCB0-C8C8-41DB-9E58-3F4C846335B0 Q34611338-417706C7-55BB-45D0-8D7F-DE8F4E9D6C70 Q34619281-4318D4A2-E2D9-4AB0-8F96-54A2CD4E82A0 Q34632938-0600062E-AA3F-425E-9A9A-65756F96D7CC Q35046420-5179D613-D750-428E-A021-9714E580D918 Q35148605-787636B0-8577-4E67-B888-3CB65B6A819F Q35227529-F8C2BAF1-A942-4287-8755-372A4D702B71 Q35624126-72A5BB1E-B76B-44E5-B491-DFBB3D50795B Q35676299-A74CF771-EDBE-438D-9FCD-C27341A50D8D Q35742807-7653B8A3-99C8-4156-BD1C-51990ADBF964 Q35815534-0D800151-A57B-4F9F-ABCA-D89BC47635FE Q35839439-88588A47-B50A-4868-9A12-A3743560B864 Q36059350-414A9261-7674-499B-ABFB-EE55CD7769F4 Q36122649-F981FB7D-B439-4244-AAE3-8D1F9E944C34 Q36243027-9DF7BDAE-90A5-4A78-9085-1BA59671EE84 Q36354712-CD8DC71F-7EFE-44C8-8C3B-DB5D308F112E Q36656704-624F38E5-CFC2-4F59-9613-AD90A870D6B1 Q36658263-5D72BC89-C56C-43CE-9BB4-C6F9EAEC9621 Q36750997-49E2793D-0C4A-4834-AAEC-00D442F01299 Q36781304-321D4907-9D48-4A29-A9D7-83A5308D2B54

P2860

Structural plasticity in the oestrogen receptor ligand-binding domain

http://www.wikidata.org/entity/Q27644641

description

2007 nî lūn-bûn

@nan

2007 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Structural plasticity in the oestrogen receptor ligand-binding domain

@ast

Structural plasticity in the oestrogen receptor ligand-binding domain

@en

Structural plasticity in the oestrogen receptor ligand-binding domain

@nl

type

label

Structural plasticity in the oestrogen receptor ligand-binding domain

@ast

Structural plasticity in the oestrogen receptor ligand-binding domain

@en

Structural plasticity in the oestrogen receptor ligand-binding domain

@nl

prefLabel

Structural plasticity in the oestrogen receptor ligand-binding domain

@ast

Structural plasticity in the oestrogen receptor ligand-binding domain

@en

Structural plasticity in the oestrogen receptor ligand-binding domain

@nl

P1433

Q27644641-57D39044-DBA1-4C12-B035-7678FC77C510

P1476

Q27644641-7CB5CB63-774C-49B2-BAB8-5A979BBD246D

P2093

Q27644641-042B4F47-1ADE-4937-B999-06601DF5C906

Q27644641-100D46F8-22D5-4DE1-A02D-4FB1BE7DCE79

Q27644641-1A3FD894-A296-4D9B-8936-A5DAB1CC6A16

Q27644641-4133F8C1-0D94-4F89-950D-824A707E0AF7

Q27644641-5D9BFDF9-6166-4289-B873-4C39B58A7BAB

Q27644641-651B71B8-2364-4850-AC53-3571F9F950F5

Q27644641-85EADC1C-5D8F-4264-BCDC-AE202FBAA6D8

Q27644641-86F72725-8006-4CE7-8812-B1E402192657

Q27644641-877B0A32-B8DA-47EC-8B32-69156E2372CF

Q27644641-DFEB75BB-E285-44A6-8C9B-D50F7D92A390

P2860

Q27644641-141E5818-2D9D-44F5-96FE-9EAABC2453C5

Q27644641-1E9DC63A-611E-4601-8185-6B25B68F8356

Q27644641-23CED066-B20E-4AA1-BB8D-CE436681DA77

Q27644641-34252138-F0AD-46D2-BAC0-30698998D89E

Q27644641-399C2656-7889-49B5-BC7F-D0D6DF43AFD9

Q27644641-3B34CB51-54C1-4D80-A5EA-EC69D7BE98F3

Q27644641-49D5F86A-58E6-488E-BC56-95C7E300C9E8

Q27644641-4C37A118-6CA1-412C-9DAE-6BE463B71FED

Q27644641-598EBAA5-E061-4BAA-890E-0DF0A8EF0614

Q27644641-59E394B0-D522-4C13-A8C2-1DAF86314E8B

P304

Q27644641-0A0E9DFD-6E1F-4BC7-BD57-DE5DF9C0828B

P31

Q27644641-205F1897-5FA1-48ED-9446-A8A4B449011F

P3181

Q27644641-B11BB01A-8896-41F7-A2C5-48E64E5DF0F1

P356

Q27644641-8716AC8B-9D55-43FC-AD35-2A282AF2F70A

P433

Q27644641-580BF60E-BF48-4EED-8BD9-07B2F75945B3

P478

Q27644641-3B470F85-93A6-4427-99C7-91BEEA92FF4B

P50

Q27644641-6C8BFA81-7F8F-4BDE-BEF5-7D3CEFFE6F2F

Q27644641-88972785-1A08-4601-81DE-174905308258

P577

Q27644641-FCF306DB-B79A-4996-A4AC-43671A260D17

P5875

Q27644641-C545E051-AD21-43DA-8095-A86EB24DF6ED

P698

Q27644641-C78ADE86-C3EA-4477-9AF3-32056DC91730

P921

Q27644641-4010680F-03C9-41BE-BAD8-7A406898B03E

P932

Q27644641-4EFC6BF0-A401-40C5-B7FA-93DF0DD48E5E

P3181

P356

SJ.EMBOR.7400963

P1433

P1476

Structural plasticity in the oestrogen receptor ligand-binding domain

@en

P2093

Alun Hughs

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

Erin E O'Neill

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

Eugene R DeSombre

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

Geoffrey L Greene

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

Jason Nowak

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

John B Bruning

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

Kendall W Nettles

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

Robert Dilis

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

Robert N Hanson

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

Younchang Kim

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

P2860

Molecular recognition of fatty acids by peroxisome proliferator-activated receptors

Structural insights into the mode of action of a pure antiestrogen

The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity

Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha

Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

Molecular basis of agonism and antagonism in the oestrogen receptor

Atomic structure of progesterone complexed with its receptor

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

Molecular determinants for the tissue specificity of SERMs

Reflections on the discovery and significance of estrogen receptor beta

P304

563-8

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

P31

scholarly article

P3181

2037235

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

P356

10.1038/SJ.EMBOR.7400963

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

P433

6

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

P478

8

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

P50

Andrzej Joachimiak

P577

2007-06-01T00:00:00Z

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

P5875

6360727

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

P698

17468738

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

P921

P932

2002528

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