A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic Receptor - Wikidata - awgldk - TriplyDB

A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic Receptor

A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic Receptor

http://www.wikidata.org/entity/Q27650801

about

G protein-coupled receptors: extranuclear mediators for the non-genomic actions of steroids Structure of an agonist-bound human A2A adenosine receptor Role of glycosphingolipids in the function of human serotonin₁A receptors Internal lipid architecture of the hetero-oligomeric cytochrome b6f complex The structural basis for agonist and partial agonist action on a β(1)-adrenergic receptor Structure of a nanobody-stabilized active state of the β(2) adrenoceptor Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist The Use of Multiscale Molecular Simulations in Understanding a Relationship between the Structure and Function of Biological Systems of the Brain: The Application to Monoamine Oxidase Enzymes Diversity and modularity of G protein-coupled receptor structures Large-scale production and protein engineering of G protein-coupled receptors for structural studies New insights for drug design from the X-ray crystallographic structures of G-protein-coupled receptors Turning receptors on and off with intracellular pepducins: new insights into G-protein-coupled receptor drug development CUP-1 is a novel protein involved in dietary cholesterol uptake in Caenorhabditis elegans Endogenous vs Exogenous Allosteric Modulators in GPCRs: A dispute for shuttling CB1 among different membrane microenvironments.Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association Membrane-sensitive conformational states of helix 8 in the metabotropic Glu2 receptor, a class C GPCR Induced effects of sodium ions on dopaminergic G-protein coupled receptors Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor Conserved Binding Mode of Human β 2 Adrenergic Receptor Inverse Agonists and Antagonist Revealed by X-ray Crystallography Structure of the Human Dopamine D3 Receptor in Complex with a D2/D3 Selective Antagonist Two distinct conformations of helix 6 observed in antagonist-bound structures of a 1-adrenergic receptor High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Environment Towards protein-crystal centering using second-harmonic generation (SHG) microscopy Crystal Structures of a Stabilized β1-Adrenoceptor Bound to the Biased Agonists Bucindolol and Carvedilol Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography The 2.1 Å Resolution Structure of Cyanopindolol-Bound β1-Adrenoceptor Identifies an Intramembrane Na+ Ion that Stabilises the Ligand-Free Receptor Structural basis for Smoothened receptor modulation and chemoresistance to anticancer drugs Understanding functional residues of the cannabinoid CB1.There Is No Simple Model of the Plasma Membrane Organization Membrane-Mediated Oligomerization of G Protein Coupled Receptors and Its Implications for GPCR Function A predicted binding site for cholesterol on the GABAA receptor Function-specific virtual screening for GPCR ligands using a combined scoring method Recombinant human melatonin receptor MT1 isolated in mixed detergents shows pharmacology similar to that in mammalian cell membranes Conformational antibody binding to a native, cell-free expressed GPCR in block copolymer membranes 3D structure prediction of human β1-adrenergic receptor via threading-based homology modeling for implications in structure-based drug designing Modulation of the interaction between neurotensin receptor NTS1 and Gq protein by lipid The Principles of Ligand Specificity on beta-2-adrenergic receptor The biology of CCR5 and CXCR4

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A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic Receptor

http://www.wikidata.org/entity/Q27650801

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին 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

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

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name

A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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label

A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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prefLabel

A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

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P356

J.STR.2008.05.001

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P1476

A Specific Cholesterol Binding ...... e Human β2-Adrenergic Receptor

@en

P2093

Christopher B Roth

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

Ellen Y T Chien

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

Jeffrey Velasquez

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

Mark T Griffith

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

Michael A Hanson

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

Peter Kuhn

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

P2860

High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor

Crystal structure of the human beta2 adrenergic G-protein-coupled receptor

The crystal structure of a hyperthermophilic archaeal TATA-box binding protein

Identification of G protein-coupled receptor genes from the human genome sequence

GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function

Comparison of helix interactions in membrane and soluble alpha-bundle proteins.

Regulation of receptor function by cholesterol.

How cells handle cholesterol.

Role of cholesterol in the function and organization of G-protein coupled receptors.

A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids.

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897-905

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scholarly article

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499158

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10.1016/J.STR.2008.05.001

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6

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

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16

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

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Raymond C Stevens

Veli-Pekka Jaakola

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2008-06-01T00:00:00Z

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5308697

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18547522

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structural biology

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2601552

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