Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association
about
Molecular dynamics simulations of membrane proteins and their interactions: from nanoscale to mesoscaleMembrane omega-3 fatty acids modulate the oligomerisation kinetics of adenosine A2A and dopamine D2 receptors.Membrane-Mediated Oligomerization of G Protein Coupled Receptors and Its Implications for GPCR FunctionDynamic Cholesterol-Conditioned Dimerization of the G Protein Coupled Chemokine Receptor Type 4.Impact of Lipid Composition and Receptor Conformation on the Spatio-temporal Organization of μ-Opioid Receptors in a Multi-component Plasma Membrane Model.Molecular Pharmacology of δ-Opioid Receptors.Cholesterol-dependent Conformational Plasticity in GPCR Dimers.Insights into the function of opioid receptors from molecular dynamics simulations of available crystal structures.Model parameters for simulation of physiological lipidsConformational Heterogeneity of Intracellular Loop 3 of the μ-opioid G-protein Coupled Receptor.Two delta opioid receptor subtypes are functional in single ventral tegmental area neurons, and can interact with the mu opioid receptor.Excessive aggregation of membrane proteins in the Martini model.GPCRs: What Can We Learn from Molecular Dynamics Simulations?Beta2-adrenergic receptor homodimers: Role of transmembrane domain 1 and helix 8 in dimerization and cell surface expression.Molecular dynamics simulations and structure-based network analysis reveal structural and functional aspects of G-protein coupled receptor dimer interactions.Closely related, yet unique: Distinct homo- and heterodimerization patterns of G protein coupled chemokine receptors and their fine-tuning by cholesterol.Molecular details of dimerization kinetics reveal negligible populations of transient µ-opioid receptor homodimers at physiological concentrations.
P2860
Q26747182-2FF2BA1B-4194-4C7C-A459-E6A637396402Q27300848-95EC954E-C62F-4478-A17B-5ABC05CD512EQ28072820-F17F2098-86EE-4B14-BE9C-7EE4C63FE38FQ36182026-3E49A108-EBF3-424A-984F-247D60055469Q36222134-0E70773A-F625-4489-AB88-FAEEE621F0FCQ37062556-5DC00093-448B-4A8F-9E89-14CC25370089Q37184788-1400BA59-1F12-470F-9B28-BF47D4CD6B3AQ39165104-289F6C09-F378-4233-8A5D-6637872B2EB8Q41484392-00C4ED75-5057-40EC-B275-62A933DAF644Q44341109-40DA3C1C-B9C9-4988-BA3C-BDE6D5B549FEQ44346788-7F96E25C-3CA4-473A-9256-5271C0DE9127Q47113820-A68AB0E6-B2F3-480B-9788-D1ECDDD71F76Q47348724-7104486D-627C-431A-82AD-A1B299025EF5Q51250449-999C8D01-A750-4392-8B03-EC9248DEF0F8Q51678306-2C9777E0-86A2-4789-9251-0C964F5444D5Q52660783-A6181457-2108-4C6B-9486-446DD0C41566Q55003590-F1A6035A-801C-412D-BD22-D14E3218FB01
P2860
Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association
description
2015 nî lūn-bûn
@nan
2015 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի մարտին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年学术文章
@wuu
2015年学术文章
@zh-cn
2015年学术文章
@zh-hans
2015年学术文章
@zh-my
2015年学术文章
@zh-sg
2015年學術文章
@yue
name
Preferred supramolecular organ ...... rom simulated self-association
@ast
Preferred supramolecular organ ...... rom simulated self-association
@en
Preferred supramolecular organ ...... rom simulated self-association
@nl
type
label
Preferred supramolecular organ ...... rom simulated self-association
@ast
Preferred supramolecular organ ...... rom simulated self-association
@en
Preferred supramolecular organ ...... rom simulated self-association
@nl
prefLabel
Preferred supramolecular organ ...... rom simulated self-association
@ast
Preferred supramolecular organ ...... rom simulated self-association
@en
Preferred supramolecular organ ...... rom simulated self-association
@nl
P2093
P2860
P3181
P1476
Preferred supramolecular organ ...... rom simulated self-association
@en
P2093
Davide Provasi
Jennifer M Johnston
Mustafa Burak Boz
P2860
P304
P3181
P356
10.1371/JOURNAL.PCBI.1004148
P407
P577
2015-03-01T00:00:00Z