Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking.
about
Positioning of proteins in membranes: a computational approachThe structural basis of arrestin-mediated regulation of G-protein-coupled receptorsCrystal structure of a photoactivated deprotonated intermediate of rhodopsinRetina, retinol, retinal and the natural history of vitamin A as a light sensorStructure of a beta1-adrenergic G-protein-coupled receptor.Activation biosensor for G protein-coupled receptors: a FRET-based m1 muscarinic activation sensor that regulates G(q)OPM: orientations of proteins in membranes databaseThe structure and function of G-protein-coupled receptorsAccessibility and dynamics of nitroxide side chains in T4 lysozyme measured by saturation recovery EPR.Production and characterization of monoclonal antibodies sensitive to conformation in the 5HT2c serotonin receptor.Activation of G protein-coupled receptors: beyond two-state models and tertiary conformational changes.Chemistry and biology of the initial steps in vision: the Friedenwald lecture.Navigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labeling and EPR Spectroscopy.Toward the fourth dimension of membrane protein structure: insight into dynamics from spin-labeling EPR spectroscopyG-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.Retinal ligand mobility explains internal hydration and reconciles active rhodopsin structuresA Straightforward Approach to the Analysis of Double Electron-Electron Resonance DataInternal hydration increases during activation of the G-protein-coupled receptor rhodopsin.Membrane model for the G-protein-coupled receptor rhodopsin: hydrophobic interface and dynamical structureRandom mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking.Modulating G-protein coupled receptor/G-protein signal transduction by small molecules suggested by virtual screening.Contribution of membrane elastic energy to rhodopsin functionRhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin bindingNormal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.Identification of orthosteric and allosteric site mutations in M2 muscarinic acetylcholine receptors that contribute to ligand-selective signaling biasHow a small change in retinal leads to G-protein activation: initial events suggested by molecular dynamics calculations.Retinal conformation and dynamics in activation of rhodopsin illuminated by solid-state H NMR spectroscopy.Complexes between photoactivated rhodopsin and transducin: progress and questions.Arrestin can act as a regulator of rhodopsin photochemistry.Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery.Structural and dynamic effects of cholesterol at preferred sites of interaction with rhodopsin identified from microsecond length molecular dynamics simulations.Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.Cholesterol modulates the membrane effects and spatial organization of membrane-penetrating ligands for G-protein coupled receptorsPhosphatidylethanolamine enhances rhodopsin photoactivation and transducin binding in a solid supported lipid bilayer as determined using plasmon-waveguide resonance spectroscopyFunctional characterization of rhodopsin monomers and dimers in detergents.Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPRModeling flexible loops in the dark-adapted and activated states of rhodopsin, a prototypical G-protein-coupled receptor.High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins.A new Lanczos-based algorithm for simulating high-frequency two-dimensional electron spin resonance spectra.A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids.
P2860
Q24647761-0B20D7CF-2C30-4508-9268-7A639819A6FFQ24657537-7B92A3EB-7EBF-44C9-8EFC-C1CAAA67705CQ24671760-CDBBE46A-080F-4E65-9E1A-98590FB52542Q26998937-8FE0245A-DFBE-4E59-90EC-545506EDC103Q27651011-925F5CB2-E113-40AD-9148-8AB3CB3B9FE4Q28483910-699473BE-56D2-49D0-9962-730705C57318Q29616317-FAE8614A-CFD4-45FA-A8CF-220F63B3A4DCQ29616792-53C80E64-9DA1-43A2-AE37-2C6C2D49116BQ30350985-8E4BA21F-725E-4824-85E2-72A9D6667736Q30360451-043DC550-624B-4FB3-93CE-E4687A8E06B5Q30364526-A18197A0-8A9E-4F5F-9832-51D8EC552866Q30368025-F96E6EDB-3EE6-41F0-AD32-1FB1C8EAF56DQ30380407-F958C241-DAC3-4089-A4D4-A72DC0D4F82AQ30409391-5015C5F1-87DC-42E2-9300-6744EAE317A1Q30427675-EB36226E-6394-4957-BBA8-20EA84322B75Q30712788-05B6C30A-947E-41A8-B0D3-BC02301453CEQ31007626-5149CE23-9832-4C4B-8B54-1DF2CEC46BB0Q31160779-1A2734F6-D70B-42F0-8133-56BCA1138364Q33200121-6F37850F-4EAA-4CCE-9258-00A2391E50A6Q33259490-6C14E6B8-9786-4C66-9C9C-B44C29BEE8E7Q33360557-03F4248D-B677-46FF-B82D-C53E3FB49CEFQ33648608-EB51FD11-97A0-4243-B805-FD22C57BC02BQ33689499-7BFCDF24-D802-40FD-A614-2322E14AE1B3Q33718901-69749292-C9F5-4301-973A-F4A6101CBEECQ33748133-5AC056BD-6D19-422B-ABE5-13DF9D808F1CQ33763840-765C9E2F-B9F7-42EE-AAE9-7A23537FE03DQ33807818-74F215AC-7418-4669-B3E0-953EFEF5FF93Q33873779-69096C47-2D94-4A05-BDB8-AE61AC2622D9Q33879152-88492426-138D-4857-A241-709175288399Q33890786-780E7A22-E8F6-4ABF-A90B-156DC903302AQ33913886-F02BA4AF-9EC0-4F40-B87D-C71FA6452308Q34083157-27C52554-507D-48C0-8D37-8BD27C936CECQ34144314-FC94776C-E76E-4649-9E47-F0FA5753EEDEQ34188443-340E61BA-9F3F-4A69-AD7F-06480F3258A3Q34313981-BC4B2DC1-D6C9-4FAE-8FA4-7957ABCBA272Q34351236-A410D264-E3E7-491E-A067-BD17EEEDD55AQ34352345-01C6FEA3-7F43-4B11-B498-0CB68BAAA674Q34534205-656575A1-886F-413A-987D-9C96663F6C5BQ34583097-7D011DC9-30D6-4F03-BB91-80E745E16B2FQ34596621-95659E89-C25D-46DE-95BA-B0B673616266
P2860
Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Rhodopsin structure, dynamics, ...... , and disulfide cross-linking.
@ast
Rhodopsin structure, dynamics, ...... , and disulfide cross-linking.
@en
type
label
Rhodopsin structure, dynamics, ...... , and disulfide cross-linking.
@ast
Rhodopsin structure, dynamics, ...... , and disulfide cross-linking.
@en
prefLabel
Rhodopsin structure, dynamics, ...... , and disulfide cross-linking.
@ast
Rhodopsin structure, dynamics, ...... , and disulfide cross-linking.
@en
P2093
P1476
Rhodopsin structure, dynamics, ...... , and disulfide cross-linking.
@en
P2093
Cheryl M Hubbell
Christian Altenbach
H Gobind Khorana
P304
P356
10.1016/S0065-3233(03)63010-X
P577
2003-01-01T00:00:00Z