Cited by 412Nicotinic Acetylcholine Receptors StudyAnesthesia and Sedative AgentsNeuroscience and Neuropharmacology Research

The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.

X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel

Open access

Nury, Hugues, Van Renterghem, Catherine, Weng, Yun, Tran, Alphonso, Baaden, Marc, Dufresne, Virginie, Changeux, Jean-Pierre, Sonner, James M., Delarue, Marc, Corringer, Pierre-Jean·2011·Nature

DOI 10.1038/nature09647

Open this paper in CoChat — free account

Abstract

General anaesthetics have enjoyed long and widespread use but their molecular mechanism of action remains poorly understood. There is good evidence that their principal targets are pentameric ligand-gated ion channels (pLGICs) such as inhibitory GABA(A) (γ-aminobutyric acid) receptors and excitatory nicotinic acetylcholine receptors, which are respectively potentiated and inhibited by general anaesthetics. The bacterial homologue from Gloeobacter violaceus (GLIC), whose X-ray structure was recently solved, is also sensitive to clinical concentrations of general anaesthetics. Here we describe the crystal structures of the complexes propofol/GLIC and desflurane/GLIC. These reveal a common general-anaesthetic binding site, which pre-exists in the apo-structure in the upper part of the transmembrane domain of each protomer. Both molecules establish van der Waals interactions with the protein; propofol binds at the entrance of the cavity whereas the smaller, more flexible, desflurane binds deeper inside. Mutations of some amino acids lining the binding site profoundly alter the ionic response of GLIC to protons, and affect its general-anaesthetic pharmacology. Molecular dynamics simulations, performed on the wild type (WT) and two GLIC mutants, highlight differences in mobility of propofol in its binding site and help to explain these effects. These data provide a novel structural framework for the design of general anaesthetics and of allosteric modulators of brain pLGICs.

Integrity signals

Registry

Crossref · 10.1038/nature09647

Cites

48 of 48 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems
Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,638
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
MacKerell, A. D., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., et al. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp973084f · Cited by 14,429
PRODRG: a tool for high-throughput crystallography of protein–ligand complexes
Schüttelkopf, A. W., & van Aalten, D. M. F. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904011679 · Cited by 4,837
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
Davis, I., Leaver‐Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., Snoeyink, J. S., Richardson, J. S., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm216 · Cited by 3,918

Show all 48 references

Research works printed but not linked: 1

Bricogne, G. et al. BUSTER, version 2.8.0. Cambridge, UK: Global Phasing. (2009)

Sorted by citations

Items 301–400 of 406

Permeating disciplines: Overcoming barriers between molecular simulations and classical structure-function approaches in biological ion transport
Howard, R. J., Carnevale, V., Delemotte, L., Hellmich, U. A., & Rothberg, B. S. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.12.013 · Cited by 9
Protein–Lipid Interfaces Can Drive the Functions of Membrane-Embedded Protein–Protein Complexes
Sarkar, D., Singh, Y., & Kalia, J. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00644 · Cited by 9
Modulation of the Gloeobacter violaceus Ion Channel by Fentanyl: A Molecular Dynamics Study
Faulkner, C., Plant, D. F., & de Leeuw, N. H. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00881 · Cited by 9
Interfacial binding sites for cholesterol on GABAA receptors and competition with neurosteroids
LEE, A. G. J. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.05.009 · Cited by 9
Effects of isoflurane on the expressed Cav2.2 currents in Xenopus oocytes depend on the activation of protein kinase C δ and its phosphorylation sites in the Cav2.2α1 subunits
Rajagopal, S., Fang, H., Lynch, C., Sando, J. J., & Kamatchi, G. L. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.02.041 · Cited by 9
Anxiolytika und Hypnotika
Lüddens, H. (2011) · Springer eBooks · doi:10.1007/978-3-642-19844-1_56 · Cited by 9
Regulation of the Nicotinic Acetylcholine Receptor by Cholesterol as a Boundary Lipid
Barrantes, F. J. (2012) · Wiley eBooks · doi:10.1002/9781118342312.ch9 · Cited by 9
Utilization of O/S-doped graphene nanoclusters for ultrasensitive detection of flurane derivatives-DFT investigations
Al-Otaibi, J. S., Almuqrin, A. H., Mary, Y. S., & Mary, Y. S. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1870155 · Cited by 8
Selective bond breaking of halothane induced by electron transfer in potassium collisions
Lozano, A. I., Maioli, L. S., Pamplona, B., Romero, J. A. R., Mendes, M., da Silva, F. F., Kossoski, F., Probst, M. M., Süβ, D., Bettega, M. H. F., et al. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/d0cp02570d · Cited by 8
Ion Channels in Anesthesia
Zhou, W., & Guan, Z. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-4254-8_19 · Cited by 9
Mutations M287L and Q266I in the Glycine Receptor α1 Subunit Change Sensitivity to Volatile Anesthetics in Oocytes and Neurons, but Not the Minimal Alveolar Concentration in Knockin Mice
Borghese, C. M., Xiong, W., Oh, S. I., Ho, A., Mihic, S. J., Zhang, L., Lovinger, D. M., Homanics, G. E., Eger, E. I., & Harris, R. A. (2012) · Anesthesiology · doi:10.1097/aln.0b013e31826a0d93 · Cited by 8
Mecamylamine inhibits muscle nicotinic acetylcholine receptors by competitive and noncompetitive mechanisms
Arias, H., Targowska‐Duda, K. M., Feuerbach, D., & Jóźwiak, K. (2013) · OA Biochemistry · doi:10.13172/2052-9651-1-1-600 · Cited by 8
Molecular Interactions between Ligands and Nicotinic Acetylcholine Receptors Revealed by Studies with Acetylcholine Binding Proteins
Arias, H. R. (2012) · Journal of Thermodynamics & Catalysis · doi:10.4172/2157-7544.1000116 · Cited by 8
Investigating the structural dynamics of the PIEZO1 channel activation and inactivation by coarse‐grained modeling
Zheng, W., & Sachs, F. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25384 · Cited by 8
Simulating ion channel activation mechanisms using swarms of trajectories
Lev, B. B., & Allen, T. W. (2019) · Journal of Computational Chemistry · doi:10.1002/jcc.26102 · Cited by 8
Protection Against Protein Aggregation by Alpha-Crystallin as a Mechanism of Preconditioning
Ferns, J. E., Theisen, C. S., Fibuch, E. E., & Seidler, N. W. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0601-4 · Cited by 7
Short-term immunological effects of non-ethanolic short-chain alcohols
Désy, O., Carignan, D., & de Campos-Lima, P. O. (2012) · Toxicology Letters · doi:10.1016/j.toxlet.2012.01.005 · Cited by 7
Predicting lipid and ligand binding sites in TRPV1 channel by molecular dynamics simulation and machine learning
Zheng, W., & Wen, H. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26075 · Cited by 7
Dipicrylamine Modulates GABAρ1 Receptors through Interactions with Residues in the TM4 and Cys-Loop Domains
Limón, A., Estrada‐Mondragón, A., Reyes‐Ruiz, J. M., & Miledi, R. (2016) · Molecular Pharmacology · doi:10.1124/mol.116.103432 · Cited by 7
Simulation of Ligand Binding to Membrane Proteins
Murail, S. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7151-0_20 · Cited by 7
Structural changes at the myrtenol backbone reverse its positive allosteric potential into inhibitory GABA A receptor modulation
Milanos, S., Kuenzel, K., Gilbert, D. F., Janzen, D., Sasi, M., Buettner, A., Frimurer, T. M., & Villmann, C. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0262 · Cited by 8
Direct stimulation of adenylyl cyclase 9 by the fungicide imidazole miconazole
Simpson, J., Pálvölgyi, A., & Antoni, F. A. (2019) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-018-01610-1 · Cited by 7
Alkylphenol inverse agonists of HCN1 gating: H-bond propensity, ring saturation and adduct geometry differentially determine efficacy and potency
Joyce, R. L., Beyer, N. P., Vasilopoulos, G., Woll, K. A., Hall, A. C., Eckenhoff, R. G., Barman, D. N., Warren, J. D., Tibbs, G. R., & Goldstein, P. A. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.02.013 · Cited by 7
Pseudo-Symmetric Assembly of Protodomains as a Common Denominator in the Evolution of Polytopic Helical Membrane Proteins
Youkharibache, P., Tran, A., & Abrol, R. (2020) · Journal of Molecular Evolution · doi:10.1007/s00239-020-09934-4 · Cited by 8
Self-citation
Monoterpenes Differently Regulate Acid-Sensitive and Mechano-Gated K2P Channels
Arazi, E., Blecher, G., & Zilberberg, N. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00704 · Cited by 7
Differential Potency of 2,6-Dimethylcyclohexanol Isomers for Positive Modulation of GABAA Receptor Currents
Chowdhury, L., Croft, C. J., Goel, S., Zaman, N., Tai, A. C.-S., Walch, E. M., Smith, K., Page, A., Shea, K. M., Hall, C. D., et al. (2016) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.228890 · Cited by 7
Functional characterization of neurotransmitter activation and modulation in a nematode model ligand‐gated ion channel
Heusser, S. A., Yoluk, Ö., Klement, G., Riederer, E. A., Lindahl, E. R., & Howard, R. J. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13644 · Cited by 7
Manipulations of extracellular Loop 2 in α1 GlyR ultra-sensitive ethanol receptors (USERs) enhance receptor sensitivity to isoflurane, ethanol, and lidocaine, but not propofol
Naito, A., Muchhala, K. H., Trang, J., Asatryan, L., Trudell, J. R., Homanics, G. E., Alkana, R. L., & Davies, D. L. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.03.034 · Cited by 7
Interplay of Hydrogen and Halogen Bonding in the Crystal Structures of 2,6‐Dihalogenated Phenols
Bauer, J. O., Koschabek, S., & Falk, A. (2021) · ChemistrySelect · doi:10.1002/slct.202101723 · Cited by 6
Discovery and functional characterization of N-(thiazol-2-yl)-benzamide analogs as the first class of selective antagonists of the Zinc-Activated Channel (ZAC)
Madjroh, N., Mellou, E., Davies, P. A., Söderhielm, P. C., & Jensen, A. A. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114782 · Cited by 6
Using molecular dynamics to elucidate the structural basis for function in pLGICs
Akabas, M. H. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316157110 · Cited by 6
Common Internal Allosteric Network Links Anesthetic Binding Sites in a Pentameric Ligand-Gated Ion Channel
Joseph, T. T., & Mincer, J. S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158795 · Cited by 6
Computational Studies for Structure-Based Drug Designing Against Transmembrane Receptors: pLGICs and Class A GPCRs
Payghan, P. V., Bera, I., Bhattacharyya, D., & Ghoshal, N. (2018) · Frontiers in Physics · doi:10.3389/fphy.2018.00052 · Cited by 7
Ketamine Inhibition of the Pentameric Ligand-Gated Ion Channel GLIC
Ion, B. F., Wells, M. M., Chen, Q., Xu, Y., & Tang, P. S. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.06.041 · Cited by 6
The Location and Nature of General Anesthetic Binding Sites on the Active Conformation of Firefly Luciferase; A Time Resolved Photolabeling Study
Shanmugasundararaj, S., Lehle, S., Yamodo, H. I., Husain, S. S., Tseng, C. C., Nguyen, K., Addona, G. H., & Miller, K. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029854 · Cited by 6
Anticonvulsant activity of Tetrahydrolinalool: behavioral, electrophysiological, and molecular docking approaches
da Fonsêca, D. V., Rocha, J. S., Pires, H. F. O., Filho, E. B. A., Reis, F. M. S., Cavalho, E. B. M., Silva, P. R., Pazos, N. D. N., de Sousa, N. F., Pires, H. F. O., et al. (2024) · ChemMedChem · doi:10.1002/cmdc.202400135 · Cited by 5
Structural insights into the molecular effects of the anthelmintics monepantel and betaine on the Caenorhabditis elegans acetylcholine receptor ACR-23
Liu, F., Li, T., Gong, H., Tian, F., Bai, Y., Wang, H., Yang, C., Li, Y., Guo, F., Liu, S., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00165-7 · Cited by 5
Micro-Solvation of Propofol in Propylene Glycol–Water Binary Mixtures: Molecular Dynamics Simulation Studies
Sharma, A., Kumar, V., & Chakraborty, S. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c04932 · Cited by 5
Asymmetric perturbation of pLGICs: action!
Maksay, G. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.04.003 · Cited by 5
Structure atomique de deux anesthésiques généraux liés à leur cible principale
Nury, H., Delarue, M. H., & Corringer, P. (2011) · médecine/sciences · doi:10.1051/medsci/20112712006 · Cited by 6
Self-citation
Combining Mutations and Electrophysiology to Map Anesthetic Sites on Ligand-Gated Ion Channels
Forman, S. A. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.01.014 · Cited by 5
Ethanol Modulation is Quantitatively Determined by the Transmembrane Domain of Humanα1 Glycine Receptors
Horani, S., Stater, E. P., Corringer, P., Trudell, J. R., Harris, R. A., & Howard, R. J. (2015) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.12735 · Cited by 5
Self-citation
Pharmaceuticals and Other Biomedical Applications
(2013) · Wiley eBooks · doi:10.1002/9783527651351.ch9 · Cited by 5
Structural basis for the inhibition of cystathionine-β-synthase by isoflurane and its role in anaesthesia-induced social dysfunction in mice
He, M., Wan, H., Cong, P., Li, X., Cheng, C., Huang, X., Zhang, Q., Wu, H., Li, T. X., Xu, K., et al. (2024) · British Journal of Anaesthesia · doi:10.1016/j.bja.2024.09.023 · Cited by 4
Constant-pH molecular dynamics simulations of closed and open states of a proton-gated ion channel
Jansen, A., Bauer, P., Howard, R. J., Hess, B., & Lindahl, E. R. (2026) · Biophysical Journal · doi:10.1016/j.bpj.2026.08.019 · Cited by 4
Differential regulation of volatile anesthetics on ion channels
Rajagopal, S., Sangam, S. R., & Singh, S. (2015) · International journal of Nutrition Pharmacology Neurological Diseases · doi:10.4103/2231-0738.167501 · Cited by 4
Modeling and Design for Membrane Protein Targets
Congreve, M., Bortolato, A., Brown, G., & Cooke, R. M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12358-3 · Cited by 4
Effect of sevoflurane versus propofol on neutrophil-to-lymphocyte ratio in healthy individuals: a sub-study of a randomised crossover trial
Hasselager, R. P., Madsen, S. S., Møller, K., Gögenür, I., & Asghar, M. S. (2022) · BJA Open · doi:10.1016/j.bjao.2022.100005 · Cited by 4
Study, by use of coarse-grained models, of the functionally crucial residues and allosteric pathway of anesthetic regulation of the Gloeobacter violaceus ligand-gated ion channel
Li, X. Y., Xie, F., Zhang, J. C., & Su, J. G. (2014) · European Biophysics Journal · doi:10.1007/s00249-014-0992-7 · Cited by 4
Phenylalanine in the Pore of the Erwinia Ligand-Gated Ion Channel Modulates Picrotoxinin Potency but Not Receptor Function
Thompson, A. J., Alqazzaz, M., Price, K. L., Weston, D. A., & Lummis, S. C. R. (2014) · Biochemistry · doi:10.1021/bi5008035 · Cited by 4
Mechanism of human α3β GlyR regulation by intracellular M3/M4 loop phosphorylation and 2,6-di-tert-butylphenol interaction
Liu, X., Krezel, M., & Wang, W. (2025) · Nature Communications · doi:10.1038/s41467-025-60516-8 · Cited by 3
Orthosteric- versus allosteric-dependent activation of the GABAA receptor requires numerically distinct subunit level rearrangements
Αmin, J., & Subbarayan, M. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-08031-9 · Cited by 3
In silico studies of the interactions between propofol and fentanyl using Gaussian accelerated molecular dynamics
Faulkner, C., & de Leeuw, N. H. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1814415 · Cited by 3
Fumarate as positive modulator of allosteric transitions in the pentameric ligand‐gated ion channel GLIC: requirement of an intact vestibular pocket
Renterghem, C. V., Nemecz, Á., Delarue‐Cochin, S., Joseph, D., & Corringer, P. (2023) · The Journal of Physiology · doi:10.1113/jp283765 · Cited by 3
Self-citation
The Unfolding Story of How General Anesthetics Act
Franks, N. P. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8441-7_45 · Cited by 3
Organofluorine Anesthetics
Reddy, V. P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-444-53748-5.00006-x · Cited by 3
A regulatory domain in the K2P2.1 (TREK-1) carboxyl-terminal allows for channel activation by monoterpenes
Arazi, E., Blecher, G., & Zilberberg, N. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2020.103496 · Cited by 3
Competitive dewetting underlies site-specific binding of general anesthetics to GABA(A) receptorsPreprint
Murlidaran, S., Hénin, J., & Brannigan, G. H. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/694612 · Cited by 3
Silapropofol: Carbon–Silicon Isosterism in a Key Anesthetic Scaffold
Koschabek, S., Kleemiss, F., Espinosa-Jalapa, N. Á., & Bauer, J. O. (2026) · ACS Omega · doi:10.1021/acsomega.5c11217 · Cited by 2
Membrane Protein Production in Escherichia coli: Overview and Protocols
Hattab, G., Suisse, A., Ilioaia, O., Casiraghi, M., Dezi, M., Warnet, X. L., Warschawski, D. E., Moncoq, K., Zoonens, M. A., & Miroux, B. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0662-8_4 · Cited by 2
Foundations of Biomolecular Simulations: A Critical Introduction to Homology Modeling, Molecular Dynamics Simulations, and Free Energy Calculations of Membrane Proteins
Hénin, J., Baaden, M., & Taly, A. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0662-8_13 · Cited by 2
Self-citation
N,6-dimethyltricyclo[5.2.1.02,6]decan-2-amine enantiomers interact with the human α4β2 nicotinic acetylcholine receptor at luminal and non-luminal domains
Arias, H., Targowska‐Duda, K. M., & Jozwiak, K. (2013) · OA Biochemistry · doi:10.13172/2052-9651-1-2-972 · Cited by 2
Free Energy Calculations for Understanding Membrane Receptors
Pohorille, A. (2016) · Royal Society of Chemistry eBooks · doi:10.1039/9781782626695-00059 · Cited by 2
X-Ray Crystallographic Studies for Revealing Binding Sites of General Anesthetics in Pentameric Ligand-Gated Ion Channels
Chen, Q., Xu, Y., & Tang, P. S. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.01.017 · Cited by 2
Characterization of the dynamic resting state of a pentameric ligand-gated ion channel by cryo-electron microscopy and simulationsPreprint
Rovšnik, U., Zhuang, Y., Axelsson, L., Forsberg, B. O., Lim, V. T., Carroni, M., Blau, C., Howard, R. J., & Lindahl, E. R. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.19.161356 · Cited by 2
The essence of using plant essential oils for pest control
Wong, C. R. (2021) · doi:10.31274/td-20240329-752 · Cited by 2
Mechanisms of Intravenous Anesthetic Action
Hemmings, H. C., & Herold, K. F. (2017) · Springer eBooks · doi:10.1007/978-3-319-47609-4_5 · Cited by 1
Comparative studies on the binding site of anesthetics to GABA a receptors using in silico docking methods
Ahn, S., LEE, J.-Y., Sung, J., Kim, H. J., & PARK, S. (2023) · Biocell · doi:10.32604/biocell.2023.027984 · Cited by 1
GAPDH in Anesthesia
Seidler, N. W. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-4716-6_9 · Cited by 1
COMparative BINding Energy (COMBINE) Analysis as a Structure-Based 3D-QSAR Method
Morreale, A., & Gago, F. (2012) · Royal Society of Chemistry eBooks · doi:10.1039/9781849735377-00244 · Cited by 1
Volatile anaesthetics modulate voltage-gated sodium channel function at a site directly linked to channel gating
Hollingworth, D., Herold, K. F., Kelly, G. P., Mikhailik, V. B., Zhang, D., Wallace, B. A., & Hemmings, H. C. (2026) · Nature Communications · doi:10.1038/s41467-026-74518-7 · Cited by 1
Mechanisms of anaesthetics: lessons learned from creatures great and small
Hales, T. G. (2011) · Anaesthesia · doi:10.1111/j.1365-2044.2011.06723.x · Cited by 1
Structural Basis for Allosteric Coupling at the Membrane-Protein Interface in GLIC
Velisetty, P., Chalamalasetti, S. V., & Chakrapani, S. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2013.11.3552 · Cited by 1
Solution NMR Studies of Anesthetic Interactions with Ion Channels
Bondarenko, V., Wells, M. M., Xu, Y., & Tang, P. S. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.01.018 · Cited by 1
Stabilizing membrane domains antagonizes n-alcohol anesthesiaPreprint
Machta, B. B., Grey, E., Nouri, M., McCarthy, N. L. C., Gray, E. M., Miller, A. L., Brooks, N. J., & Veatch, S. L. (2016) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/057257 · Cited by 1
7-Transmembrane Helical (7TMH) Proteins: Pseudo-Symmetry and Conformational PlasticityPreprint
Youkharibache, P., Tran, A., & Abrol, R. (2018) · bioRxiv · doi:10.1101/465302
Self-citation
Identification of novel allosteric modulators of the glycine receptor using phage display technology
Tipps, M. E. (2011) · Texas ScholarWorks (Texas Digital Library)
Nicotinic and other Cys-loop receptors: From identification to mechanisms of action and creation of new drugs
Tsetlin, V. I. (2013) · Nanotechnologies in Russia · doi:10.1134/s1995078013030208
Probing residues in the pore-forming (M2) domain of the Cys-loop receptor homologue GLIC reveals some unusual features
Alqazzaz, M., & Lummis, S. C. R. (2015) · Molecular Membrane Biology · doi:10.3109/09687688.2015.1023377
Design and biophysical characterization of a monomeric four-alpha-helix bundle protein Aα4 with affinity for the volatile anesthetic halothane
Morstadt, L. M., Meng, Q. C., & Johansson, J. S. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.06.007
Mechanisms of general anesthetic action: Focus on the cellular network
Turina, D., & Björnström, K. (2011) · Translational Neuroscience · doi:10.2478/s13380-011-0022-5
Structural Understanding of Ion Channels in Atomic Detail
Stansfeld, P. J. (2014) · Royal Society of Chemistry eBooks · doi:10.1039/9781849735087-00056
Propofol changes the cytoskeletal function in neurons : An experimental study in cortical cultures
Turina, D. (2012) · DiVA (Linkoping University)
How to prepare for the biomedical equipment technician certification exam.
Xu, Y. (1996) · PubMed
Mapping the Allosteric Pathway Leading from a Mutation in the Nicotinic Acetylcholine Receptor to a Congenital Myasthenic Syndrome
Domville, J. A. (2017) · uO Research (University of Ottawa) · doi:10.20381/ruor-21309
Mécanismes d'immunomodulation par les alcanols aliphatiques
Carignan, D. (2013) · Corpus Université Laval (Université Laval)
Membrane Proteins and Their Natural Environment
Popot, J. (2018) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-73148-3_1
Ion Channel Simulations
Pandey, S. K., Bonhenry, D., & Ettrich, R. H. (2018) · Methods and principles in medicinal chemistry · doi:10.1002/9783527806836.ch10
Current World Literature
(2012) · Current Opinion in Anaesthesiology · doi:10.1097/aco.0b013e3283521230
Protein Function | Allostery in Proteins: Canonical Models and New Insights
Kim, E. D., Kim, C. D., Chaney, J., & Kim, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00259-0
Faculty Opinions recommendation of Crystal structures of a GABAA-receptor chimera reveal new endogenous neurosteroid-binding sites.
Wulff, H. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.731602723.793537544
Self-Monitoring
Lou, H. C. (2021) · Springer eBooks · doi:10.1007/978-3-319-19650-3_3125
Self-Monitoring
Lou, H. C. (2017) · Springer eBooks · doi:10.1007/978-3-319-16999-6_3125-1
Discovery of lipid binding sites in a ligand-gated ion channel by integrating simulations and cryo-EMPreprint
Bergh, C. C., Rovšnik, U., Howard, R. J., & Lindahl, E. R. (2023) · eLife · doi:10.7554/elife.86016.1
eLife assessment: Discovery of lipid binding sites in a ligand-gated ion channel by integrating simulations and cryo-EM
Goldschen-Ohm, M. P. (2024) · eLife · doi:10.7554/elife.86016.3.sa0
Effects of the γ2 K289M mutation on the structure and function of GABA Type A Receptors: Insights from molecular dynamics simulations
Patel, A., & Patel, R. (2022) · World Journal of Biological and Pharmaceutical Research · doi:10.53346/wjbpr.2022.2.1.0023
Etude de la dimérisation et de la dynamique structurale des mGluR par la technologie trFRET : de nouvelles pistes pour de nouveaux médicaments
Doumazane, E. (2011) · theses.fr (ABES) · doi:10.70675/35aad135z0f70z4530zb264za9a154b42494
The role of the nicotinic receptors in prefrontal cortex spontaneous neuronal activity in the normal and diseased brain
Koukouli, F. (2016) · theses.fr (ABES) · doi:10.70675/83df9f57z48cfz4372z8c94za5f54e4b5e30
Structural and functional studies of pentameric ligand-gated ion channels from bacteria
Hu, H. (2017) · doi:10.70675/1a714cd3zcdf6z4190z946ez5527effc0116
Applications de la fluorescence pour la caractérisation structurale et dynamique d'intermédiaires conformationnels des récepteurs-canaux pentamériques
Lefebvre, S. N. (2019) · theses.fr (ABES) · doi:10.70675/95b39d7aza5f4z49c3zac3ez79bfe67b2f97

Authors: Nury, H., Van Renterghem, C., Weng, Y., Tran, A., Baaden, M., Dufresne, V., Changeux, J.-P., Sonner, J. M., Delarue, M., & Corringer, P.-J.
Affiliations: Institut Pasteur (FR)
University of California, San Francisco (US)
Centre National de la Recherche Scientifique (FR)
Corresponding author: Changeux, Jean-Pierre
Delarue, Marc
Corringer, Pierre-Jean
ORCID: Nury, Hugues
Baaden, Marc
Changeux, Jean-Pierre
Delarue, Marc
Corringer, Pierre-Jean
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2011-01
Volume: 469
Issue: 7330
Pages: 428-431
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature09647
OpenAlex: W2104389482
Cited by: 412
References: 48
Citations by year: 2026: 5 · 2025: 2 · 2024: 8 · 2023: 8 · 2022: 8 · 2021: 23 · 2020: 18 · 2019: 21 · 2018: 28 · 2017: 32 · 2016: 33 · 2015: 34 · 2014: 36 · 2013: 62 · 2012: 56
FWCI: 25.08
Type: journal article
Language: en
Open access: green
infoscience.epfl.ch
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
RePEc: Research Papers in Economics (submittedVersion)
eScholarship (California Digital Library) (submittedVersion)
Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
Funders: National Institute of General Medical Sciences (R01GM069379)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
Health Sciences › Medicine › Anesthesiology and Pain Medicine › Anesthesia and Sedative Agents
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords: general anesthetics, pentameric ligand-gated ion channels, propofol, desflurane, transmembrane domain, allosteric modulators, proton sensitivity, molecular dynamics simulation, GABAA receptor, nicotinic acetylcholine receptors
MeSH terms: Desflurane, Cyanobacteria, Binding Sites, Isoflurane, Ligands, Models, Molecular, Protein Binding, Protons, Propofol, Protein Structure, Tertiary, Crystallography, X-Ray, Anesthetics, General, Mutant Proteins, Electrophysiological Phenomena, Molecular Dynamics Simulation, Ligand-Gated Ion Channels

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks