Cargando…

Cryo-EM structure of the human α1β3γ2 GABA(A) receptor in a lipid bilayer

Type A γ-aminobutyric acid receptors (GABA(A)Rs) are pentameric ligand-gated ion channels (pLGICs) and the main drivers of fast inhibitory neurotransmission in the vertebrate nervous system1,2. Their dysfunction is implicated in a range of neurological disorders, including depression, epilepsy and s...

Descripción completa

Detalles Bibliográficos
Autores principales:	Laverty, Duncan, Desai, Rooma, Uchański, Tomasz, Masiulis, Simonas, Stec, Wojciech J., Malinauskas, Tomas, Zivanov, Jasenko, Pardon, Els, Steyaert, Jan, Miller, Keith W., Aricescu, A. Radu
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	2019
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6364807/ https://www.ncbi.nlm.nih.gov/pubmed/30602789 http://dx.doi.org/10.1038/s41586-018-0833-4

Ejemplares similares

GABA(A) receptor signalling mechanisms revealed by structural pharmacology
por: Masiulis, Simonas, et al.
Publicado: (2019)

A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis
por: Zivanov, Jasenko, et al.
Publicado: (2019)

Estimation of high-order aberrations and anisotropic magnification from cryo-EM data sets in RELION-3.1
por: Zivanov, Jasenko, et al.
Publicado: (2020)

New tools for automated high-resolution cryo-EM structure determination in RELION-3
por: Zivanov, Jasenko, et al.
Publicado: (2018)

High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
por: Righetto, Ricardo D., et al.
Publicado: (2020)

Cryo-EM Structure of an Atypical Proton-Coupled Peptide Transporter: Di- and Tripeptide Permease C
por: Killer, Maxime, et al.
Publicado: (2022)

Author Correction: High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica
por: Righetto, Ricardo D., et al.
Publicado: (2020)

Crystal structure of a human GABA(A) receptor
por: Miller, Paul S., et al.
Publicado: (2014)

Cryo-EM structures reveal native GABA(A) receptor assemblies and pharmacology
por: Sun, Chang, et al.
Publicado: (2023)

CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers
por: Menny, Anaïs, et al.
Publicado: (2018)

Cryo-EM structure of GABA transporter 1 reveals substrate recognition and transport mechanism
por: Nayak, Smruti Ranjan, et al.
Publicado: (2023)

Cryo-EM structure of type 1 IP(3)R channel in a lipid bilayer
por: Baker, Mariah R., et al.
Publicado: (2021)

Cryo-EM structure of the benzodiazepine-sensitive α1β1γ2S tri-heteromeric GABA(A) receptor in complex with GABA
por: Phulera, Swastik, et al.
Publicado: (2018)

An improved yeast surface display platform for the screening of nanobody immune libraries
por: Uchański, Tomasz, et al.
Publicado: (2019)

A snapshot of cryo‐EM
por: Skiniotis, Georgios
Publicado: (2016)

Interpreting the cryo-EM map
por: Rosenthal, Peter B.
Publicado: (2019)

COVID-19 and cryo-EM
por: Subramaniam, Sriram
Publicado: (2020)

Cryo-EM at ACA 2022
por: Subramaniam, Sriram, et al.
Publicado: (2022)

Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer
por: Sengupta, Nayanika, et al.
Publicado: (2021)

Tools for the cryo-EM gold rush: going from the cryo-EM map to the atomistic model
por: Kim, Doo Nam, et al.
Publicado: (2017)

A Bayesian approach to single-particle electron cryo-tomography in RELION-4.0
por: Zivanov, Jasenko, et al.
Publicado: (2022)

CryoEM structure of the spliceosome immediately after branching
por: Galej, Wojciech P., et al.
Publicado: (2016)

Exploring applications of crowdsourcing to cryo-EM
por: Bruggemann, Jacob, et al.
Publicado: (2018)

Cryo-EM Structure of the Exocyst Complex
por: Mei, Kunrong, et al.
Publicado: (2018)

Density modification of cryo-EM maps
por: Terwilliger, Thomas C., et al.
Publicado: (2020)

Fast multiscale reconstruction for Cryo-EM()
por: Donati, Laurène, et al.
Publicado: (2018)

Cryo‐EM targets in CASP14
por: Cragnolini, Tristan, et al.
Publicado: (2021)

Cryo-EM structure of the SEA complex
por: Tafur, Lucas, et al.
Publicado: (2022)

Cryo‐EM structures of coagulation factors
por: Di Cera, Enrico, et al.
Publicado: (2022)

AlphaFold2 and CryoEM: Revisiting CryoEM modeling in near-atomic resolution density maps
por: Hryc, Corey F., et al.
Publicado: (2022)

Detergents and alternatives in cryo-EM studies of membrane proteins: Detergents and alternatives in cryo-EM studies of membrane proteins
por: Li, Shuo
Publicado: (2022)

‘Cryo-EM’: electron cryomicroscopy, cryo electron microscopy or something else?
por: Henderson, Richard, et al.
Publicado: (2023)

High-level production and purification in a functional state of an extrasynaptic gamma-aminobutyric acid type A receptor containing α4β3δ subunits
por: Zhou, Xiaojuan, et al.
Publicado: (2018)

Topaz-Denoise: general deep denoising models for cryoEM and cryoET
por: Bepler, Tristan, et al.
Publicado: (2020)

CryoDRGN: Reconstruction of heterogeneous cryo-EM structures using neural networks
por: Zhong, Ellen D., et al.
Publicado: (2021)

In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM
por: Huang, Cheng-Yu, et al.
Publicado: (2022)

Cryo-EM enters a new era
por: Kühlbrandt, Werner
Publicado: (2014)

The Local Resolution of Cryo-EM Density Maps
por: Kucukelbir, Alp, et al.
Publicado: (2013)

Cryo-EM structure of the mitochondrial calcium uniporter
por: Nguyen, Nam X., et al.
Publicado: (2018)

Cryo-EM structure of alpha-synuclein fibrils
por: Guerrero-Ferreira, Ricardo, et al.
Publicado: (2018)

Cannot write session to /tmp/vufind_sessions/sess_jf0o01o21b3grffb73bs5p8dhj