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Author Correction: GABA_A receptor signalling mechanisms revealed by structural pharmacology

Simonas Masiulis
Rooma Desai
A. Radu Aricescu
Amendments and Corrections07 Feb 2019
Nature

Volume: 566, P: E8
Allosteric nanobodies to study the interactions between SOS1 and RAS

Protein-protein interactions are central in cell metabolism but research tools for their characterization are missing. Here, the authors introduce strategies for the discovery of nanobodies that modulate the SOS1•RAS complex formation.

Baptiste Fischer
Tomasz Uchański
Jan Steyaert
ResearchOpen Access23 Jul 2024
Nature Communications

Volume: 15, P: 1-10
Single-particle cryo-EM at atomic resolution

Advances in electron cryo-microscopy hardware allow proteins to be studied at atomic resolution.

Takanori Nakane
Abhay Kotecha
Sjors H. W. Scheres
Research21 Oct 2020
Nature

Volume: 587, P: 152-156
GABA_A receptor signalling mechanisms revealed by structural pharmacology

Cryo-electron microscopy structures are reported in which the full-length human α1β3γ2L GABA_A receptor in lipid nanodiscs is bound to the channel-blocker picrotoxin, the competitive antagonist bicuculline, the agonist GABA, and the benzodiazepines alprazolam and diazepam.

Simonas Masiulis
Rooma Desai
A. Radu Aricescu
Research02 Jan 2019
Nature

Volume: 565, P: 454-459
Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM

Megabodies, built by grafting nanobodies onto larger protein scaffolds, help alleviate problems of particle size and preferential orientation at the water–air interfaces during cryo-EM based structure determination experiments and are shown to be generalizable to soluble and membrane-bound proteins.

Tomasz Uchański
Simonas Masiulis
Jan Steyaert
Research06 Jan 2021
Nature Methods

Volume: 18, P: 60-68
Cryo-EM structure of the human α1β3γ2 GABA_A receptor in a lipid bilayer

A high-resolution cryo-electron microscopy structure is reported for the full-length human α1β3γ2L GABA_A receptor, functionally reconstituted in lipid nanodiscs.

Duncan Laverty
Rooma Desai
A. Radu Aricescu
Research02 Jan 2019
Nature

Volume: 565, P: 516-520
An improved yeast surface display platform for the screening of nanobody immune libraries

Tomasz Uchański
Thomas Zögg
Jan Steyaert
ResearchOpen Access23 Jan 2019
Scientific Reports

Volume: 9, P: 1-12

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Author Correction: GABAA receptor signalling mechanisms revealed by structural pharmacology

Allosteric nanobodies to study the interactions between SOS1 and RAS

Single-particle cryo-EM at atomic resolution

GABAA receptor signalling mechanisms revealed by structural pharmacology

Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM

Cryo-EM structure of the human α1β3γ2 GABAA receptor in a lipid bilayer

An improved yeast surface display platform for the screening of nanobody immune libraries

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Author Correction: GABA_A receptor signalling mechanisms revealed by structural pharmacology

GABA_A receptor signalling mechanisms revealed by structural pharmacology

Cryo-EM structure of the human α1β3γ2 GABA_A receptor in a lipid bilayer