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Cryo-EM structure of haemoglobin at 3.2 Å determined with the Volta phase plate

Single particle cryo-EM is commonly used for the structure determination of large complexes. Here, the authors present the 3.2 Å resolution cryo-EM structure of human haemoglobin, which has a molecular weight of 64 kDa.

Maryam Khoshouei
Mazdak Radjainia
Radostin Danev
ResearchOpen Access30 Jun 2017
Nature Communications

Volume: 8, P: 1-6
Volta phase plate cryo-EM of the small protein complex Prx3

Although the resolution achievable with cryo-EM can now rival crystallography, its application to small protein assemblies remains challenging. Here the authors demonstrate the use of the Volta phase plate for single particle analysis and its potential for the study of small specimens.

Maryam Khoshouei
Mazdak Radjainia
Radostin Danev
ResearchOpen Access28 Jan 2016
Nature Communications

Volume: 7, P: 1-5
Dynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation

The glucagon-like peptide-1 receptor (GLP-1R) can be targeted in the treatment of diabetes, obesity and other metabolic disorders. Here, the authors assess the molecular mechanisms of peptide agonists binding to GLP-1R and the responses elucidated by these ligands, including distinct kinetics of G protein activation.

Giuseppe Deganutti
Yi-Lynn Liang
Denise Wootten
ResearchOpen Access10 Jan 2022
Nature Communications

Volume: 13, P: 1-18
Cryo-EM structure of the active, G_s-protein complexed, human CGRP receptor

The structure of a complex containing calcitonin gene-related peptide, the human calcitonin gene-related peptide receptor and the G_s heterotrimer, determined using Volta phase-plate cryo-electron microscopy, provides structural insight into the regulation of G-protein-coupled receptors by receptor activity modifying protein 1.

Yi-Lynn Liang
Maryam Khoshouei
Patrick M. Sexton
Research12 Sept 2018
Nature

Volume: 561, P: 492-497
Structure of the adenosine-bound human adenosine A₁ receptor–G_i complex

The cryo-electron microscopy structure of the human adenosine A₁ receptor in complex with adenosine and heterotrimeric G_i2 protein provides molecular insights into receptor and G-protein selectivity.

Christopher J. Draper-Joyce
Maryam Khoshouei
Arthur Christopoulos
Research20 Jun 2018
Nature

Volume: 558, P: 559-563
Structure and dynamics of the active Gs-coupled human secretin receptor

The class B secretin GPCR (SecR) has broad physiological effects, with target potential for treatment of metabolic and cardiovascular disease. Here, authors present a cryo-EM structure and biochemical studies of secretin binding to the SecR:Gs complex which show that interactions between peptide and receptor were dynamic.

Maoqing Dong
Giuseppe Deganutti
Laurence J. Miller
ResearchOpen Access18 Aug 2020
Nature Communications

Volume: 11, P: 1-17
Phase-plate cryo-EM structure of a class B GPCR–G-protein complex

Volta phase-plate cryo-electron microscopy reveals the structure of the full-length calcitonin receptor in complex with its peptide ligand and Gα_sβγ.

Yi-Lynn Liang
Maryam Khoshouei
Patrick M. Sexton
Research24 Apr 2017
Nature

Volume: 546, P: 118-123
Author Correction: DCAF1-based PROTACs with activity against clinically validated targets overcoming intrinsic- and acquired-degrader resistance

Martin Schröder
Martin Renatus
Claudio R. Thoma
Amendments and CorrectionsOpen Access19 Aug 2024
Nature Communications

Volume: 15, P: 1-5
DCAF1-based PROTACs with activity against clinically validated targets overcoming intrinsic- and acquired-degrader resistance

Targeted protein degradation (TPD) is a key modality for drug discovery. Here the authors present the discovery and analysis of reversible DCAF1-PROTACs, which show efficacy in cellular environments resistant to VHL-PROTACs or with acquired resistance to CRBN-PROTACs.

Martin Schröder
Martin Renatus
Claudio R. Thoma
ResearchOpen Access04 Jan 2024
Nature Communications

Volume: 15, P: 1-19
Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor–Gs complex

The structure of the glucagon-like peptide 1 receptor (GLP-1R) with its biased agonist exendin-P5 sheds light on both receptor activation and the mechanism of biased agonism.

Yi-Lynn Liang
Maryam Khoshouei
Denise Wootten
Research21 Feb 2018
Nature

Volume: 555, P: 121-125

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