Author

M. J. Belousoff

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 7 Pharmacology & Toxicology· 4 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 11 Assay:cryo-EM· 7 Research Focus:host-pathogen & immune response· 4 Organism:human· 4 Assay:structural biology· 4 Research Focus:drug response / drug discovery· 3 Research Focus:protein folding & dynamics· 3 Research Focus:protein structure prediction· 3

Frequent Co-Authors

D. Wootten· 7 shared P. M. Sexton· 7 shared R. Danev· 7 shared H. Venugopal· 6 shared A. Christopoulos· 4 shared X. Zhang· 4 shared Y.-L. Liang· 4 shared A. Glukhova· 3 shared

Activity by Year

2020-2022 · peak 6/yr

Co-Author Collaboration Network

10 top collaborators · 42 mutual co-author links

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7 shared papersPharmacology & Toxicology

D. Wootten

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Author profile →

12 papers

Recent·Most cited

Energy extraction from air: structural basis of atmospheric hydrogen oxidation

R. Grinter, A. Kropp, H. Venugopal, M. Senger, J. Badley, P. Cabotaje, S. T. Stripp, C. Barlow, M. J. Belousoff, G. M. Cook, K. Vincent, R. B. Schittenhelm, S. Khalid, G. Berggren, C. Greening

This paper determines the structure of a mycobacterial hydrogenase and explains how it selectively oxidizes atmospheric H2 while avoiding O2, enabling energy extraction from air.

bioRxiv · Oct 9, 2022 · PreprintBiochemistry

Pharmacological hallmarks of allostery at the M4 muscarinic receptor elucidated through structure and dynamics

Z. Vuckovic, J. Wang, V. Pham, J. I. Mobbs, M. J. Belousoff, A. Bhattarai, W. A. C. Burger, G. Thompson, M. Yeasmin, K. Leach, E. T. van der Westhuizen, E. Khajehali, Y.-L. Liang, A. Glukhova, D. Wootten, , D. M. Thal

The paper presents cryo-EM structures of the M4 mAChR with ligands and modulators, revealing structural and dynamic insights into allosteric modulation and receptor activation mechanisms.

bioRxiv · Sep 27, 2022Pharmacology & Toxicology

Molecular insights into peptide agonist engagement with the PTH1 receptor

B. P. Cary, E. J. Gerrard, M. J. Belousoff, M. M. Fletcher, Y. Jiang, I. C. Russell, S. J. Piper, D. Wootten, P. M. Sexton

This study presents cryo-EM structures of the PTH1R bound to various agonists, revealing how different peptides engage the receptor and providing insights for drug design.

bioRxiv · Sep 4, 2022 · PreprintBiochemistry

Discovery and Biosynthesis of Persiathiacins: Unusual Polyglycosylated Thiopeptides Active against Multi-drug resistant Tuberculosis

Y. Dashti, F. Mohammadipanah, M. J. Belousoff, A. Vocat, D. Zabala, C. D. Fage, I. Romero-Canelon, B. Bunk, C. Sproer, J. Overmann, S. T. Cole, G. L. Challis

This study discovers two novel polyglycosylated thiopeptides, persiathiacins A and B, active against drug-resistant tuberculosis and identifies their biosynthetic gene cluster.

bioRxiv · Oct 24, 2021 · PreprintMicrobiology

Structures of the human cholecystokinin 1 (CCK1) receptor bound to Gs and Gq mimetic proteins: insight into mechanisms of G protein selectivity

J. Mobbs, M. J. Belousoff, K. G. Harikumar, S. J. Piper, X. Xu, S. G. B. Furness, H. Venugopal, A. Christopoulos, R. Danev, D. Wootten, D. M. Thal, L. J. Miller, P. M. Sexton

The paper determines cryo-EM structures of the CCK1R bound to Gs and Gq proteins, revealing conformational changes that enable promiscuous G protein coupling.

bioRxiv · May 6, 2021Pharmacology & Toxicology

Dynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation

G. Deganutti, Y.-L. Liang, X. Zhang, M. Khoshouei, L. Clydesdale, M. J. Belousoff, H. Venugopal, T. T. Truong, A. Glukhova, A. N. Keller, K. J. Gregory, K. Leach, A. Christopoulos, R. Danev, C. A. Reynolds, , D. M. Wootten

The paper investigates how different GLP-1R agonists affect G protein activation kinetics through structural and functional analyses.

bioRxiv · Mar 10, 2021Biochemistry

Structural and Functional Diversity among Agonist-Bound States of the GLP-1 Receptor

B. P. Cary, P. Zhao, T. T. Truong, S. J. Piper, M. J. Belousoff, R. Danev, P. M. Sexton, D. Wootten, S. H. Gellman

This study investigates how peptide agonist conformational plasticity influences GLP-1R activation through structural and functional analysis.

bioRxiv · Feb 24, 2021Pharmacology & Toxicology

Structure and dynamics of semaglutide and taspoglutide bound GLP-1R-Gs complexes

X. Zhang, M. J. Belousoff, Y.-L. Liang, R. Danev, P. M. Sexton, D. Wootten

This study determines cryo-EM structures of GLP-1R-Gs complexes bound with semaglutide and taspoglutide, revealing similar peptide binding modes but distinct 3D motions compared to GLP-1.

bioRxiv · Jan 12, 2021Biochemistry

Evolving cryo-EM structural approaches for GPCR drug discovery

X. Zhang, R. M. Johnson, I. Drulyte, L. Yu, A. Kotecha, R. Danev, D. Wootten, P. M. Sexton, M. J. Belousoff

This study validates stable GPCR:Gs complexes without Nb35 stabilizers and evaluates 200kV vs 300kV cryo-EM imaging for drug discovery.

bioRxiv · Jan 11, 2021Biochemistry

Metal Dependent Dynamic Equilibrium: A Regulatory Mechanism for M17 Aminopeptidases from Plasmodium falciparum and Plasmodium vivax

T. R. Malcolm, M. J. Belousoff, H. Venugopal, N. A. Borg, N. Drinkwater, S. C. Atkinson, S. McGowan

This study identifies a metal-dependent dynamic equilibrium in M17 aminopeptidases from Plasmodium species that regulates hexamer formation and catalytic activity.

bioRxiv · Oct 8, 2020 · PreprintBiochemistry

Differential GLP-1R binding and activation by peptide and non-peptide agonists

X. Zhang, M. J. Belousoff, P. Zhao, A. J. Kooistra, T. T. Truong, S. Y. Ang, C. R. Underwood, T. Egebjerg, P. Senel, G. D. Stewart, Y.-L. Liang, A. Glukhova, H. Venugopal, A. Christopoulos, S. G. Furness, , D. Wootten

The paper compares the binding and activation of the GLP-1 receptor by peptide and non-peptide agonists, revealing structural and functional differences that inform drug design.

bioRxiv · Aug 16, 2020Pharmacology & Toxicology

Structural basis for control of antibiotic production by bacterial hormones

S. Zhou, H. Bhukya, N. Malet, P. J. Harrison, D. Rea, M. J. Belousoff, H. Venugopal, P. K. Sydor, K. M. Styles, L. Song, M. J. Cryle, L. M. Alkhalaf, V. Fülöp, G. L. Challis, C. Corre

This study determines the structural basis for hormone-controlled antibiotic production in Actinobacteria by solving the X-ray structure of an MmfR-AHFCA complex and elucidating DNA release mechanisms.

bioRxiv · May 2, 2020Biochemistry