Author

J. Munro

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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Microbiology· 2 Biochemistry· 1 Biophysics· 1 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 4 Organism:human· 2 Organism:mouse· 2 Assay:bulk RNA-seq· 1 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

J. Luban· 2 shared M. Llinas· 2 shared A. Barve· 1 shared A. Baum· 1 shared A. Berkman· 1 shared A. C. Aguiar· 1 shared A. Churchyard· 1 shared A. D. Campbell· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersBiophysics

J. Luban

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

eIF4A1 is essential for reprogramming the translational landscape of Wnt-driven colorectal cancers

J. A. Waldron, G. Kanellos, R. C. L. Smith, J. R. P. Knight, J. Munro, C. Alexandrou, N. Vlahov, L. Pardo-Fernandez, M. Moore, S. L. Gillen, D. Strathdee, D. Stevenson, F. C. Warrander, K. Gilroy, C. Nixon, , O. J. Sansom

This study shows eIF4A1 is critical for supporting translational demands in Wnt-driven colorectal cancers, while eIF4A2 loss accelerates tumourigenesis, and eFT226 inhibits eIF4A1 function in these models.

bioRxiv · Nov 10, 2023 · PreprintCancer Biology

Regulation of Ebola GP conformation and membrane binding by the chemical environment of the late endosome

A. Jain, R. Govindan, A. Berkman, J. Luban, N. D. Durham, J. Munro

This study investigates how acidic pH, Ca2+, and anionic phospholipids in the late endosome regulate Ebola GP conformation and membrane binding, revealing key residues and mechanisms involved in virus entry.

bioRxiv · Jan 18, 2023Biophysics

Preclinical characterization and target validation of the antimalarial pantothenamide MMV693183

L. E. de Vries, P. A. Jansen, C. Barcelo, J. Munro, J. M. Verhoef, C. F. A. Pasaje, K. Rubiano, J. Striepen, J. M. Bolscher, R. Henderson, T. Huijs, K. M. Koolen, P. K. Tumwebaze, T. Yeo, A. C. Aguiar, , K. J. Dechering

This paper characterizes MMV693183, a novel antimalarial compound targeting acetyl-CoA synthetase, showing in vitro and in vivo efficacy against Plasmodium species and transmission blocking.

bioRxiv · May 12, 2021Microbiology

Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant

L. Yurkovetskiy, X. Wang, K. E. Pascal, C. Tompkins-Tinch, T. Nyalile, Y. Wang, A. Baum, W. E. Diehl, A. Dauphin, C. Carbone, K. Veinotte, S. B. Egri, S. F. Schaffner, J. E. Lemieux, J. Munro, , J. Luban

This study shows the D614G SARS-CoV-2 spike protein variant is more infectious but has reduced ACE2 affinity and altered trimer conformation, affecting viral entry and antibody neutralization.

bioRxiv · Jul 4, 2020Microbiology

Genetic ablation of the mitochondrial ribosome in Plasmodium falciparum sensitizes the human malaria parasite to antimalarial drugs targeting mitochondrial functions

L. Ling, M. Mulaka, J. Munro, S. Dass, M. W. Mather, M. K. Riscoe, M. Llinas, J. Zhou, H. Ke

This study shows that disrupting the mitochondrial ribosome in Plasmodium falciparum makes the parasite more sensitive to drugs targeting mitochondrial functions.

bioRxiv · Jan 14, 2020 · PreprintBiochemistry