Author

M. J. Conley

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· 3

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Assay:cryo-EM· 2 Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

D. Bhella· 3 shared I. G. Goodfellow· 2 shared J. Streetley· 2 shared A. M. Burns· 1 shared B. J. Power· 1 shared E. Emmott· 1 shared G. Zanetti· 1 shared H. Jaffery· 1 shared

Activity by Year

2018-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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3 shared papersMicrobiology

D. Bhella

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Helical Ordering of Envelope Associated Proteins and Glycoproteins in Respiratory Syncytial Virus Filamentous Virions

M. J. Conley, J. M. Short, J. Hutchings, A. M. Burns, J. Streetley, S. E. Bakker, H. Jaffery, M. Stewart, B. J. Power, G. Zanetti, R. Fearns, S. Vijayakrishnan, D. Bhella

This study uses cryoEM and cryoET to reveal helical symmetry in RSV virions, showing how M proteins and glycoproteins are organized and their implications for vaccine targets.

bioRxiv · Aug 4, 2021Microbiology

The cryo-EM structure of vesivirus 2117 highlights functional variations in entry pathways for viruses in different clades of the vesivirus genus.

H. Sutherland, M. J. Conley, E. Emmott, J. Streetley, I. G. Goodfellow, D. Bhella

This study determines the cryo-EM structure of vesivirus 2117, revealing structural differences in the capsid that suggest variations in entry pathways among vesivirus clades.

bioRxiv · Feb 5, 2021Microbiology

Calicivirus VP2 forms a portal to mediate endosome escape

M. J. Conley, M. McElwee, L. B. Azmi, M. Gabrielsen, O. Byron, I. G. Goodfellow, D. Bhella

This paper identifies VP2 as a portal structure in caliciviruses that facilitates endosome escape, revealing its role in viral genome release.

bioRxiv · Aug 23, 2018Microbiology