Author

C. M. Boyd

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 4 Organism:bacteria (other)· 3 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Assay:DNA methylation· 1 Research Focus:gene regulatory network inference· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

D. Bubeck· 2 shared A. Menny· 1 shared A. P. Joseph· 1 shared B. Hoogenboom· 1 shared B. P. Morgan· 1 shared D. T. Dunham· 1 shared E. S. Parsons· 1 shared K. D. Seed· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersBiochemistry

D. Bubeck

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A Vibrio cholerae viral satellite maximizes its spread and inhibits phage by remodeling hijacked phage coat proteins into small capsids

C. M. Boyd, S. Subramanian, D. T. Dunham, K. N. Parent, K. D. Seed

This study identifies TcaP as a protein that remodels phage ICP1 capsids into smaller structures, enhancing PLE satellite transduction and inhibiting ICP1.

bioRxiv · Mar 1, 2023 · PreprintMicrobiology

A phage satellite tunes inducing phage gene expression using a domesticated endonuclease to balance inhibition and virion hijacking

Z. Netter, C. M. Boyd, T. V. Silvas, K. Seed

This study reveals how the phage satellite PLE in Vibrio cholerae uses a domesticated endonuclease to regulate ICP1 gene expression, balancing inhibition and virion hijacking.

bioRxiv · Nov 28, 2020Microbiology

Structural basis for tuning activity and membrane specificity of bacterial cytolysins

N. R. Shah, T. B. Voisin, E. S. Parsons, C. M. Boyd, B. Hoogenboom, D. Bubeck

This study investigates how bacterial cytolysins use cholesterol to selectively lyse cells by analyzing structural changes in intermedilysin bound to CD59.

bioRxiv · Jun 16, 2020Biochemistry

CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers

A. Menny, M. Serna, C. M. Boyd, S. Gardner, A. P. Joseph, B. P. Morgan, M. Topf, N. J. Brooks, D. Bubeck

This study uses cryo-EM to show how the complement membrane attack complex interacts with lipid bilayers through distinct mechanisms involving C6/C7 and C8/C9, revealing structural insights into pore formation and membrane disruption.

bioRxiv · Aug 17, 2018Biophysics