Author

Alexander C. Anderson

University of GuelphORCID 0000-0002-1870-2903Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 2 Approach:experimental assay· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Assay:metagenomics· 1

Frequent Co-Authors

Anthony J. ClarkeiD· 2 shared David SychanthaiD· 2 shared Adrian J. VersteriD· 1 shared Amirahmad AzhiehiD· 1 shared Ashley S. BrottiD· 1 shared Bailey J. SchultziD· 1 shared Benjamin D. RossiD· 1 shared Benjamin G EmmanueliD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiochemistry

Anthony J. ClarkeORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Denuded peptidoglycan oligosaccharides enable the biochemical investigation of bacterial cell wall recognition, modification, and degradation

Benjamin G Emmanuel, Grace DelMistro, Alexander C. Anderson, Chris Vandenende, Anthony J. Clarke, David Sychantha

This paper describes an enzymatic method to generate defined peptidoglycan oligosaccharides for studying bacterial cell wall recognition and enzyme activity.

Journal of Biological Chemistry · Aug 17, 2026Peer-reviewedBiochemistry

Rapidly evolving orphan immunity genes protect human gut bacteria from intoxication by the type VI secretion system

Amirahmad Azhieh, Paul Hernandez, Alexander C. Anderson, David Sychantha, Adrian J. Verster, John C. C. Whitney, Benjamin D. Ross

The paper identifies rapidly evolving orphan immunity genes in human gut bacteria that protect against T6SS intoxication through high-affinity protein interactions and shows their evolutionary dynamics across microbiomes.

bioRxiv · May 3, 2025 · PreprintMicrobiology

The mechanism of peptidoglycan O-acetylation in Gram-negative bacteria typifies bacterial MBOAT-SGNH acyltransferases

Alexander C. Anderson, Bailey J. Schultz, Eric D. Snow, Ashley S. Brott, Stefen Stangherlin, Tyler Malloch, J. R. London, Suzanne Walker, Anthony J. Clarke

This study elucidates the mechanism of MBOAT-SGNH acyltransferases in Gram-negative bacteria, showing that a tyrosine-containing peptide shuttles acyl groups from MBOAT to SGNH active sites for peptidoglycan O-acetylation.

Journal of Biological Chemistry · Apr 23, 2025Peer-reviewedBiochemistry