Author

G. M. Kaus

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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Organism:C. elegans· 2 Research Focus:cell signaling & trafficking· 2 Organism:E. coli· 2 Research Focus:cell type annotation· 1 Approach:experimental assay· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

A. Yahashiri· 2 shared D. L. Popham· 2 shared D. S. Weiss· 2 shared C. D. Ellermeier· 1 shared J. C. D. Houtman· 1 shared J. W. McCausland· 1 shared J. Xiao· 1 shared L. F. Snyder· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersMicrobiology

A. Yahashiri

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Author profile →

3 papers

Recent·Most cited

Comparative study of bacterial SPOR domains identifies functionally important differences in glycan binding affinity

A. Yahashiri, G. M. Kaus, D. L. Popham, J. C. D. Houtman, D. S. Weiss

This study compares the glycan binding affinity of bacterial SPOR domains using ITC and shows that affinity differences impact function for some domains but not others.

bioRxiv · Jul 1, 2022Microbiology

FtsN activates septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthase in E. coli

Z. Lyu, A. Yahashiri, X. Yang, J. W. McCausland, G. M. Kaus, R. McQuillen, D. S. Weiss, J. Xiao

This study shows FtsN activates septal peptidoglycan synthesis by forming a processive complex with FtsWI on the sPG-track, rather than displacing FtsWI from the Z-track.

bioRxiv · Aug 23, 2021Microbiology

Lysozyme resistance in C. difficile is dependent on two peptidoglycan deacetylases

G. M. Kaus, L. F. Snyder, U. Muh, M. J. Flores, D. L. Popham, C. D. Ellermeier

This paper identifies two peptidoglycan deacetylases, PgdA and PdaV, as essential for lysozyme resistance in C. difficile, showing they are partially redundant and critical for this resistance mechanism.

bioRxiv · Jul 17, 2020Microbiology