Author

D. L. Popham

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 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Research Focus:development & morphogenesis· 1 Organism:E. coli· 1

Frequent Co-Authors

G. M. Kaus· 2 shared A. Yahashiri· 1 shared C. D. Ellermeier· 1 shared D. S. Weiss· 1 shared f. Cava· 1 shared J. C. D. Houtman· 1 shared K. S. Ramamurthi· 1 shared L. Aravind· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersMicrobiology

G. M. Kaus

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Author profile →

3 papers

Recent·Most cited

Bacterial cell surface nanoenvironment requires a specialized chaperone to activate a peptidoglycan biosynthetic enzyme

T. Delerue, S. Chareyre, V. Anantharaman, M. C. Gilmore, D. L. Popham, f. Cava, L. Aravind, K. S. Ramamurthi

This study identifies SpoVK as a chaperone that activates MurG during spore surface assembly in Bacillus subtilis, highlighting the need for specialized chaperones in specific nanoenvironments.

bioRxiv · Oct 6, 2023Microbiology

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

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