Author

C. W. Kenner

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

K. V. Korotkov· 4 shared J. S. Rush· 3 shared N. Korotkova· 3 shared S. Zamakhaeva· 3 shared C. T. Chaton· 2 shared G. Widmalm· 2 shared J. Li· 2 shared M. M. Rahman· 2 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 42 mutual co-author links

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4 shared papersMicrobiology

K. V. Korotkov

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Author profile →

4 papers

Recent·Most cited

Structure and mechanism of biosynthesis of Streptococcus mutans cell wall polysaccharide

J. S. Rush, S. Zamakhaeva, N. R. Murner, P. Deng, A. J. Morris, C. W. Kenner, I. Black, C. Heiss, P. Azadi, K. V. Korotkov, G. Widmalm, N. Korotkova

This study identifies the structure and biosynthesis mechanism of Streptococcus mutans cell wall polysaccharide, revealing key modifications and their roles in bacterial morphology and biofilm formation.

bioRxiv · May 9, 2024 · PreprintMicrobiology

Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci

M. M. Rahman, S. Zamakhaeva, J. S. Rush, C. T. Chaton, C. W. Kenner, Y. M. Hla, H.-C. T. Tsui, V. N. Uversky, M. E. Winkler, K. V. Korotkov, N. Korotkova

The paper identifies glycosylation of serine/threonine-rich IDRs in streptococcal membrane proteins and shows its role in biofilm formation.

bioRxiv · May 5, 2024Microbiology

PplD is a de-N-acetylase of the cell wall linkage unit of streptococcal rhamnopolysaccharides

J. S. Rush, P. Parajuli, A. Ruda, J. Li, A. A. Pohane, S. Zamakhaeva, M. M. Rahman, J. C. Chang, A. Gogos, C. W. Kenner, G. Lambeau, M. J. Federle, K. V. Korotkov, G. Widmalm, N. Korotkova

This study identifies PplD as a de-N-acetylase that modifies the cell wall linkage unit of streptococcal rhamnopolysaccharides, enhancing resistance to host antimicrobial proteins.

bioRxiv · Sep 23, 2021Microbiology

Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site

C. T. Chaton, E. S. Rodriguez, R. W. Reed, J. Li, C. W. Kenner, K. V. Korotkov

The paper determines the crystal structures of three homoserine transacetylases and identifies MtMetX as highly druggable.

bioRxiv · Dec 10, 2019Biochemistry