Author

J. C. Whitney

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Microbiology· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:bacteria (other)· 4 Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell type annotation· 1 Assay:protein structure· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

N. P. Bullen· 2 shared A. G. McArthur· 1 shared A. Ostaszewski· 1 shared B. A. Duerkop· 1 shared C. N. Johnson· 1 shared D. Quentin· 1 shared D. W. Grebenc· 1 shared E. Razvi· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersMicrobiology

N. P. Bullen

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

An enterococcal phage protein broadly inhibits type IV restriction enzymes involved in antiphage defense

N. P. Bullen, C. N. Johnson, S. E. Andersen, G. Arya, S. R. Marotta, Y.-J. Lee, P. Weigele, J. C. Whitney, B. A. Duerkop

The paper identifies a phage protein that inhibits type IV restriction enzymes in drug-resistant enterococci, revealing how phages evolve to overcome bacterial defense mechanisms.

bioRxiv · Nov 16, 2023Microbiology

Structure of a tripartite protein complex that targets toxins to the type VII secretion system

T. A. Klein, P. Y. Shah, P. Gkragkopoulou, D. W. Grebenc, Y. Kim, J. C. Whitney

The paper presents the structure of a tripartite protein complex involving LXG domains and Lap proteins, revealing a conserved mechanism for toxin export via the type VII secretion system.

bioRxiv · Jul 21, 2023Microbiology

Structural basis for effector transmembrane domain recognition by type VI secretion system chaperones

S. Ahmad, K. K. Tsang, K. Sachar, D. Quentin, T. M. Tashin, N. P. Bullen, S. Raunser, A. G. McArthur, G. Prehna, J. C. Whitney

The paper identifies a conserved motif in TMD-containing effectors and reveals how Eag chaperones stabilize these domains for T6SS-mediated secretion.

bioRxiv · Oct 28, 2020Biochemistry

PelX is a UDP-N-acetylglucosamine C4-epimerase involved in Pel polysaccharide-dependent biofilm formation

L. S. Marmont, G. B. Whitfield, R. Pfoh, R. J. Williams, T. E. Randall, A. Ostaszewski, E. Razvi, R. A. Groves, H. Robinson, M. Nitz, M. R. Parsek, I. A. Lewis, J. C. Whitney, J. J. Harrison, P. L. Howell

The paper identifies PelX as a UDP-GlcNAc C4-epimerase essential for Pel polysaccharide synthesis and biofilm formation in Pseudomonas protegens.

Journal of Biological Chemistry · Aug 1, 2020Peer-reviewedMicrobiology