Author

J. Shaul

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

Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:drug response / drug discovery· 1 Organism:E. coli· 1 Organism:human· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Frommlet· 3 shared A. O. Frank· 3 shared E. Ornelas· 3 shared A. Bermingham· 2 shared A. Lingel· 2 shared A. Ruzin· 2 shared B. Benton· 2 shared C. J. Balibar· 2 shared

Activity by Year

2019-2019 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 45 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

3 shared papersBiochemistry

A. Frommlet

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Two distinct mechanisms of small molecule inhibition of LpxA acyltransferase essential for lipopolysaccharide biosynthesis

W. Han, X. Ma, C. J. Balibar, C. M. Baxter Rath, B. Benton, A. Bermingham, F. Casey, B. Chie-Leon, M.-K. Cho, A. O. Frank, A. Frommlet, C.-M. Ho, P. S. Lee, M. Li, A. Lingel, , T. Uehara

The paper identifies two distinct mechanisms by which small molecules inhibit LpxA acyltransferase, a key enzyme in lipopolysaccharide biosynthesis.

bioRxiv · Dec 17, 2019 · PreprintBiochemistry

Two distinct mechanisms of small molecule inhibition of LpxA acyltransferase essential for lipopolysaccharide biosynthesis

W. Han, X. Ma, C. J. Balibar, C. M. Baxter Rath, B. Benton, A. Bermingham, F. Casey, B. Chi-Leon, M.-K. Cho, A. O. Frank, A. Frommlet, C.-M. Ho, P. S. Lee, M. Li, A. Lingel, , T. Uehara

This study identifies two small-molecule inhibitors of LpxA, revealing distinct inhibition mechanisms and highlighting compound 2's improved properties for antibacterial development.

bioRxiv · Dec 14, 2019 · PreprintBiochemistry

A VP2/3-derived peptide exhibits potent antiviral activity against BK and JC polyomaviruses by targeting a novel VP1 binding site

J. R. Kane, S. Fong, J. Shaul, A. Frommlet, A. O. Frank, M. Knapp, D. E. Bussiere, P. Kim, E. Ornelas, C. Cuellar, J. R. Abend, C. A. Wartchow

The paper identifies a VP2/3-derived peptide that inhibits BK and JC polyomaviruses by binding to a novel VP1 pore site, showing potent antiviral activity with low nanomolar affinity.

bioRxiv · Aug 8, 2019 · PreprintMicrobiology