Author

A. Frommlet

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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Biochemistry· 2 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Research Focus:drug response / drug discovery· 1 Organism:E. coli· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

A. O. Frank· 4 shared E. Ornelas· 3 shared J. Shaul· 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 4/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBiochemistry

A. O. Frank

Mutual co-authors in cluster

Author profile →

4 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

The Structural Basis of Indisulam-Mediated Recruitment of RBM39 to the DCAF15-DDB1-DDA1 E3 Ligase Complex

D. E. Bussiere, L. Xie, W. Shu, H. Srinivas, W. Shu, A. Burke, C. Be, J. Zhao, A. Godbole, D. King, R. G. Karki, V. Hornak, F. Xu, J. Cobb, N. Carte, , J. Paulk

This study determines the structure of the DCAF15-DDB1-DDA1-Indisulam-RBM39 complex, revealing how Indisulam promotes RBM39 degradation via a novel degron motif.

bioRxiv · Aug 16, 2019Biophysics

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