Author

M. Gengenbacher

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:drug response / drug discovery· 2 Organism:bacteria (other)· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Organism:mouse· 1 Assay:whole-genome sequencing· 1

Frequent Co-Authors

T. Dick· 3 shared V. A. Dartois· 3 shared M. Zimmerman· 2 shared A. E. Marrouni· 1 shared A. Madani· 1 shared B. Bosch· 1 shared C. A. Engelhart· 1 shared C. Boyce· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersMicrobiology

T. Dick

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Mycobacterium tuberculosis DprE1 inhibitor OPC-167832 is active against Mycobacterium abscessus in vitro

J. P. Sarathy, M. Zimmerman, M. Gengenbacher, V. A. Dartois, T. Dick

OPC-167832, a DprE1 inhibitor active against Mycobacterium tuberculosis, shows in vitro activity against Mycobacterium abscessus but lacks efficacy in a mouse model due to moderate potency.

bioRxiv · Sep 14, 2022Microbiology

Activity of Tricyclic Pyrrolopyrimidine Gyrase B Inhibitor against Mycobacterium abscessus

A. Madani, D. A. Negatu, A. E. Marrouni, R. Miller, C. Boyce, N. Murgolo, C. J. Bungard, M. Zimmerman, V. A. Dartois, M. Gengenbacher, D. B. Olsen, T. Dick

This study evaluates the activity of TPP8, a tricyclic pyrrolopyrimidine gyrase B inhibitor, against Mycobacterium abscessus in vitro, ex vivo, and in vivo.

bioRxiv · May 16, 2022Microbiology

A chemical-genetic map of the pathways controlling drug potency in Mycobacterium tuberculosis

S. Li, N. C. Poulton, J. S. Chang, Z. A. Azadian, M. A. Dejusus, N. Ruecker, M. D. Zimmerman, K. Eckartt, B. Bosch, C. A. Engelhart, D. Sullivan, M. Gengenbacher, V. A. Dartois, D. Schnappinger, J. M. Rock

This study uses a CRISPR interference platform to map drug resistance pathways in Mtb, identifying new intrinsic and acquired resistance mechanisms and potential drug targets.

bioRxiv · Nov 27, 2021 · PreprintMicrobiology

Pyrazinamide triggers degradation of its target aspartate decarboxylase

P. Gopal, J. Sarathy, M. Yee, P. Ragunathan, J. Shin, S. Bhushan, J. Zhu, T. Akopian, O. Kandror, T. K. Lim, M. Gengenbacher, Q. Lin, E. J. Rubin, G. Grueber, T. Dick

This paper shows that pyrazinamide's active form, POA, triggers degradation of its target enzyme PanD via the ClpC1-ClpP protease, rather than inhibiting it directly.

Nature Communications · Apr 3, 2020Peer-reviewedMicrobiology