Author

M. Kutsch

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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Immunology· 2 Biochemistry· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 3 Organism:human· 3 Research Focus:cell type annotation· 2 Approach:genetic perturbation / CRISPR· 2 Organism:mouse· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2

Frequent Co-Authors

J. Coers· 3 shared C. Herrmann· 2 shared G. Wallace· 2 shared A. Haldar· 1 shared A. Piro· 1 shared A. S. Piro· 1 shared c. lesser· 1 shared D. Hernandez· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersImmunology

J. Coers

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Elucidating the activation mechanism for GBP1 oligomerization

O. Daumke, M. Weismehl, X. Chu, M. Kutsch, P. Lauterjung, C. Herrmann, M. Kudryashev

This study reveals the activation mechanism of GBP1 oligomerization through cryo-EM structures, showing nucleotide-dependent conformational changes drive dimerization, oligomerization, and membrane binding for pathogen encapsulation.

bioRxiv · Aug 1, 2023 · PreprintBiochemistry

GBP2 aggregates LPS and activates the caspase-4 inflammasome independent of the bacterial encapsulation factor GBP1

M. S. Dickinson, M. Kutsch, L. Sistemich, D. Hernandez, D. Needham, c. lesser, C. Herrmann, J. Coers

This paper shows GBP2 can trigger pyroptosis by aggregating free LPS and activating caspase-4, independent of GBP1's bacterial binding function.

Proceedings of the National Academy of Sciences · Apr 6, 2023Peer-reviewedImmunology

Dynamin-related Irgm proteins modulate LPS-induced caspase-4 activation and septic shock

R. Finethy, J. Dockterman, M. Kutsch, N. Orench-Rivera, G. Wallace, A. Piro, S. Luoma, A. Haldar, S. Hwang, J. Martinez, M. Kuehn, G. Taylor, J. Coers

This study identifies Irgm proteins as negative regulators of caspase-4 activation in response to LPS, showing their role in preventing septic shock.

bioRxiv · Mar 18, 2020Immunology

A rapidly evolving polybasic motif modulates bacterial detection by guanylate binding proteins

K. M. Kohler, M. Kutsch, A. S. Piro, G. Wallace, J. Coers, M. F. Barber

The paper shows that a rapidly evolving polybasic motif in primate GBP proteins modulates bacterial detection, specifically targeting Shigella flexneri through evolutionary changes.

bioRxiv · Jul 2, 2019Microbiology