Author

M. Bantscheff

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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Bioengineering· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:proteomics· 3 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:development & morphogenesis· 1 Research Focus:differential expression· 1

Frequent Co-Authors

W. Huber· 2 shared A. C. Balestra· 1 shared A. H. Smits· 1 shared A. Hainard· 1 shared A. J. Perrin· 1 shared A. P. Snijders· 1 shared A. Rutkowska· 1 shared A.-M. Michon· 1 shared

Activity by Year

2018-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBioengineering

W. Huber

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

A multipass membrane protein interacts with the cGMP-dependent protein kinase to regulate critical calcium signals in malaria parasites

A. C. Balestra, K. Koussis, N. Klages, S. A. Howell, H. R. Flynn, M. Bantscheff, C. Pasquarello, A. J. Perrin, L. Brusini, P. Arboit, O. Sanz, L. Peces-Barba Castano, C. Withers-Martinez, A. Hainard, S. Ghidelli-Disse, , M. Brochet

This study identifies ICM1, a multipass membrane protein interacting with PKG in malaria parasites, and shows it regulates calcium signals critical for gametogenesis and parasite survival.

bioRxiv · Jul 18, 2020Microbiology

Biological Plasticity Rescues Target Activity in CRISPR Knockouts

A. H. Smits, F. Ziebell, G. Joberty, N. Zinn, W. F. Mueller, S. Clauder-Münster, D. Eberhard, M. Fälth Savitski, P. Grandi, P. Jakob, A.-M. Michon, H. Sun, K. Tessmer, T. Bürckstümmer, M. Bantscheff, , W. Huber

The paper quantifies residual protein expression in CRISPR-Cas9 knockouts using RNA-seq and SPS-MS3, identifying mechanisms of partial protein preservation and functional retention.

bioRxiv · Jul 26, 2019Bioengineering

Proteome thermal stability reflects organ physiology and identifies drug-target engagement in vivo

J. Perrin, T. Werner, N. Kurzawa, D. D. Childs, M. Kalxdorf, A. Rutkowska, D. Poeckel, D. C. Sevin, E. Stonehouse, K. Strohmer, B. Heller, D. Thomson, J. Vappiani, J. Krause, H. C. Eberl, , G. Bergamini

This study introduces tissue-TPP and blood-CETSA to measure proteome thermal stability, revealing organ physiology and drug-target engagement in vivo.

bioRxiv · Dec 20, 2018 · PreprintCell Biology