Author

Maximilian Schmitz

University of BonnORCID 0009-0002-6078-6503Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:benchmarking· 1 Research Focus:cancer & tumor microenvironment· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

Matthias GeyeriD· 3 shared Sophie C. BinderiD· 2 shared Christina Schülein-Völk· 1 shared Christophe RouilloniD· 1 shared Claire E. EyersiD· 1 shared Daniel Fleischhauer· 1 shared Daniel SolvieiD· 1 shared Dimitrios PapadopoulosiD· 1 shared

Activity by Year

2024-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersBiochemistry

Matthias GeyerORCID

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3 papers

Recent·Most cited

Cancer BiologybioRxivPreprintJan 15, 2025

The MYCN/Aurora-A complex is a cyclin activating kinase for CDK12

Mareike Müller, Lorenz Eing, Leonie Uhl…·Gabriele Büchel

This study identifies Aurora-A as a CDK12-activating kinase in neuroblastoma, showing its role in transcription termination and tumor growth suppression.

3 citations

humanproteomics

𝕏 PostBluesky

BiochemistryNucleic Acids ResearchPeer-reviewedJul 24, 2024

The SAVED domain of the type III CRISPR protease CalpL is a ring nuclease

Sophie C. Binder, Niels Schneberger, Maximilian Schmitz…·Gregor Hagelueken

This study identifies the SAVED domain of CalpL as a ring nuclease that cleaves cA4, revealing its role in regulating the CRISPR defense system.

10 citations

proteomicsexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivPreprintFeb 14, 2024

Structural basis of Cdk7 activation by dual T-loop phosphorylation

Robert Düster, K. Anand, Sophie C. Binder…·Matthias Geyer

This study reports the crystal structure of fully activated Cdk7/Cyclin H/Mat1 complex with dual T-loop phosphorylations, revealing their distinct roles in kinase activity and substrate recognition.

5 citations

humanstructural biology

𝕏 PostBluesky