Author

Robin Alexander Rothemann

University of CologneORCID 0000-0002-9502-5360Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

Jan RiemeriD· 3 shared Christine ZargesiD· 2 shared Simon PoepseliD· 2 shared Aleksandra TrifunovićiD· 1 shared Alexander von der MalsburgiD· 1 shared Carmelina Petrungaro· 1 shared Dan EhningeriD· 1 shared Daniele BanoiD· 1 shared

Activity by Year

2025-2025 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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3 shared papersBiochemistry

Jan RiemerORCID

Mutual co-authors in cluster

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3 papers

Recent·Most cited

Topology control by a conserved cysteine pair in the OMM-protein CCDC127 enables MICOS interaction

Christine Zarges, Pauline Schepsky, Robin Alexander Rothemann, Tobias Bock-Bierbaum, Alexander von der Malsburg, Linda C. Baumann, Aleksandra Trifunović, Oliver Daumke, Martin van der Laan, Karina von der Malsburg, Jan Riemer

The paper identifies CCDC127 as a mitochondrial disulfide relay substrate that interacts with MICOS components, revealing its role in OMM topology and mitochondrial membrane organization.

bioRxiv · Dec 15, 2025 · PreprintBiochemistry

The mitochondrial disulphide relay substrate FAM136A safeguards IMS proteostasis and cellular fitness

Christine Zarges, Hanna Fieler, Robin Alexander Rothemann, Simon Poepsel, Lucas T. Jae, Jan Riemer

This study identifies FAM136A as a mitochondrial disulphide relay substrate essential for IMS proteostasis, showing its role in cellular fitness and stress response.

Redox Biology · Oct 9, 2025Peer-reviewedBiochemistry

Interaction with AK2A links AIFM1 to cellular energy metabolism

Robin Alexander Rothemann, Egor A. Pavlenko, Mrityunjoy Mondal, Sarah Gerlich, Pavel Grobushkin, Sebastian Mostert, Julia Racho, Konstantin Weiss, Dylan Stobbe, Katharina Stillger, Kim Jasmin Lapacz, Silja Lucia Salscheider, Carmelina Petrungaro, Dan Ehninger, Thi Hoang Duong Nguyen, , Jan Riemer

The paper identifies AIFM1's interaction with AK2A and shows how this stabilizes AK2A and enhances NADH oxidoreductase activity, highlighting AIFM1's role in energy metabolism.

Molecular Cell · Jun 26, 2025Peer-reviewedBiochemistry