Author

M. Gersch

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 2 Cell Biology· 2 Cancer Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:proteomics· 5 Approach:experimental assay· 4 Organism:human· 4 Research Focus:drug response / drug discovery· 3 Research Focus:cancer & tumor microenvironment· 2 Research Focus:cell signaling & trafficking· 2 Research Focus:chromatin & epigenetic regulation· 2 Approach:biophysical modeling· 1

Frequent Co-Authors

A. Pinto-Fernandez· 2 shared B. M. Kessler· 2 shared D. Komander· 2 shared H. C. Scott· 2 shared M. J. Clague· 2 shared S. Ioannidis· 2 shared S. Urbe· 2 shared A. Behrens· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersCancer Biology

A. Pinto-Fernandez

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Monovalent Pseudo-Natural Product Degraders Supercharge the Native Degradation of IDO1 by KLHDC3

E. Hennes, B. Lucas, N. S. Scholes, X.-f. Cheng, D. C. Scott, M. Bischoff, K. Reich, R. Gasper, M. Lucas, T. T. Xu, L.-M. Pulvermacher, L. Doetsch, H. Imrichova, A. Brause, K. R. Naredla, , H. Waldmann

The paper identifies iDegs, which enhance IDO1 degradation via the native CRL2KLHDC3 pathway, reducing kynurenine formation and offering new therapeutic potential for cancer.

bioRxiv · Jul 10, 2024Cell Biology

Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53

K. Wendrich, K. Gallant, S. Recknagel, S. Petroulia, S. Führer, K. Bezstarosti, R. O'Dea, J. Demmers, M. Gersch

This study identifies USP53 and USP54 as active deubiquitinases specific for K63-linked polyubiquitin, revealing their role in regulating tricellular junctions and correcting previous annotations of them as pseudo-enzymes.

bioRxiv · Jul 7, 2024Biochemistry

Surprising variety in the USP deubiquitinase catalytic mechanism

N. Keijzer, A. Priyanka, Y. Stijf-Bultsma, A. Fish, M. Gersch, T. K. Sixma

This paper reveals that USP deubiquitinases use different catalytic mechanisms, with some relying on a conserved aspartate instead of a canonical third residue for catalysis.

bioRxiv · Jul 24, 2023Biochemistry

USP28 deletion and small molecule inhibition destabilises c-Myc and elicits regression of squamous cell lung carcinoma

E. J. Ruiz, A. Pinto-Fernandez, A. P. Turnbull, L. Lan, T. M. Charlton, H. C. Scott, A. Damianou, G. Vere, E. M. Riising, C. Da Costa, W. W. Krajewski, D. Guerin, J. Kearns, S. Ioannidis, M. Katz, , A. Behrens

This study shows that deleting or inhibiting USP28 reduces c-Myc levels and causes regression of lung squamous cell carcinoma in mice and human xenografts.

bioRxiv · Nov 17, 2020Cancer Biology

A novel USP30 inhibitor recapitulates genetic loss of USP30 and sets the trigger for PINK1-PARKIN amplification of mitochondrial ubiquitylation.

E. Rusilowicz-Jones, J. Jardine, A. Kallinos, A. Pinto-Fernandez, F. Guenther, M. Giurrandino, F. G. Barone, K. McCarron, C. J. Burke, A. Murad, A. Martinez, E. Marcassa, M. Gersch, A. Buckmelter, K. Kayser-Bricker, , M. J. Clague

The paper identifies a USP30 inhibitor that mimics genetic loss of USP30, revealing its role in regulating mitochondrial ubiquitylation and mitophagy through TOM complex components.

bioRxiv · Apr 16, 2020Cell Biology