Author

Siska Führer

TU Dortmund UniversityORCID 0009-0000-4334-221XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Organism:human· 3 Assay:proteomics· 3 Research Focus:drug response / drug discovery· 2 Approach:experimental assay· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1

Frequent Co-Authors

Malte GerschiD· 3 shared Alexandra Brause· 1 shared Annette PascheniD· 1 shared Barbara M. GrüneriD· 1 shared Belén LucasiD· 1 shared Bikash AdhikariiD· 1 shared Brenda Arlene SchulmaniD· 1 shared Ciriana OrabonaiD· 1 shared

Activity by Year

2024-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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3 shared papersBiochemistry

Malte GerschORCID

Mutual co-authors in cluster

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3 papers

Recent·Most cited

BiochemistryNature CommunicationsPeer-reviewedMay 13, 2026

Targeted degradation of USP7 in solid cancer cells reveals disparate effects of deubiquitinase inhibition vs. acute protein depletion

Nikolas Klink, Sebastian Urban, Johanna A. Seier…·Malte Gersch

This paper compares the effects of USP7 inhibition and degradation in cancer cells, finding distinct phenotypic and proteomic responses.

1 citation

humanproteomics

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Cell BiologyNature ChemistryPeer-reviewedJan 7, 2026

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

Elisabeth Hennes, Belén Lucas, Natalie S. Scholes…·Herbert Waldmann

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

18 citationstop 1%

humanproteomics

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BiochemistryNature Chemical BiologyPeer-reviewedNov 25, 2024

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

Kim Wendrich, Kai Gallant, Sarah Recknagel…·Malte 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.

28 citations

humanproteomics

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