Author

Samuel A. Maiwald

Max Planck Institute of BiochemistryORCID 0000-0002-7235-2748Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

Brenda Arlene SchulmaniD· 2 shared Jiale DuiD· 2 shared Susanne von Gronau· 2 shared Alexander HerrmanniD· 1 shared Alina S. ThieleniD· 1 shared Andreas OderiD· 1 shared Andrei N. LupasiD· 1 shared Birte Hernandez AlvareziD· 1 shared

Activity by Year

2026-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersBiochemistry

Brenda Arlene SchulmanORCID

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3 papers

Recent·Most cited

BiochemistrybioRxivPreprintOct 11, 2026

Cereblon on Steroids: Beyond the Canonical Ligand Space

Alexander Herrmann, Christopher Heim, Samuel A. Maiwald…·Marcus D. Hartmann

This paper expands the known ligand space of Cereblon by identifying new chemically distinct ligands that bind through non-canonical mechanisms.

DOI 10.64898/2026.08.28.747849

humanexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivPreprintSep 16, 2026

Multimodal substrate recruitment enables CTLH-MKLN1 E3 ligase to target N-, C-, and internal degrons

Sara Sepic, Karthik V Gottemukkala, Jiale Du…·Brenda Arlene Schulman

This study reveals how MKLN1's discoidin and Kelch domains recognize diverse degrons through multivalent interactions, enabling substrate recruitment by the CTLH-MKLN1 E3 ligase.

DOI 10.64898/2026.09.10.750665

experimental assay

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BiochemistryNature CommunicationsPeer-reviewedMay 7, 2026

Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1

Gisele A. Andree, Luca J. Stier, Kerstin Schmiederer…·Brenda Arlene Schulman

The paper identifies LRRC58 as a cysteine-responsive E3 ligase that regulates CDO1 stability via ubiquitylation, revealing a mechanism linking cysteine availability to proteasomal turnover.

1 citation

humanproteomics

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