Author

Henning D. Mootz

University of MünsterORCID 0000-0002-3385-0234Unclaimed 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 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Organism:human· 1 Assay:protein sequence· 1

Frequent Co-Authors

Wolfgang DörneriD· 3 shared Daniel KümmeliD· 2 shared Alexander SchröderiD· 1 shared Amanda K. ChapliniD· 1 shared Benedikt Hermanns· 1 shared Benjamin M. FosteriD· 1 shared Christine K. SchmidtiD· 1 shared Christoph HumbergiD· 1 shared

Activity by Year

2025-2025 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiochemistry

Wolfgang DörnerORCID

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3 papers

Recent·Most cited

BiochemistryAngewandte Chemie International EditionPeer-reviewedJul 8, 2025

Structural Basis for a Scaffolding Role of the COM Domain in Nonribosomal Peptide Synthetases

Julia Diecker, Benedikt Hermanns, Jennifer Rüschenbaum…·Henning D. Mootz

The paper presents the first crystal structure of a cis-COM domain in NRPSs and shows its role in scaffolding domain architecture for efficient peptide synthesis.

4 citations

experimental assayprotein folding & dynamics

𝕏 PostBluesky

Molecular BiologybioRxivPreprintJun 16, 2025

UFMylation orchestrates chromatin engagement of core NHEJ components to promote DNA double-strand break repair

Zijuan Wang, Benjamin M. Foster, Isabelle Cristine da Costa…·Christine K. Schmidt

The paper identifies UFM1 as a regulator of NHEJ by orchestrating chromatin engagement of core components, linking UFMylation defects to DSB repair defects.

DOI 10.1101/2025.06.16.659844

humanexperimental assay

𝕏 PostBluesky

BiochemistryNature CommunicationsPeer-reviewedMar 19, 2025

A Cysteine-Less and Ultra-Fast Split Intein Rationally Engineered from Being Aggregation-Prone to Highly Efficient in Protein trans-Splicing

Christoph Humberg, Zahide Yilmaz, Katharina Fitzian…·Henning D. Mootz

The paper identifies aggregation as the cause of low splicing efficiency in a cysteine-less split intein and presents a rationally engineered variant with high activity.

9 citations

protein sequencebiophysical modeling

𝕏 PostBluesky