Author

D. Dormann

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

Biology Disciplines

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Biochemistry· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

S. Hutten· 2 shared A. Niedner-Boblenz· 1 shared A. P. Gerber· 1 shared C. Abou-Ajram· 1 shared C. Heine· 1 shared D. Edbauer· 1 shared D. Niessing· 1 shared E. Davydova· 1 shared

Activity by Year

2018-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

S. Hutten

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation

A. Niedner-Boblenz, T. Monecke, J. Hennig, M. Klostermann, M. Hofweber, E. Davydova, A. P. Gerber, I. Anosova, W. Mayer, M. Mueller, R. Heym, R. Janowski, J.-C. Paillart, D. Dormann, K. Zarnack, , D. Niessing

This study identifies PUN motifs in yeast Loc1p that cooperate to catalyze RNA folding and drive phase separation, suggesting a role in RNA and DNA-related processes across species.

bioRxiv · Mar 27, 2024Biochemistry

Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregation

L. A. Gruijs da Silva, F. Simonetti, S. Hutten, H. Riemenschneider, E. L. Sternburg, L. M. Pietrek, J. Gebel, V. Doetsch, D. Edbauer, G. Hummer, L. S. Stelzl, D. Dormann

This study shows that hyperphosphorylation of TDP-43 reduces its phase separation and aggregation, suggesting it may act as a protective mechanism against neurodegeneration.

bioRxiv · Apr 30, 2021Biochemistry

Interaction modulation through arrays of clustered methyl-arginine protein modifications

J. Woodsmith, V. Casado-Medrano, N. Benlasfer, R. Eccles, S. Hutten, C. Heine, V. Thormann, C. Abou-Ajram, O. Rocks, D. Dormann, U. Stelzl

The paper analyzes human arginine methylation events, showing they can function either isolated or clustered, with clustered methylation in SYNCRIP influencing protein interactions through distinct regulatory mechanisms.

bioRxiv · Sep 5, 2018Cell Biology