Author

Matthias Elgeti

Leipzig UniversityORCID 0000-0002-0550-4852Unclaimed 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:drug response / drug discovery· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Assay:DNA methylation· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

Dean P. Staus· 2 shared Julia BelyaevaiD· 2 shared Mahdi Bagherpoor HelabadiD· 2 shared Alem W. KahsaiiD· 1 shared Ali MasoudiiD· 1 shared Angus Li· 1 shared Arun Jyothidasan· 1 shared Carl‐Mikael SuomivuoriiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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2 shared papersBiochemistry

Dean P. Staus

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3 papers

Recent·Most cited

Exploring the bistable equilibrium of methylated CpG DNA recognition by the MBD2 protein

Senta Volkenandt, Julia Belyaeva, Torry Li, Matthias Elgeti, Ralf Metzler, Petra Imhof, David C Williams, Mahdi Bagherpoor Helabad

The paper uses molecular dynamics simulations and experimental assays to show MBD2 binds methylated CpG DNA with a bistable equilibrium, involving two stable conformations with different affinities.

Nucleic Acids Research · Oct 13, 2026Peer-reviewedMolecular Biology

Conformational Basis of Functionally Selective Allosteric Modulation of the Angiotensin II type 1 Receptor by Small Molecules

Samuel Liu, Peng Xiao, Matthias Elgeti, Eve J. Fine, E Lucero, Mikkel Vestergaard, Junyan Wang, Arun Jyothidasan, Angus Li, Changxiu Qu, Eva Olsen, Georgios Mazis, Josephine K. Madsen, Carl‐Mikael Suomivuori, Ji Hee Kim, , Robert J. Lefkowitz

The paper identifies and characterizes small molecule allosteric modulators of the AT1R, revealing their conformational mechanisms and effects on G protein and β-arrestin pathways.

bioRxiv · Jul 16, 2026 · PreprintBiochemistry

Angiotensin receptor conformations stabilized by biased ligands differentially modulate β-arrestin interactions

Matthias Elgeti, Julia Belyaeva, Mahdi Bagherpoor Helabad, Dean P. Staus, Laura M. Wingler

The paper shows that biased ligands of the AT1R receptor stabilize different conformations that differentially modulate β-arrestin interactions, affecting signaling and desensitization.

Journal of Biological Chemistry · Dec 29, 2025Peer-reviewedBiochemistry