Author

M. Etzkorn

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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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:biophysical modeling· 2 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. K. Buell· 1 shared A. Viegas· 1 shared B. Frieg· 1 shared B. Strodel· 1 shared B. Uluca· 1 shared C. Chu· 1 shared C. Poojari· 1 shared C. Vargas· 1 shared

Activity by Year

2017-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperBiophysics

A. K. Buell

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3 papers

Recent·Most cited

Capturing G protein-coupled receptors into native lipid-bilayer nanodiscs using new diisobutylene/maleic acid (DIBMA) copolymers

C. Chu, C. Vargas, M. C. Barbosa, S. Sommerhage, G. F. Schroeder, S. Keller, M. Etzkorn

This paper introduces new DIBMA-based copolymers for extracting GPCRs into native lipid-bilayer nanodiscs, showing improved performance over existing polymers like SMA.

bioRxiv · Jan 20, 2024Biochemistry

Biophysical and pharmacokinetic characterization of a small-molecule inhibitor of RUNX1/ETO tetramerization with anti-leukemic effects

M. Gopalswamy, T. Kroeger, D. Bickel, B. Frieg, S. Akter, S. Schott-Verdugo, A. Viegas, T. Pauly, M. Mayer, J. Przibilla, J. Reiners, L. Nagel-Steger, S. H. J. Smits, G. Groth, M. Etzkorn, H. Gohlke

This paper characterizes a small-molecule inhibitor of RUNX1/ETO tetramerization, showing it disrupts tetramer stability and has favorable pharmacokinetic properties for potential anti-leukemic therapy.

bioRxiv · Dec 22, 2021Biophysics

A structural and kinetic link between membrane association and amyloid fibril formation of α-Synuclein

T. Viennet, M. M. Wördehoff, B. Uluca, C. Poojari, H. Shaykhalishahi, D. Willbold, B. Strodel, H. Heise, A. K. Buell, W. Hoyer, M. Etzkorn

This study investigates how α-Synuclein interacts with membrane surfaces and how these interactions influence its aggregation into amyloid fibrils.

bioRxiv · Aug 8, 2017Biophysics