Author

Gyula Hoffka

University of DebrecenORCID 0000-0002-1684-8538Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:statistical model· 3 Approach:simulation· 2 Organism:bacteria (other)· 1 Approach:deep learning· 1 Approach:experimental assay· 1 Research Focus:phylogenetics / evolution· 1 Research Focus:protein design· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

Shina Caroline Lynn KamerliniD· 2 shared Andrej BergiD· 1 shared Boldizsár Tüű-SzabóiD· 1 shared Colin Schür· 1 shared Dina ListoviD· 1 shared Elske van der PoliD· 1 shared Eva VosiD· 1 shared Jan Georg GerstenbergeriD· 1 shared

Activity by Year

2019-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiochemistry

Shina Caroline Lynn KamerlinORCID

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3 papers

Recent·Most cited

Ancestors of Arylmalonate Decarboxylase show increased Activity, Stability and Stereoselectivity

Elske van der Pol, Jan Georg Gerstenberger, Xenia Georgiadou, Gyula Hoffka, Lisa-Marie Krammer, Klaus Peter Schliep, Colin Schür, Shina Caroline Lynn Kamerlin, Selin Kara, Robert Kourist

Ancestral sequence reconstruction of a bacterial decarboxylase gave enzymes with up to 294-fold longer half-life at 45 °C, higher activity, and 99.7% ee on a vinyl malonate substrate.

bioRxiv · Aug 20, 2026 · PreprintBiochemistry✦ In-depth digest

High-efficiency Kemp eliminases by complete computational design

Dina Listov, Eva Vos, Gyula Hoffka, Shlomo Yakir Hoch, Andrej Berg, Shelly Hamer-Rogotner, Orly Dym, Shina Caroline Lynn Kamerlin, Sarel Jacob Fleishman

This paper presents a computational design of high-efficiency Kemp eliminases with unprecedented catalytic efficiency and stability through de novo enzyme design.

Nature · Jun 18, 2025Peer-reviewedBiochemistry

Altered dynamics may drift pathological fibrillization in membraneless organelles

Boldizsár Tüű-Szabó, Gyula Hoffka, Norbert Duro, L. Koczy, Mónika Fuxreiter

The paper uses a computational framework to show that linker dynamics regulate the phase transition and aggregation propensity of biomolecular condensates, with implications for pathological fibrillization.

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · Apr 15, 2019Peer-reviewedBioinformatics