Author

Ricardo Zarate

Freie Universität Berlin

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

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Approach:deep learning· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

Beate KokschiD· 2 shared Kevin PageliD· 2 shared Andreas HermanniD· 1 shared Artem PavloviD· 1 shared Birgit StrodeliD· 1 shared Boris SchadeiD· 1 shared Charlotte Radelof· 1 shared Clemens KrageiD· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiophysics

Beate KokschORCID

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Glycosaminoglycans Promote Amyloid-β Aggregation via Multivalent, pH-Dependent Interactions

Eunjin Moon, Charlotte Radelof, Jana Sticht, Yu Wang, Felicia Fürstenberg, Clemens Krage, Sebastian Straeten, Wesley Pietsch, Boris Schade, Artem Pavlov, Ricardo Zarate, Gaël M. Vos, Gergő Péter Szekeres, Birgit Strodel, Beate Koksch, , Nicklas Österlund

This study shows glycosaminoglycans promote amyloid-β aggregation under acidic conditions through pH-dependent electrostatic interactions and multivalency.

bioRxiv · May 20, 2026 · PreprintBiophysics

HMGB1 B-box domain self-complexes promote protein-polyelectrolyte interactions.

Marten Kagelmacher, Marina A. Pigaleva, Ricardo Zarate, Leïla Bechtella, Kevin Pagel, Beate Koksch, Jens Dernedde, Andreas Hermann, Thomas Risse

This study shows that HMGB1's B-box domain forms self-associates that enhance interactions with heparin through charge redistribution and conformational changes.

bioRxiv · Mar 28, 2025 · PreprintBiochemistry