Author

Patryk Ludzia

University of CambridgeORCID 0000-0002-1678-6875Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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

Frequent Co-Authors

Bungo AkiyoshiiD· 2 shared Christina RedfieldiD· 2 shared Midori IshiiiD· 2 shared Aleksandra Ciszek· 1 shared Christopher W. WoodiD· 1 shared Christos SpanosiD· 1 shared Gabriele MarcianòiD· 1 shared Gauri DeákiD· 1 shared

Activity by Year

2024-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersCell Biology

Bungo AkiyoshiORCID

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2 papers

Recent·Most cited

Cell BiologybioRxivPreprintAug 18, 2026

The centromere localization domain of kinetoplastid kinetochore protein KKT2 recognizes the free N-terminus of histone H3

Aleksandra Ciszek, Patryk Ludzia, Gabriele Marcianò…·Bungo Akiyoshi

This study shows that the KKT2 CL domain binds histone H3 N-terminus and that methylation of this region disrupts binding, suggesting a mechanism for kinetochore assembly in kinetoplastids.

DOI 10.64898/2026.08.13.744621

proteomicsexperimental assay

𝕏 PostBluesky

Cell BiologyStructurePeer-reviewedNov 22, 2024

The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail

Patryk Ludzia, Midori Ishii, Gauri Deák…·Bungo Akiyoshi

This study determines the structure and function of KKT23, a kinetochore acetyltransferase in trypanosomes, showing it acetylates histone H2A and interacts with KKT22.

7 citations

humanmouse

𝕏 PostBluesky