Author

Michel Choudalakis

University of StuttgartORCID 0000-0002-8778-3380Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Developmental Biology· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Assay:ChIP-seq· 3 Research Focus:differential expression· 2 Approach:experimental assay· 2 Research Focus:gene regulatory network inference· 2 Organism:human· 2 Organism:mouse· 2 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1

Frequent Co-Authors

Albert JeltschiD· 2 shared Pavel BashtrykoviD· 2 shared Adeel ManafiD· 1 shared Alexander Bröhm· 1 shared Alexandra G. Kouroukli· 1 shared Annika V Geijer-SimpsoniD· 1 shared Arne KlunglandiD· 1 shared Elisabeth KommisrudiD· 1 shared

Activity by Year

2023-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

Albert JeltschORCID

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3 papers

Recent·Most cited

Major waves of H2A.Z incorporation during mouse oogenesis

Madeleine Fosslie, Erkut Ilaslan, Trine Skuland, Michel Choudalakis, M. Dige Soegaard, Jason Alexander Halliwell, Shaista Khan, Marie Indahl, María Vera-Rodríguez, Adeel Manaf, Annika V Geijer-Simpson, Rajikala Suganthan, Ingunn Jermstad, Knut Tomas Dalen, Ragnhild Eskeland, , Mads Lerdrup

The paper maps H2A.Z incorporation during mouse oogenesis, identifying distinct patterns and their relationship with epigenetic marks and transposable elements.

Nature Communications · Dec 2, 2025Peer-reviewedDevelopmental Biology

SETDB1 activity is globally directed by H3K14 acetylation via its Triple Tudor Domain

T. T. Chandrasekaran, Michel Choudalakis, Alexander Bröhm, Sara Weirich, Alexandra G. Kouroukli, Ole Ammerpohl, Philipp Rathert, Pavel Bashtrykov, Albert Jeltsch

This study shows that H3K14 acetylation directs SETDB1 activity via its Triple Tudor Domain, enabling H3K9 methylation and heterochromatin formation.

Nucleic Acids Research · Oct 24, 2024Peer-reviewedBiochemistry

Refined read-out: The hUHRF1 Tandem-Tudor domain prefers binding to histone H3 tails containing K4me1 in the context of H3K9me2/3

Michel Choudalakis, Goran Kungulovski, Rebekka Mauser, Pavel Bashtrykov, Albert Jeltsch

This study identifies a novel read-out mechanism of UHRF1-TTD binding to H3K4me1-K9me2/3 double marks, showing its role in gene down-regulation and chromatin binding.

Protein Science · Aug 18, 2023Peer-reviewedMolecular Biology