Seychelle M. Vos

CTCF dimerization on stacked nucleosomes is resolved by cryo-EM through a ZnF6-7-8 interface. Disrupting it in mouse stem cells weakens CTCF-cohesin loops more than insulation and impairs germline differentiation.

This study identifies the structural basis of BRD4 interaction with P-TEFb and shows how BRD4 and AFF4 regulate P-TEFb activity through distinct mechanisms.

A reconstituted, direct-RNA-sequencing transcription assay on 1,000 human promoter-proximal sequences identified a TFIIS-insensitive consensus super pause, whose cryo-EM structure shows a one-nucleotide sidetracked polymerase state.

DNAsight automates AFM image analysis of chromatin organization, revealing protein-specific structural signatures and nucleosome spacing distributions.

This study identifies ELOF1 as a critical factor enhancing promoter-proximal RNA polymerase II pausing, showing its role in counteracting TFIIF effects.

The paper shows CTCF controls chromatin boundary permeability through a dynamic conformational ensemble, not static occupancy, influencing cohesin capture probabilities.

The paper introduces chemical crosslinking with mass spectrometry and a new search engine, NuXL, to identify nucleic acid-protein crosslinks at amino acid resolution, enhancing structural analysis.

This paper presents the cryo-EM structure of a human AGO-guide complex bound to a fully paired target, revealing structural rearrangements that enable slicing-competent conformation and explain RNA slicing mechanism.

This study identifies a DNA binding region in MORC2 that is essential for gene silencing and shows that phosphorylation affects its DNA affinity and nuclear localization.

This study shows that MYC multimerization driven by RNA binding suppresses innate immune signaling by promoting exosome recruitment to R-loops and preventing immunogenic RNA accumulation.

The paper reports the cryo-EM structure of the complete S. cerevisiae Rpd3S-nucleosome complex, revealing its subunit arrangement and substrate specificity mechanisms.

The paper reports the cryo-EM structure of a mammalian transcribing RNA polymerase II-U1 snRNP complex and describes its role in co-transcriptional splicing.