Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The human BAF chromatin remodeler processes nucleosomes bound by pioneer transcription factors OCT4-SOX2.
Journal, issue, pages	Mol Cell, Vol. 86, Issue 4, Page 625-639.e8, Year 2026
Publish date	Feb 19, 2026
Authors	Joscha Weiss / Luca Vecchia / David Domjan / Simone Cavadini / Anton Sabantsev / Georg Kempf / Ganesh R Pathare / Klaus Brackmann / Alicia K Michael / Lukas Kater / Eric Hietter-Pfeiffer / Mina Haddawi / Urja P Kuber / Sandra Mühlhäusser / Ralph S Grand / Michael B Stadler / Sebastian Deindl / Nicolas H Thomä /
PubMed Abstract	Chromatin remodeling complexes mobilize nucleosomes and promote transcription factor (TF) binding. Using ensemble and single-molecule assays combined with cryo-electron microscopy (cryo-EM), we ...Chromatin remodeling complexes mobilize nucleosomes and promote transcription factor (TF) binding. Using ensemble and single-molecule assays combined with cryo-electron microscopy (cryo-EM), we studied the interaction between pioneer TFs OCT4-SOX2 and the human BRG1/BRM-associated factor (BAF) complex on nucleosomes. BAF engages TF-bound substrates in two orientations, placing OCT4-SOX2 at either the remodeler ENTRY or EXIT site. At the ENTRY site, OCT4-SOX2 initially coexists with BAF without structural interference. However, continued DNA translocation is expected to cause collisions with bound TFs, which can trigger remodeling direction reversals or may induce TF dissociation. To accommodate TFs at the EXIT site, BAF undergoes structural rearrangements, and ensemble assays reveal a nucleosome subpopulation translocating away from TF-binding sites. Moreover, single-molecule experiments show that nucleosome-bound BAF frequently changes remodeling direction, and we identify an ADP-bound remodeler conformation as a potential intermediate. Together, these findings reveal key aspects of the conformational dynamics and remodeling outcomes underlying BAF processing of TF-bound nucleosomes.
External links	Mol Cell / PubMed:41679301
Methods	EM (single particle)
Resolution	3.5 - 6.52 Å
Structure data	54030 9rl4 EMDB-54030, PDB-9rl4: Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL-6 Method: EM (single particle) / Resolution: 3.5 Å 54056 9rmc EMDB-54056, PDB-9rmc: Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL+6 class 1 Method: EM (single particle) / Resolution: 4.2 Å 54077 9rn1 EMDB-54077, PDB-9rn1: Structure of BAF-nucleosome complex with OCT4-SOX2 at SHL+6 in ADP-bound state, BAF47 bound to ATPase lobe 2 Method: EM (single particle) / Resolution: 5.9 Å 54078 9rn2 EMDB-54078, PDB-9rn2: Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL+6 class 2 Method: EM (single particle) / Resolution: 4.1 Å EMDB-54154: Structure of BAF-nucleosome complex with OCT4-SOX2 at SHL+6 in ADP-bound state, BAF47 bound to ATPase lobe 2 (Focused refinement of nucleosome and ATPase lobes) Method: EM (single particle) / Resolution: 4.17 Å EMDB-54155: Structure of BAF-nucleosome complex with OCT4-SOX2 at SHL+6 in ADP-bound state, BAF47 bound to ATPase lobe 2 (Consensus map) Method: EM (single particle) / Resolution: 5.63 Å EMDB-54156: Structure of BAF-nucleosome complex with OCT4-SOX2 at SHL+6 in ADP-bound state, BAF47 bound to ATPase lobe 2 (Focused refinement of BAF) Method: EM (single particle) / Resolution: 6.52 Å
Chemicals	ChemComp-PTD: PENTANEDIAL ChemComp-ZN: Unknown entry
Source	homo sapiens (human) synthetic construct (others) Homo spaiens (human) aequorea victoria (jellyfish)
Keywords	GENE REGULATION / remodelling / chromatin / transcription / remodeler / remodeller