{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bartholomew B"],"funding":["NIGMS NIH HHS"],"pagination":["671-96"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4332854"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["83"],"pubmed_abstract":["A large family of chromatin remodelers that noncovalently modify chromatin is crucial in cell development and differentiation. They are often the targets of cancer, neurological disorders, and other human diseases. These complexes alter nucleosome positioning, higher-order chromatin structure, and nuclear organization. They also assemble chromatin, exchange out histone variants, and disassemble chromatin at defined locations. We review aspects of the structural organization of these complexes, the functional properties of their protein domains, and variation between complexes. We also address the mechanistic details of these complexes in mobilizing nucleosomes and altering chromatin structure. A better understanding of these issues will be vital for further analyses of subunits of these ch"],"journal":["Annual review of biochemistry"],"pubmed_title":["Regulating the chromatin landscape: structural and mechanistic perspectives."],"pmcid":["PMC4332854"],"funding_grant_id":["R01 GM048413"],"pubmed_authors":["Bartholomew B"],"additional_accession":[]},"is_claimable":false,"name":"Regulating the chromatin landscape: structural and mechanistic perspectives.","description":"A large family of chromatin remodelers that noncovalently modify chromatin is crucial in cell development and differentiation. They are often the targets of cancer, neurological disorders, and other human diseases. These complexes alter nucleosome positioning, higher-order chromatin structure, and nuclear organization. They also assemble chromatin, exchange out histone variants, and disassemble chromatin at defined locations. We review aspects of the structural organization of these complexes, the functional properties of their protein domains, and variation between complexes. We also address the mechanistic details of these complexes in mobilizing nucleosomes and altering chromatin structure. A better understanding of these issues will be vital for further analyses of subunits of these ch","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014","modification":"2025-04-21T21:15:26.121Z","creation":"2019-03-27T01:46:40Z"},"accession":"S-EPMC4332854","cross_references":{"pubmed":["24606138"],"doi":["10.1146/annurev-biochem-051810-093157"]}}