<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Luger K</submitter><funding>Howard Hughes Medical Institute</funding><funding>NIGMS NIH HHS</funding><pagination>436-47</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3408961</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(7)</volume><pubmed_abstract>The compaction of genomic DNA into chromatin has profound implications for the regulation of key processes such as transcription, replication and DNA repair. Nucleosomes, the repeating building blocks of chromatin, vary in the composition of their histone protein components. This is the result of the incorporation of variant histones and post-translational modifications of histone amino acid side chains. The resulting changes in nucleosome structure, stability and dynamics affect the compaction of nucleosomal arrays into higher-order structures. It is becoming clear that chromatin structures are not nearly as uniform and regular as previously assumed. This implies that chromatin structure must also be viewed in the context of specific biological functions.</pubmed_abstract><journal>Nature reviews. Molecular cell biology</journal><pubmed_title>New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?</pubmed_title><pmcid>PMC3408961</pmcid><funding_grant_id>GM088409</funding_grant_id><funding_grant_id>P01 GM088409</funding_grant_id><pubmed_authors>Tremethick DJ</pubmed_authors><pubmed_authors>Dechassa ML</pubmed_authors><pubmed_authors>Luger K</pubmed_authors></additional><is_claimable>false</is_claimable><name>New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?</name><description>The compaction of genomic DNA into chromatin has profound implications for the regulation of key processes such as transcription, replication and DNA repair. Nucleosomes, the repeating building blocks of chromatin, vary in the composition of their histone protein components. This is the result of the incorporation of variant histones and post-translational modifications of histone amino acid side chains. The resulting changes in nucleosome structure, stability and dynamics affect the compaction of nucleosomal arrays into higher-order structures. It is becoming clear that chromatin structures are not nearly as uniform and regular as previously assumed. This implies that chromatin structure must also be viewed in the context of specific biological functions.</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Jun</publication><modification>2025-04-18T17:22:35.68Z</modification><creation>2019-06-05T17:29:22Z</creation></dates><accession>S-EPMC3408961</accession><cross_references><pubmed>22722606</pubmed><doi>10.1038/nrm3382</doi></cross_references></HashMap>