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The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats
Eukaryotic chromatin is a complex yet dynamic structure, which is regulated in part by the assembly and disassembly of nucleosomes. Key to this process is a group of proteins termed histone chaperones that guide the thermodynamic assembly of nucleosomes by interacting with soluble histones. Here we...
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| Pubblicato in: | Nucleic Acids Res |
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| Autori principali: | , , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Oxford University Press
2016
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4838342/ https://ncbi.nlm.nih.gov/pubmed/26673727 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gkv1372 |
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