Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome-Reference-Cited by-同舟云学术

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Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome

Published:2010-05-10 Issue:21 Volume:107 Page:9620-9625
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Syed S. H.,Goutte-Gattat D.,Becker N.,Meyer S.,Shukla M. S.,Hayes J. J.,Everaers R.,Angelov D.,Bednar J.,Dimitrov S.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference24 articles.

1. Crystal structure of the nucleosome core particle at 2.8 Å resolution

2. Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin

3. Linker Histone-dependent DNA Structure in Linear Mononucleosomes

4. The globular domain of histone H5 is internally located in the 30 nm chromatin fiber: an immunochemical study.

5. Accessibility of the globular domain of histones H1 and H5 to antibodies upon folding of chromatin

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2. HMGB1 restores a dynamic chromatin environment in the presence of linker histone by deforming nucleosomal DNA;2024-08-24

3. A DNA condensation code for linker histones;Proceedings of the National Academy of Sciences;2024-08-08

4. Structural basis for linker histone H5–nucleosome binding and chromatin fiber compaction;Cell Research;2024-08-05

5. Chromatin compaction;Chromatin;2024

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