Histone fold modifications control nucleosome unwrapping and disassembly. - Wikidata - wikimedia - TriplyDB

Histone fold modifications control nucleosome unwrapping and disassembly.

Histone fold modifications control nucleosome unwrapping and disassembly.

http://www.wikidata.org/entity/Q35149617

about

DNA replication at the single-molecule level H3R42me2a is a histone modification with positive transcriptional effects New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?Structural dynamics of nucleosomes at single-molecule resolution Accessing DNA damage in chromatin: Preparing the chromatin landscape for base excision repair Post-translational modifications of histones that influence nucleosome dynamics Histone variants: the tricksters of the chromatin world Shearing of the CENP-A dimerization interface mediates plasticity in the octameric centromeric nucleosome.Chemical and biological tools for the preparation of modified histone proteins Application of the protein semisynthesis strategy to the generation of modified chromatin Discovery of histone modification crosstalk networks by stable isotope labeling of amino acids in cell culture mass spectrometry (SILAC MS)Solution scattering and FRET studies on nucleosomes reveal DNA unwrapping effects of H3 and H4 tail removal PHF1 Tudor and N-terminal domains synergistically target partially unwrapped nucleosomes to increase DNA accessibility Probing Nucleosome Stability with a DNA Origami Nanocaliper Micro- and nanoscale devices for the investigation of epigenetics and chromatin dynamics.Recent advances in single molecule studies of nucleosomes Unzipping single DNA molecules to study nucleosome structure and dynamics.Routes to DNA accessibility: alternative pathways for nucleosome unwinding.Quantitative models for accelerated protein dissociation from nucleosomal DNA.Scratching the (lateral) surface of chromatin regulation by histone modifications.Histone H3 globular domain acetylation identifies a new class of enhancers.Closing the gap between single molecule and bulk FRET analysis of nucleosomes Histone chaperone-mediated nucleosome assembly process Heritable capture of heterochromatin dynamics in Saccharomyces cerevisiae.Histones: at the crossroads of peptide and protein chemistry.Traceless semisynthesis of a set of histone 3 species bearing specific lysine methylation marks.Chromatin signatures at Notch-regulated enhancers reveal large-scale changes in H3K56ac upon activation.Histone core phosphorylation regulates DNA accessibility.Histone Acetylation near the Nucleosome Dyad Axis Enhances Nucleosome Disassembly by RSC and SWI/SNF.Distinct Cellular Assembly Stoichiometry of Polycomb Complexes on Chromatin Revealed by Single-molecule Chromatin Immunoprecipitation Imaging.Crucial role of dynamic linker histone binding and divalent ions for DNA accessibility and gene regulation revealed by mesoscale modeling of oligonucleosomes.Atomic force microscopy of chromatin arrays reveal non-monotonic salt dependence of array compaction in solution Regulation of the nucleosome unwrapping rate controls DNA accessibility.Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis Hybrid phase ligation for efficient synthesis of histone proteins.Cell-cycle-dependent structural transitions in the human CENP-A nucleosome in vivo.Site-specific Acetylation of Histone H3 Decreases Polymerase β Activity on Nucleosome Core Particles in Vitro Acetylated histone H3K56 interacts with Oct4 to promote mouse embryonic stem cell pluripotency.Electron Paramagnetic Resonance of a Single NV Nanodiamond Attached to an Individual Biomolecule.

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P2860

Histone fold modifications control nucleosome unwrapping and disassembly.

http://www.wikidata.org/entity/Q35149617

description

2011 nî lūn-bûn

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2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2011 թվականի հուլիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Histone fold modifications control nucleosome unwrapping and disassembly.

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Histone fold modifications control nucleosome unwrapping and disassembly.

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type

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Histone fold modifications control nucleosome unwrapping and disassembly.

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Histone fold modifications control nucleosome unwrapping and disassembly.

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prefLabel

Histone fold modifications control nucleosome unwrapping and disassembly.

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Histone fold modifications control nucleosome unwrapping and disassembly.

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PNAS.1106264108

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Histone fold modifications control nucleosome unwrapping and disassembly.

@en

P2093

Jennifer J Ottesen

http://www.w3.org/2001/XMLSchema#string

John C Shimko

http://www.w3.org/2001/XMLSchema#string

Justin A North

http://www.w3.org/2001/XMLSchema#string

Marek Simon

http://www.w3.org/2001/XMLSchema#string

Meng Zhang

http://www.w3.org/2001/XMLSchema#string

Michael G Poirier

http://www.w3.org/2001/XMLSchema#string

Michelle B Ferdinand

http://www.w3.org/2001/XMLSchema#string

Mridula Manohar

http://www.w3.org/2001/XMLSchema#string

Richard Fishel

http://www.w3.org/2001/XMLSchema#string

Robert A Forties

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Behavior of supercoiled DNA.

Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions

Architecture of the SWI/SNF-nucleosome complex.

Acetylation in histone H3 globular domain regulates gene expression in yeast.

Chromatin structure: a repeating unit of histones and DNA

Rad51 polymerization reveals a new chromatin remodeling mechanism

The biology of chromatin remodeling complexes

Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae.

Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes.

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12711-12716

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scholarly article

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10.1073/PNAS.1106264108

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31

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108

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51501451

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21768347

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3150920

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