Structural basis for histone H2B deubiquitination by the SAGA DUB module.
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Direct screening for chromatin status on DNA barcodes in yeast delineates the regulome of H3K79 methylation by Dot1Structural mechanism for the recognition and ubiquitination of a single nucleosome residue by Rad6-Bre1Molecular architecture of polycomb repressive complexesCentromeres are maintained by fastening CENP-A to DNA and directing an arginine anchor-dependent nucleosome transition.Chemical Synthesis of Phosphorylated Histone H2A at Tyr57 Reveals Insight into the Inhibition Mode of the SAGA Deubiquitinating Module.The Chd1 chromatin remodeler shifts hexasomes unidirectionally.Loss of GCN5 leads to increased neuronal apoptosis by upregulating E2F1- and Egr-1-dependent BH3-only protein Bim.Role of remodeling and spacing factor 1 in histone H2A ubiquitination-mediated gene silencing.Total chemical synthesis of SUMO-2-Lys63-linked diubiquitin hybrid chains assisted by removable solubilizing tags.Chemical and semisynthetic approaches to study and target deubiquitinases.Recognition of ubiquitinated nucleosomes.Cryo-electron microscopy of chromatin biology.SAGA complex mediates the transcriptional up-regulation of antiviral RNA silencing.The replicative lifespan-extending deletion of SGF73 results in altered ribosomal gene expression in yeast.Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.Chemical Synthesis of K34-Ubiquitylated H2B for Nucleosome Reconstitution and Single-Particle Cryo-Electron Microscopy Structural Analysis.Cytoplasmic ATXN7L3B Interferes with Nuclear Functions of the SAGA Deubiquitinase Module.The RNF168 paralog RNF169 defines a new class of ubiquitylated histone reader involved in the response to DNA damage.Structural and biochemical analyses of monoubiquitinated human histones H2B and H4.ATXN7L3 and ENY2 Coordinate Activity of Multiple H2B Deubiquitinases Important for Cellular Proliferation and Tumor Growth.The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6.Sortase-mediated chemical protein synthesis reveals the bidentate binding of bisphosphorylated p62 with K63 diubiquitin.Recruitment and allosteric stimulation of a histone deubiquitinating enzyme during heterochromatin assembly.A molecular engineering toolbox for the structural biologist.Structural diversity of the nucleosome.Ubiquitin Specific Peptidase 22 Regulates Histone H2B Mono-Ubiquitination and Exhibits Both Oncogenic and Tumor Suppressor Roles in Cancer.The evolutionarily conserved factor Sus1/ENY2 plays a role in telomere length maintenance.Total chemical synthesis of histones and their analogs, assisted by native chemical ligation and palladium complexes.ISWI chromatin remodellers sense nucleosome modifications to determine substrate preference.A systematic analysis of nucleosome core particle and nucleosome-nucleosome stacking structure.The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin.Whole-Genome Sequencing of Suppressor DNA Mixtures Identifies Pathways That Compensate for Chromosome Segregation Defects in Schizosaccharomyces pombe.Total Chemical Synthesis of Modified Histones.Mechanisms of Ubiquitin-Nucleosome Recognition and Regulation of 53BP1 Chromatin Recruitment by RNF168/169 and RAD18.Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding in Saccharomyces cerevisiae.Cryo-EM of nucleosome core particle interactions in trans.Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosomeActive site alanine mutations convert deubiquitinases into high-affinity ubiquitin-binding proteinsSpecificity for deubiquitination of monoubiquitinated FANCD2 is driven by the N-terminus of USP1
P2860
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P2860
Structural basis for histone H2B deubiquitination by the SAGA DUB module.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Structural basis for histone H2B deubiquitination by the SAGA DUB module.
@en
type
label
Structural basis for histone H2B deubiquitination by the SAGA DUB module.
@en
prefLabel
Structural basis for histone H2B deubiquitination by the SAGA DUB module.
@en
P2093
P2860
P356
P1433
P1476
Structural basis for histone H2B deubiquitination by the SAGA DUB module
@en
P2093
Alison E Ringel
Ashraf Brik
Mahmood Haj-Yahya
Michael T Morgan
Prasanthi Bandi
P2860
P304
P356
10.1126/SCIENCE.AAC5681
P407
P577
2016-02-01T00:00:00Z