SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites
Published 2017 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites
Authors
Keywords
-
Journal
Nucleus
Volume 9, Issue 1, Pages 87-94
Publisher
Informa UK Limited
Online
2017-11-03
DOI
10.1080/19491034.2017.1395543
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Genetic complementation analysis showed distinct contributions of the N-terminal tail of H2A.Z to epigenetic regulations
- (2016) Masayuki Kusakabe et al. GENES TO CELLS
- Coordinated Regulation of TIP60 and Poly(ADP-Ribose) Polymerase 1 in Damaged-Chromatin Dynamics
- (2016) Masae Ikura et al. MOLECULAR AND CELLULAR BIOLOGY
- Histone Variant H2A.Z.2 Mediates Proliferation and Drug Sensitivity of Malignant Melanoma
- (2015) Chiara Vardabasso et al. MOLECULAR CELL
- Reorganization of Damaged Chromatin by the Exchange of Histone Variant H2A.Z-2
- (2014) Ikuno Nishibuchi et al. INTERNATIONAL JOURNAL OF RADIATION ONCOLOGY BIOLOGY PHYSICS
- SWR1 and INO80 Chromatin Remodelers Contribute to DNA Double-Strand Break Perinuclear Anchorage Site Choice
- (2014) Chihiro Horigome et al. MOLECULAR CELL
- Structural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2
- (2013) Naoki Horikoshi et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- SETD6 monomethylates H2AZ on lysine 7 and is required for the maintenance of embryonic stem cell self-renewal
- (2013) Olivier Binda et al. Epigenetics
- Activation of the SUMO modification system is required for the accumulation of RAD51 at sites of DNA damage
- (2013) H. Shima et al. JOURNAL OF CELL SCIENCE
- Gene dysregulation by histone variant H2A.Z in bladder cancer
- (2013) Kyunghwan Kim et al. Epigenetics & Chromatin
- Histone phosphorylation
- (2012) Dorine Rossetto et al. Epigenetics
- Histone H2A.Z Controls a Critical Chromatin Remodeling Step Required for DNA Double-Strand Break Repair
- (2012) Ye Xu et al. MOLECULAR CELL
- Histone methylation: a dynamic mark in health, disease and inheritance
- (2012) Eric L. Greer et al. NATURE REVIEWS GENETICS
- H2A.Z-dependent crosstalk between enhancer and promoter regulates Cyclin D1 expression
- (2012) M Dalvai et al. ONCOGENE
- Acetylation of H2A.Z is a key epigenetic modification associated with gene deregulation and epigenetic remodeling in cancer
- (2011) F. Valdes-Mora et al. GENOME RESEARCH
- Identification and characterization of the two isoforms of the vertebrate H2A.Z histone variant
- (2010) Ryo Matsuda et al. NUCLEIC ACIDS RESEARCH
- The SWR1 Histone Replacement Complex Causes Genetic Instability and Genome-Wide Transcription Misregulation in the Absence of H2A.Z
- (2010) Macarena Morillo-Huesca et al. PLoS One
- The evolutionary differentiation of two histone H2A.Z variants in chordates (H2A.Z-1 and H2A.Z-2) is mediated by a stepwise mutation process that affects three amino acid residues
- (2009) José M Eirín-López et al. BMC EVOLUTIONARY BIOLOGY
- Chromosome-wide Rad51 Spreading and SUMO-H2A.Z-Dependent Chromosome Fixation in Response to a Persistent DNA Double-Strand Break
- (2009) Marian Kalocsay et al. MOLECULAR CELL
- Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks
- (2009) Yaron Galanty et al. NATURE
- The DNA-damage response in human biology and disease
- (2009) Stephen P. Jackson et al. NATURE
- Histone Ubiquitination: Triggering Gene Activity
- (2008) Vikki M. Weake et al. MOLECULAR CELL
- Genomic analysis of estrogen cascade reveals histone variant H2A.Z associated with breast cancer progression
- (2008) Sujun Hua et al. Molecular Systems Biology
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreCreate your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create Now