DDB2 association with PCNA is required for its degradation after UV-induced DNA damage
Published 2013 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
DDB2 association with PCNA is required for its degradation after UV-induced DNA damage
Authors
Keywords
-
Journal
CELL CYCLE
Volume 13, Issue 2, Pages 240-248
Publisher
Informa UK Limited
Online
2013-12-06
DOI
10.4161/cc.26987
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair
- (2013) M. Robu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- p300/CBP acetyl transferases interact with and acetylate the nucleotide excision repair factor XPG
- (2012) Micol Tillhon et al. DNA REPAIR
- Direct Role for Proliferating Cell Nuclear Antigen in Substrate Recognition by the E3 Ubiquitin Ligase CRL4Cdt2
- (2012) Courtney G. Havens et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1
- (2012) Alex Pines et al. JOURNAL OF CELL BIOLOGY
- DDB2 promotes chromatin decondensation at UV-induced DNA damage
- (2012) Martijn S. Luijsterburg et al. JOURNAL OF CELL BIOLOGY
- Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization and its roles in chromatinized DNA repair
- (2012) J. I. Yeh et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase
- (2011) Jill O. Fuss et al. DNA REPAIR
- Dynamics of mammalian NER proteins
- (2011) Wim Vermeulen DNA REPAIR
- Mechanism of CRL4Cdt2, a PCNA-dependent E3 ubiquitin ligase
- (2011) C. G. Havens et al. GENES & DEVELOPMENT
- p21 Cooperates with DDB2 Protein in Suppression of Ultraviolet Ray-induced Skin Malignancies
- (2011) Tanya Stoyanova et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- p21CDKN1A participates in base excision repair by regulating the activity of poly(ADP-ribose) polymerase-1
- (2010) Ornella Cazzalini et al. DNA REPAIR
- CRL4Cdt2 E3 Ubiquitin Ligase Monoubiquitinates PCNA to Promote Translesion DNA Synthesis
- (2010) Kenta Terai et al. MOLECULAR CELL
- Multiple roles of the cell cycle inhibitor p21CDKN1A in the DNA damage response
- (2010) Ornella Cazzalini et al. MUTATION RESEARCH-REVIEWS IN MUTATION RESEARCH
- CUL4A Abrogation Augments DNA Damage Response and Protection against Skin Carcinogenesis
- (2009) Liren Liu et al. MOLECULAR CELL
- DDB2 decides cell fate following DNA damage
- (2009) T. Stoyanova et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex
- (2008) T. Abbas et al. GENES & DEVELOPMENT
- The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to control replication licensing
- (2008) Y. Kim et al. GENES & DEVELOPMENT
- CDK Inhibitor p21 Is Degraded by a Proliferating Cell Nuclear Antigen-coupled Cul4-DDB1Cdt2Pathway during S Phase and after UV Irradiation
- (2008) Hideo Nishitani et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Cellular Concentrations of DDB2 Regulate Dynamic Binding of DDB1 at UV-Induced DNA Damage
- (2008) S. Alekseev et al. MOLECULAR AND CELLULAR BIOLOGY
- Interaction of p21 CDKN1A with PCNA regulates the histone acetyltransferase activity of p300 in nucleotide excision repair
- (2008) Ornella Cazzalini et al. NUCLEIC ACIDS RESEARCH
- Regulation of proliferating cell nuclear antigen ubiquitination in mammalian cells
- (2008) A. Niimi et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationCreate your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create Now