DDB2 promotes chromatin decondensation at UV-induced DNA damage
In addition to its role in DNA lesion recognition, the damaged DNA-binding protein DDB2 elicits unfolding of large-scale chromatin structure independently of the CRL4 ubiquitin ligase complex.
Main Authors: | Luijsterburg, Martijn S., Lindh, Michael, Acs, Klara, Vrouwe, Mischa G., Pines, Alex, van Attikum, Haico, Mullenders, Leon H., Dantuma, Nico P. |
---|---|
Format: | Online |
Language: | English |
Published: |
The Rockefeller University Press
2012
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3328393/ |
Similar Items
-
PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1
by: Pines, Alex, et al.
Published: (2012) -
SUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites
by: González-Prieto, Román, et al.
Published: (2015) -
Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly
by: Segura-Totten, Miriam, et al.
Published: (2002) -
Proposed mechanism for sperm chromatin condensation/decondensation in the male rat
by: Chapman, John C, et al.
Published: (2003) -
Ectopically tethered CP190 induces large-scale chromatin decondensation
by: Ahanger, Sajad H., et al.
Published: (2014)