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XPC (show XPC ELISA Kits) dissociation from the damage site could become a rate-limiting step in nucleotide excision repair (NER (show NR1H2 ELISA Kits)) of certain types of DNA adducts, leading to repression of NER (show NR1H2 ELISA Kits).
HR23B role in DNA reapair, in protein degradation and stability, tumorigenesis and neurodegenerative disorders [review]
Data show that nucleotide excision repair factor XPC (show XPC ELISA Kits)-RAD23B is a target of poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 (PARP1 (show PARP1 ELISA Kits)).
RAD23B has a potential role in breast cancer progression and a tumor suppressor role of nuclear RAD23B in breast cancer.
It is unlikely that the RAD23B 249Val/Val polymorphism may contribute to the individual susceptibility to cancer risk.
Results define a regulatory mechanism that involves the interplay between HR23B and HDAC6 (show HDAC6 ELISA Kits) that influences the biological outcome of HDAC (show HDAC3 ELISA Kits) inhibitor treatment.
Polymorphism in RAD23B gene is associated with breast cancer.
HR23B expression was associated with disease stabilization for patients with unresectable hepatocellular carcinoma treated with epigenetic therapy using belinostat, a histone deacetylase (show HDAC1 ELISA Kits) inhibitor.
Single nucleotide polymorphisms of CCND2 (show CCND2 ELISA Kits), RAD23B, GRP78 (show HSPA5 ELISA Kits), CEP164 (show CEP164 ELISA Kits), MDM2 (show MDM2 ELISA Kits), and ALDH2 (show ALDH2 ELISA Kits) genes were significantly associated with development and recurrence of hepatocellular carcinoma in Japanese patients with hepatitis C virus.
PNGase (show NGLY1 ELISA Kits)-PUB serves not only as p97 (show EIF4G2 ELISA Kits)-binding module but also as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms.
the mammalian RAD23 proteins play a direct role in damage recognition by enhancing the binding of XPC (show XPC ELISA Kits) to DNA damage in living cells in addition to stabilizing XPC (show XPC ELISA Kits). RAD23 proteins rapidly dissociated from XPC (show XPC ELISA Kits) upon binding to damaged DNA.
analysis of mHR23A/B double-mutant cells showed that HR23 proteins function in nucleotide excision repair by governing xeroderma pigmentosum group C protein stability via partial protection against proteasomal degradation
The crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma pigmentosum group C binding domain from HR23B is described; the results suggest a co-evolution of ER-associated degradation and DNA repair pathways.
This illustrates that impairment of the ubiquitin-proteasome system (UPS) by expanded glutamine (show GFPT1 ELISA Kits) repeats, including the sequestration of HR23B, is not affecting NER (show NR1H2 ELISA Kits).
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in the nucleotide excision repair (NER). This protein was found to be a component of the protein complex that specifically complements the NER defect of xeroderma pigmentosum group C (XP-c) cell extracts in vitro. This protein was also shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, and thus this protein may be involved in the ubiquitin mediated proteolytic pathway in cells. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
UV excision repair protein RAD23 homolog B
, RAD23 homolog B (S. cerevisiae)
, RAD23 homolog B
, RAD23, yeast homolog of, B
, XP-C repair complementing complex 58 kDa
, XP-C repair complementing protein
, XP-C repair-complementing complex 58 kDa protein
, RAD23b homolog