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Dog (Canine) Monoclonal RAD23B Primary Antibody for IF, WB - ABIN968319
Masutani, Sugasawa, Yanagisawa, Sonoyama, Ui, Enomoto, Takio, Tanaka, van der Spek, Bootsma: Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. in The EMBO journal 1994
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Dog (Canine) Monoclonal RAD23B Primary Antibody for IF, WB - ABIN968320
Reardon, Mu, Sancar: Overproduction, purification, and characterization of the XPC subunit of the human DNA repair excision nuclease. in The Journal of biological chemistry 1996
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Human Monoclonal RAD23B Primary Antibody for WB - ABIN1944896
Huang, Wang, Xu, Lu, Xu, Li, Zhou, Sha: Expression of a novel RAD23B mRNA splice variant in the human testis. in Journal of andrology 2004
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Human Polyclonal RAD23B Primary Antibody for WB - ABIN2801856
Ota, Suzuki, Nishikawa, Otsuki, Sugiyama, Irie, Wakamatsu, Hayashi, Sato, Nagai, Kimura, Makita, Sekine, Obayashi, Nishi, Shibahara, Tanaka, Ishii, Yamamoto, Saito, Kawai, Isono, Nakamura, Nagahari et al.: Complete sequencing and characterization of 21,243 full-length human cDNAs. ... in Nature genetics 2003
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Human Polyclonal RAD23B Primary Antibody for ELISA, WB - ABIN129561
Shen, Valencia, Szostak, Szostak, Dong, Liu: Scanning the human proteome for calmodulin-binding proteins. in Proceedings of the National Academy of Sciences of the United States of America 2005
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Human Polyclonal RAD23B Primary Antibody for ICC, IF - ABIN4317293
Jones, Moskaluk, Gillenwater, Petroni, Burks, Philips, Rehm, Olazagasti, Kozower, Bao: Phase I trial of induction histone deacetylase and proteasome inhibition followed by surgery in non-small-cell lung cancer. in Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer 2012
XPC (show XPC Antibodies) dissociation from the damage site could become a rate-limiting step in nucleotide excision repair (NER (show NR1H2 Antibodies)) of certain types of DNA adducts, leading to repression of NER (show NR1H2 Antibodies).
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 Antibodies)-RAD23B is a target of poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 (PARP1 (show PARP1 Antibodies)).
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 Antibodies) that influences the biological outcome of HDAC (show HDAC3 Antibodies) 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 Antibodies) inhibitor.
Single nucleotide polymorphisms of CCND2 (show CCND2 Antibodies), RAD23B, GRP78 (show HSPA5 Antibodies), CEP164 (show CEP164 Antibodies), MDM2 (show MDM2 Antibodies), and ALDH2 (show ALDH2 Antibodies) genes were significantly associated with development and recurrence of hepatocellular carcinoma in Japanese patients with hepatitis C virus.
PNGase (show NGLY1 Antibodies)-PUB serves not only as p97 (show EIF4G2 Antibodies)-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 Antibodies) to DNA damage in living cells in addition to stabilizing XPC (show XPC Antibodies). RAD23 proteins rapidly dissociated from XPC (show XPC Antibodies) 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 Antibodies) repeats, including the sequestration of HR23B, is not affecting NER (show NR1H2 Antibodies).
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