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Human Monoclonal RAD23B Primary Antibody for WB - ABIN1944896
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
Show all 4 Pubmed References
Human Polyclonal RAD23B Primary Antibody for WB - ABIN2801856
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 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
Show all 2 Pubmed References
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
miR (show MLXIP Antibodies)-196b improved radiosensitivity of SNU-638 cells by targeting RAD23B.
Several mutations in the two parts of the central "crest" of the arrestin (show SAG Antibodies) molecule, middle-loop and C-loop, enhanced or reduced arrestin-3 (show ARRB2 Antibodies) interactions with several GPCRs in receptor subtype and functional state-specific manner.
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.
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.
RAD23, yeast homolog of, B
, UV excision repair protein RAD23 homolog B
, XP-C repair complementing complex 58 kDa
, XP-C repair complementing protein
, XP-C repair-complementing complex 58 kDa protein
, RAD23b homolog
, RAD23 homolog B (S. cerevisiae)
, RAD23 homolog B