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Bacteria Polyclonal MUTYH Primary Antibody for ICC, IF - ABIN153079
Bonde, Gao, Chen, Miyashita, Montgomery, Harmon, Wei: Duodenal reflux leads to down regulation of DNA mismatch repair pathway in an animal model of esophageal cancer. in The Annals of thoracic surgery 2007
Show all 9 Pubmed References
Human Monoclonal MUTYH Primary Antibody for IP, RNAi - ABIN561883
van der Post, Kets, Ligtenberg, van Krieken, Hoogerbrugge: Immunohistochemistry is not an accurate first step towards the molecular diagnosis of MUTYH-associated polyposis. in Virchows Archiv : an international journal of pathology 2008
Show all 7 Pubmed References
Human Polyclonal MUTYH Primary Antibody for IF, IHC - ABIN6712779
Shinmura, Goto, Suzuki, Tao, Yamada, Igarashi, Matsuura, Maeda, Konno, Matsuda, Sugimura: Reduced expression of MUTYH with suppressive activity against mutations caused by 8-hydroxyguanine is a novel predictor of a poor prognosis in human gastric cancer. in The Journal of pathology 2011
Show all 2 Pubmed References
Human Polyclonal MUTYH Primary Antibody for ELISA, WB - ABIN188666
Russo, De Luca, Casorelli, Degan, Molatore, Barone, Mazzei, Pannellini, Musiani, Bignami: Role of MUTYH and MSH2 in the control of oxidative DNA damage, genetic instability, and tumorigenesis. in Cancer research 2009
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This study demonstrated that the Cerebellar Abiotrophy associated single nucleotide polymorphism introduces a new binding site for a novel transcription factor (Myelin Transcription Factor-1 Like protein, MYT1L). and Cerebellar Abiotrophy-affected horses show differential expression of a specific isoform of MUTYH as well as different localization in the Purkinje and granular neurons of the cerebellum.
qPCR analysis of cDNA from the cerebella of affected and unaffected horses suggested that MUTYH expression is down-regulated in affected horses.
These findings suggest that MUTYH does not rely upon the wedge residue for damage site recognition, but this residue stabilizes the lesion recognition complex.
An intronic single nucleotide polymorphism in the MUTYH gene is associated with increased risk for hepatitis C virus-induced hepatocellular carcinoma.
This study aimed to evaluate patterns of APC and MUTYH germ-line mutations in Russian patients with colorectal malignancies. APC gene defects were identified in 26/38 (68%) subjects with colon polyposis; 8/26 (31%) APC mutations were associated with 2 known mutational hotspots
MUTYH gene mutation is associated with familial adenomatous polyposis.
Study did not find a significant increase in breast cancer risk associated with monoallelic MUTYH mutations.
Study reports the first cohort of individuals with MUTYH-associated polyposis identified by multi-gene hereditary cancer panel testing. Findings demonstrate a wide range of polyp count and a phenotypic spectrum overlapping with familial adenomatous polyposis and Lynch syndrome, including observations of extracolonic manifestations of each syndrome.
Genetic testing identified two heterozygous germline MUTYH mutations in both twins. In addition to the common hotspot mutation c.536A>G; p.Tyr179Cys, a new variant c.1323+1G>A (NM_001128425) was identified.
Findings highlight associations between the MUTYH Gln324His (CAG/CAC) polymorphism and susceptibility to cervical squamous cell carcinoma, high-risk human papillomavirus infection and specific prognostic factors, supporting the utility of this variant as an early indicator for patients at high risk of cervical carcinoma.
The MUTYH is similarly redox-active, but MUTYH C306W undergoes rapid oxidative degradation of its cluster to [3Fe4S](+), with loss of redox signalling.
The 2 main missense mutations of MUTYH - c.1145G>A, p.Gly382Asp and c.494A>G, p.Tyr165Cys were associated with the development of Colorectal adenomas/Serrated polyps in the monoallelic mutation carriers.
MUTYH and ORAI1 SNPs are associated with osteoarthritis susceptibility in the Chinese Han population
The MUTYH gene presents downregulation in the more advanced stages of colorectal cancer
MUTYH variants among Japanese colorectal polyposis patients.
Our results suggest that p.(Gly396Asp) in MUTYH, and potentially other mutations in additional members of the same DNA excision-repair pathway (such as the OGG1 gene) might be involved in driving the tumorigenesis leading to familial and sporadic small intestinal neuroendocrine tumors .
Knockdown of MYH in pancreatic cancer cells reduces tumor growth and sensitizes cells to antineoplastic agents.
Rheumatoid arthritis is associated with increased serum level of the MUTYH protein.
Inactivating MUTYH germline mutations are associated with high-grade midline gliomas.
this review focuses on multifaceted roles of MUTYH in the cell, both in the prevention of mutagenesis and tumorigenesis
Acetohexamide exerted this protective function by antagonizing expression of the DNA glycosylase, MUTYH. Together, our data reveal the existence of an NER-independent mechanism to remove UV-induced DNA damage and prevent cell death.
Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA.
results suggested that MYH, which interacts with TRADD, inhibits TNF-alpha necroptotic signaling. Therefore, MYH inactivation is essential for necroptosis via the downregulation of caspase-8.
Ogg1 and Mutyh regulate hippocampal gene expression related to cognition and behavior, suggesting a role for the glycosylases in regulating adaptive behavior.
MUTYH loss is associated with an increase in inflammation associated colorectal cancer risk, which involves immunosuppression and altered inflammatory response.
Results show that MYH is a vital DNA repair enzyme that protects cells from oxidative DNA damage and is critical for a proper cellular response to DNA damage.
a 5-methylcytosine glycosylase activity for the murine DNA base excision repair enzyme Myh is described and shown that it is critically involved in remodeling the IL-2 Promoter for transcription.
Data indicate that maternal folate depletion during pregnancy and high-fat feeding from weaning altered gene expression of Ogg1, Neil1, Mutyh and Xrcc1 in the brain of adult offspring.
The action of MUTYH, which initiates excision repair of adenine opposite 8-oxoG, triggers neurodegeneration in mice.
OGG1 and MYH appear to be dispensable for antimutator function in mitochondria.
Mutyh plays a major role in maintaining intestinal integrity by affecting the inflammatory response.
Aim of this study was to characterize the biological effects, in a mammalian cell background, of human MUTYH mutations identified in MUTYH-associated polyposis patients
Replication-associated repair of adenine:8-oxoguanine mispairs by MYH
a specific germ-line mutation (G382D) is identified in mutyH which may be responsible for the mutator phenotype
MUTYHalpha and MUTYHbeta were detected in wild-type embryonic stem (ES) cells or thymocytes prepared from wild-type mice
The C-terminal domain of MUTYH is necessary for its ability to prevent OGG1 or APEX1 from inappropriately processing its substrate.
Because there is an increased incidence of lung and small intestine cancer in Myh(-/-)/Ogg1(-/-) mice, these findings support a causal role for unrepaired oxidized DNA bases in cancer development.
MUTYH has a DNA glycosylase activity excising not only adenine opposite 8-oxoguanine (8-oxoG) but also 2-hydroxyadenine (2-OH-A) opposite guanine.
MUTYH suppresses spontaneous tumorigenesis in mice, thus providing experimental evidence for the association between biallelic germ-line MUTYH mutations and a recessive form of human hereditary colorectal adenoma and carcinoma
Required for normal cell-cycle progression and nuclear division, suggesting multiple roles of Myh in the maintenance of genome stability and tumor prevention.
A large fraction of the cancer-prone phenotype of Msh2 deficient mice depends on Mutyh activity.
This gene encodes a DNA glycosylase involved in oxidative DNA damage repair. The enzyme excises adenine bases from the DNA backbone at sites where adenine is inappropriately paired with guanine, cytosine, or 8-oxo-7,8-dihydroguanine, a major oxidatively damaged DNA lesion. The protein is localized to the nucleus and mitochondria. Mutations in this gene result in heritable predisposition to colon and stomach cancer. Multiple transcript variants encoding different isoforms have been found for this gene.
mutY homolog (E. coli)
, A/G-specific adenine DNA glycosylase
, A/G-specific adenine DNA glycosylase-like
, mutY homolog
, adenine-DNA glycosylase
, mutY homolog alpha
, the full-length form type A, 5' region