Defective MUTYH mutants do not cleave adenine mispaired with 8-oxoguanine - Wikidata - wikimedia - TriplyDB

Defective MUTYH mutants do not cleave adenine mispaired with 8-oxoguanine

Defective MUTYH mutants do not cleave adenine mispaired with 8-oxoguanine

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Defective MUTYH substrate processing

P527

Q56860949-B7BC5287-75E2-4A47-9450-CB8EFD5AF80B

P527

Defective MUTYH mutants do not cleave adenine mispaired with 8-oxoguanine

http://www.wikidata.org/entity/Q56858071

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An instance of the biological ...... h 8-oxoguanine in Homo sapiens

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biologisch proces

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name

Defective MUTYH mutants do not cleave adenine mispaired with 8-oxoguanine

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label

Defective MUTYH mutants do not cleave adenine mispaired with 8-oxoguanine

@en

prefLabel

Defective MUTYH mutants do not cleave adenine mispaired with 8-oxoguanine

@en

P2860

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Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis

Biallelic germline mutations in MYH predispose to multiple colorectal adenoma and somatic G:C-->T:A mutations

Multiple colorectal adenomas, classic adenomatous polyposis, and germ-line mutations in MYH

Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant proteins found in patients with colorectal polyposis and cancer

Functional characterization of human MutY homolog (hMYH) missense mutation (R231L) that is linked with hMYH-associated polyposis.

Cancer-associated variants and a common polymorphism of MUTYH exhibit reduced repair of oxidative DNA damage using a GFP-based assay in mammalian cells.

Catalytically impaired hMYH and NEIL1 mutant proteins identified in patients with primary sclerosing cholangitis and cholangiocarcinoma.

Characterization of mutant MUTYH proteins associated with familial colorectal cancer.

Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer.

Cells with pathogenic biallelic mutations in the human MUTYH gene are defective in DNA damage binding and repair.

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reactome:R-HSA-9605313

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biological process

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Defective MUTYH substrate processing

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R-HSA-9605313

http://www.w3.org/2001/XMLSchema#string

P527

MUTYH LOF mutants:(OGUA:Ade)-dsDNA

P703