PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
19300419-4	2009	MUTYH gene encodes a DNA glycosylase that can initiate the base excision repair (BER) pathway and prevent G:C > T:A transversion by excising adenine mispaired with 8-hydroxyguanine produced by reactive oxygen species (ROS).	Adenine	141-148	mutY DNA glycosylase	Homo sapiens	0-5
19300419-4	2009	MUTYH gene encodes a DNA glycosylase that can initiate the base excision repair (BER) pathway and prevent G:C > T:A transversion by excising adenine mispaired with 8-hydroxyguanine produced by reactive oxygen species (ROS).	8-hydroxyguanine	164-180	mutY DNA glycosylase	Homo sapiens	0-5
19300419-4	2009	MUTYH gene encodes a DNA glycosylase that can initiate the base excision repair (BER) pathway and prevent G:C > T:A transversion by excising adenine mispaired with 8-hydroxyguanine produced by reactive oxygen species (ROS).	Reactive Oxygen Species	193-216	mutY DNA glycosylase	Homo sapiens	0-5
19300419-4	2009	MUTYH gene encodes a DNA glycosylase that can initiate the base excision repair (BER) pathway and prevent G:C > T:A transversion by excising adenine mispaired with 8-hydroxyguanine produced by reactive oxygen species (ROS).	Reactive Oxygen Species	218-221	mutY DNA glycosylase	Homo sapiens	0-5
18534194-1	2008	BACKGROUND & AIMS: The human mutyh gene encodes a base excision repair protein that prevents G:C to T:A transversions in DNA.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	33-38
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Glutamine	266-269	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Glutamine	266-269	mutY DNA glycosylase	Homo sapiens	69-73
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Glutamine	266-269	mutY DNA glycosylase	Homo sapiens	250-254
18848840-8	2008	In the smoking group, there was a 0.15-fold (OR(adj), 0.15; 95% CI, 0.03-0.68; P=0.01) decreased risk of CBP for subjects carrying genotypes of hMYH 324His/Gln+Gln/Gln compared with those of genotype of hMYH 324His/His.	Glutamine	156-159	mutY DNA glycosylase	Homo sapiens	144-148
18848840-8	2008	In the smoking group, there was a 0.15-fold (OR(adj), 0.15; 95% CI, 0.03-0.68; P=0.01) decreased risk of CBP for subjects carrying genotypes of hMYH 324His/Gln+Gln/Gln compared with those of genotype of hMYH 324His/His.	Glutamine	160-163	mutY DNA glycosylase	Homo sapiens	144-148
18848840-8	2008	In the smoking group, there was a 0.15-fold (OR(adj), 0.15; 95% CI, 0.03-0.68; P=0.01) decreased risk of CBP for subjects carrying genotypes of hMYH 324His/Gln+Gln/Gln compared with those of genotype of hMYH 324His/His.	Glutamine	160-163	mutY DNA glycosylase	Homo sapiens	144-148
18848840-8	2008	In the smoking group, there was a 0.15-fold (OR(adj), 0.15; 95% CI, 0.03-0.68; P=0.01) decreased risk of CBP for subjects carrying genotypes of hMYH 324His/Gln+Gln/Gln compared with those of genotype of hMYH 324His/His.	Histidine	152-155	mutY DNA glycosylase	Homo sapiens	144-148
19032956-1	2009	BACKGROUND & AIMS: Biallelic mutations in the base excision DNA repair gene MUTYH lead to MUTYH-associated polyposis (MAP) and predisposition to colorectal cancer (CRC).	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	80-85
19032956-1	2009	BACKGROUND & AIMS: Biallelic mutations in the base excision DNA repair gene MUTYH lead to MUTYH-associated polyposis (MAP) and predisposition to colorectal cancer (CRC).	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	94-99
19513679-5	2009	Knockdown of MUTYH which excises adenine opposite 8-oxoG in DNA prevents degradation of mitochondrial DNA and activation of calpain, thus suppressing the cell death induced by menadione.	Adenine	33-40	mutY DNA glycosylase	Homo sapiens	13-18
19513679-5	2009	Knockdown of MUTYH which excises adenine opposite 8-oxoG in DNA prevents degradation of mitochondrial DNA and activation of calpain, thus suppressing the cell death induced by menadione.	Vitamin K 3	176-185	mutY DNA glycosylase	Homo sapiens	13-18
20110747-1	2009	BACKGROUND: Biallelic MUTYH exon 7 and 13 mutations are associated with a high frequency of somatic K-ras gene guanine to thymine transversion mutations at codon 12 position 1 in MUTYH-associated polyposis patients who have increased risk of colon cancer.	Guanine	111-118	mutY DNA glycosylase	Homo sapiens	22-27
20110747-1	2009	BACKGROUND: Biallelic MUTYH exon 7 and 13 mutations are associated with a high frequency of somatic K-ras gene guanine to thymine transversion mutations at codon 12 position 1 in MUTYH-associated polyposis patients who have increased risk of colon cancer.	Guanine	111-118	mutY DNA glycosylase	Homo sapiens	179-184
20110747-1	2009	BACKGROUND: Biallelic MUTYH exon 7 and 13 mutations are associated with a high frequency of somatic K-ras gene guanine to thymine transversion mutations at codon 12 position 1 in MUTYH-associated polyposis patients who have increased risk of colon cancer.	Thymine	122-129	mutY DNA glycosylase	Homo sapiens	22-27
20110747-1	2009	BACKGROUND: Biallelic MUTYH exon 7 and 13 mutations are associated with a high frequency of somatic K-ras gene guanine to thymine transversion mutations at codon 12 position 1 in MUTYH-associated polyposis patients who have increased risk of colon cancer.	Thymine	122-129	mutY DNA glycosylase	Homo sapiens	179-184
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	326cys	54-60	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Cysteine	57-60	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	324his	74-80	mutY DNA glycosylase	Homo sapiens	69-73
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	324his	74-80	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Histidine	77-80	mutY DNA glycosylase	Homo sapiens	69-73
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Histidine	77-80	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Cysteine	61-64	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Serine	230-233	mutY DNA glycosylase	Homo sapiens	69-73
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Serine	230-233	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Serine	238-241	mutY DNA glycosylase	Homo sapiens	69-73
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Serine	238-241	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	324his	255-261	mutY DNA glycosylase	Homo sapiens	69-73
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	324his	255-261	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Glutamine	262-265	mutY DNA glycosylase	Homo sapiens	69-73
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Glutamine	262-265	mutY DNA glycosylase	Homo sapiens	250-254
18848840-7	2008	Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln.	Glutamine	266-269	mutY DNA glycosylase	Homo sapiens	69-73
19013464-1	2008	BACKGROUND & AIMS: MYH-associated polyposis (MAP) is a disorder caused by a bi-allelic germline MYH mutation, characterized by multiple colorectal adenomas.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	23-26
18534194-4	2008	METHODS: MUTYH variants were cloned and assayed for their glycosylase and DNA binding activities using synthetic double-stranded oligonucleotide substrates by analyzing cleavage products by polyacrylamide gel electrophoresis.	Oligonucleotides	129-144	mutY DNA glycosylase	Homo sapiens	9-14
18534194-4	2008	METHODS: MUTYH variants were cloned and assayed for their glycosylase and DNA binding activities using synthetic double-stranded oligonucleotide substrates by analyzing cleavage products by polyacrylamide gel electrophoresis.	polyacrylamide	190-204	mutY DNA glycosylase	Homo sapiens	9-14
18155253-3	2008	OGG1, NEIL1 and MUTYH are all involved in the repair and prevention of 8-oxodG-derived mutations and may be up-regulated by oxidative stress.	8-ohdg	71-78	mutY DNA glycosylase	Homo sapiens	16-21
18776649-0	2008	OGG1, MYH and MTH1 gene variants identified in gastric cancer patients exhibiting both 8-hydroxy-2"-deoxyguanosine accumulation and low inflammatory cell infiltration in their gastric mucosa.	8-ohdg	87-114	mutY DNA glycosylase	Homo sapiens	6-9
18271935-1	2008	The MUTYH gene encodes a DNA glycosylase that can initiate the base excision repair pathway and prevent G:C > T:A transversion by excising adenine mispaired with 8-hydroxyguanine.	Adenine	142-149	mutY DNA glycosylase	Homo sapiens	4-9
18271935-1	2008	The MUTYH gene encodes a DNA glycosylase that can initiate the base excision repair pathway and prevent G:C > T:A transversion by excising adenine mispaired with 8-hydroxyguanine.	8-hydroxyguanine	165-181	mutY DNA glycosylase	Homo sapiens	4-9
17638869-1	2007	MUTYH is a mammalian DNA glycosylase that initiates base excision repair by excising adenine opposite 8-oxoguanine and 2-hydroxyadenine opposite guanine, thereby preventing G:C to T:A transversion caused by oxidative stress.	Adenine	85-92	mutY DNA glycosylase	Homo sapiens	0-5
18172263-0	2008	Identification of patients with (atypical) MUTYH-associated polyposis by KRAS2 c.34G > T prescreening followed by MUTYH hotspot analysis in formalin-fixed paraffin-embedded tissue.	Formaldehyde	143-151	mutY DNA glycosylase	Homo sapiens	43-48
18172263-0	2008	Identification of patients with (atypical) MUTYH-associated polyposis by KRAS2 c.34G > T prescreening followed by MUTYH hotspot analysis in formalin-fixed paraffin-embedded tissue.	Paraffin	158-166	mutY DNA glycosylase	Homo sapiens	43-48
17207658-2	2007	Several pathways are involved in the repair of DNA lesions caused by oxidative stress, such as the base excision repair system (BER), which repairs mutation involving 8-oxoguanine and comprises the MUTYH, OGG1 and MTH1 genes.	8-hydroxyguanine	167-179	mutY DNA glycosylase	Homo sapiens	198-203
17638869-1	2007	MUTYH is a mammalian DNA glycosylase that initiates base excision repair by excising adenine opposite 8-oxoguanine and 2-hydroxyadenine opposite guanine, thereby preventing G:C to T:A transversion caused by oxidative stress.	8-hydroxyguanine	102-114	mutY DNA glycosylase	Homo sapiens	0-5
17638869-1	2007	MUTYH is a mammalian DNA glycosylase that initiates base excision repair by excising adenine opposite 8-oxoguanine and 2-hydroxyadenine opposite guanine, thereby preventing G:C to T:A transversion caused by oxidative stress.	isoguanine	119-135	mutY DNA glycosylase	Homo sapiens	0-5
17638869-1	2007	MUTYH is a mammalian DNA glycosylase that initiates base excision repair by excising adenine opposite 8-oxoguanine and 2-hydroxyadenine opposite guanine, thereby preventing G:C to T:A transversion caused by oxidative stress.	Guanine	107-114	mutY DNA glycosylase	Homo sapiens	0-5
17581577-4	2007	The importance of preventing mutations associated with 8-oxoguanine is shown by a direct association between defects in the DNA glycosylase MUTYH and colorectal cancer.	8-hydroxyguanine	55-67	mutY DNA glycosylase	Homo sapiens	140-145
17219200-2	2007	The base excision repair gene MYH protects against ROS-mediated damage to DNA.	Reactive Oxygen Species	51-54	mutY DNA glycosylase	Homo sapiens	30-33
17081686-1	2007	The MutY homolog (MYH) can excise adenines misincorporated opposite to guanines or 7,8-dihydro-8-oxo-guanines (8-oxoG) during DNA replication; thereby preventing G:C to T:A transversions.	Adenine	34-42	mutY DNA glycosylase	Homo sapiens	18-21
17081686-1	2007	The MutY homolog (MYH) can excise adenines misincorporated opposite to guanines or 7,8-dihydro-8-oxo-guanines (8-oxoG) during DNA replication; thereby preventing G:C to T:A transversions.	Guanine	71-79	mutY DNA glycosylase	Homo sapiens	18-21
17081686-1	2007	The MutY homolog (MYH) can excise adenines misincorporated opposite to guanines or 7,8-dihydro-8-oxo-guanines (8-oxoG) during DNA replication; thereby preventing G:C to T:A transversions.	7,8-dihydro-8-oxoguanine	83-109	mutY DNA glycosylase	Homo sapiens	18-21
17425590-8	2007	MUTYH, a mammalian ortholog of E. coli MutY, excises an adenine paired with 8-oxoG.	Adenine	56-63	mutY DNA glycosylase	Homo sapiens	0-5
17279544-4	2007	The other two enzymes are 8-oxoG DNA glycosylase encoded by the OGG1 gene and adenine/2-hydroxyadenine DNA glycosylase encoded by the MUTYH gene.	Adenine	78-85	mutY DNA glycosylase	Homo sapiens	134-139
17279544-4	2007	The other two enzymes are 8-oxoG DNA glycosylase encoded by the OGG1 gene and adenine/2-hydroxyadenine DNA glycosylase encoded by the MUTYH gene.	isoguanine	86-102	mutY DNA glycosylase	Homo sapiens	134-139
17279544-5	2007	We have shown a significant increase in 8-oxoG in mitochondrial DNA as well as an elevated expression of MTH1, OGG1, and MUTYH in nigrostriatal dopaminergic neurons of PD patients, suggesting that the buildup of these lesions may cause dopamine neuron loss.	Dopamine	144-152	mutY DNA glycosylase	Homo sapiens	121-126
17135312-6	2006	Immunodepletion of the NE with antibody against OGG1 or MYH decreased the incision of DNA adducts induced by As2O3, NaAsO2, monomethylarsonic acid, and dimethylarsinic acid, while antibodies against XPA, XPB, XPD, XPF, or XPG, did not.	monomethylarsonic acid	124-146	mutY DNA glycosylase	Homo sapiens	56-59
16769088-2	2007	In mammalian cells, base excision repair (BER) mediated by the OGG1 and MYH DNA glycosylases prevents the accumulation of 8-oxoguanine (8-oxoG) in DNA.	8-hydroxyguanine	122-134	mutY DNA glycosylase	Homo sapiens	72-75
16769088-2	2007	In mammalian cells, base excision repair (BER) mediated by the OGG1 and MYH DNA glycosylases prevents the accumulation of 8-oxoguanine (8-oxoG) in DNA.	8-hydroxyguanine	136-142	mutY DNA glycosylase	Homo sapiens	72-75
17368238-1	2007	BACKGROUND & AIMS: Whereas it has conclusively been demonstrated that biallelic MutY human homolog (MYH) mutations confer a significant risk for colorectal cancer (CRC), the influence of monoallelic mutations remains controversial.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	104-107
17161978-3	2007	MUTYH functions as a base excision repair DNA glycosylase that excises adenines misincorporated opposite 8-oxo-7,8-dihydro-2"-deoxyguanosine, one of the most stable products of oxidative DNA damage.	Adenine	71-79	mutY DNA glycosylase	Homo sapiens	0-5
17161978-3	2007	MUTYH functions as a base excision repair DNA glycosylase that excises adenines misincorporated opposite 8-oxo-7,8-dihydro-2"-deoxyguanosine, one of the most stable products of oxidative DNA damage.	8-ohdg	105-140	mutY DNA glycosylase	Homo sapiens	0-5
16879101-1	2006	The MYH (MutY glycosylase homologue) increases replication fidelity by removing adenines or 2-hydroxyadenine misincorporated opposite GO (7,8-dihydro-8-oxo-guanine).	Adenine	80-88	mutY DNA glycosylase	Homo sapiens	4-7
16879101-1	2006	The MYH (MutY glycosylase homologue) increases replication fidelity by removing adenines or 2-hydroxyadenine misincorporated opposite GO (7,8-dihydro-8-oxo-guanine).	isoguanine	92-108	mutY DNA glycosylase	Homo sapiens	4-7
16879101-1	2006	The MYH (MutY glycosylase homologue) increases replication fidelity by removing adenines or 2-hydroxyadenine misincorporated opposite GO (7,8-dihydro-8-oxo-guanine).	7,8-dihydro-8-oxoguanine	138-163	mutY DNA glycosylase	Homo sapiens	4-7
16879101-9	2006	A significant fraction of the hMYH nuclear foci co-localizes with hRad9 foci in H2O2-treated cells.	Hydrogen Peroxide	80-84	mutY DNA glycosylase	Homo sapiens	30-34
17135312-6	2006	Immunodepletion of the NE with antibody against OGG1 or MYH decreased the incision of DNA adducts induced by As2O3, NaAsO2, monomethylarsonic acid, and dimethylarsinic acid, while antibodies against XPA, XPB, XPD, XPF, or XPG, did not.	Cacodylic Acid	152-172	mutY DNA glycosylase	Homo sapiens	56-59
17135312-7	2006	These results suggest that these trivalent arsenicals induce the formation of only oxidative DNA adducts and that OGG1 and MYH are involved in these incision processes.	Arsenicals	43-53	mutY DNA glycosylase	Homo sapiens	123-126
16720376-1	2006	The base excision repair carried out by bacterial MutY DNA glycosylase and eukaryotic MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite G and 7,8-dihydro-8-oxo-guanines (8-oxoG); thereby preventing G:C to T:A mutations.	Adenine	133-141	mutY DNA glycosylase	Homo sapiens	100-103
17135312-6	2006	Immunodepletion of the NE with antibody against OGG1 or MYH decreased the incision of DNA adducts induced by As2O3, NaAsO2, monomethylarsonic acid, and dimethylarsinic acid, while antibodies against XPA, XPB, XPD, XPF, or XPG, did not.	Arsenic Trioxide	109-114	mutY DNA glycosylase	Homo sapiens	56-59
17135312-6	2006	Immunodepletion of the NE with antibody against OGG1 or MYH decreased the incision of DNA adducts induced by As2O3, NaAsO2, monomethylarsonic acid, and dimethylarsinic acid, while antibodies against XPA, XPB, XPD, XPF, or XPG, did not.	sodium arsenite	116-122	mutY DNA glycosylase	Homo sapiens	56-59
16720376-1	2006	The base excision repair carried out by bacterial MutY DNA glycosylase and eukaryotic MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite G and 7,8-dihydro-8-oxo-guanines (8-oxoG); thereby preventing G:C to T:A mutations.	7,8-dihydro-8-oxoguanine	182-208	mutY DNA glycosylase	Homo sapiens	100-103
16720376-1	2006	The base excision repair carried out by bacterial MutY DNA glycosylase and eukaryotic MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite G and 7,8-dihydro-8-oxo-guanines (8-oxoG); thereby preventing G:C to T:A mutations.	7,8-dihydro-8-oxoguanine	210-216	mutY DNA glycosylase	Homo sapiens	100-103
16720376-4	2006	The eukaryotic MYH can excise adenines misincorporated opposite GO, G, or C; remove 2-hydroxyadenines mispaired with A,G, and GO; excise G from G/GO mismatch weakly, thereby preventing G:C to T:A transversions.	Adenine	30-38	mutY DNA glycosylase	Homo sapiens	15-18
16720376-4	2006	The eukaryotic MYH can excise adenines misincorporated opposite GO, G, or C; remove 2-hydroxyadenines mispaired with A,G, and GO; excise G from G/GO mismatch weakly, thereby preventing G:C to T:A transversions.	isoguanine	84-101	mutY DNA glycosylase	Homo sapiens	15-18
16773329-2	2006	The human MutY homolog (hMUTYH) which removes misincorporated adenine opposite 8-oxoG in DNA functions in post-replication, and is localized in the nuclei and mitochondria.	Adenine	62-69	mutY DNA glycosylase	Homo sapiens	24-30
16616356-1	2006	BACKGROUND & AIMS: Biallelic mutations in the base-excision repair gene MYH have recently been associated with recessive inheritance of multiple colorectal adenomas.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	76-79
16606334-7	2006	MUTYH deficiency may also increase G:C to T:A transversions through the misincorporation of 2-OH-dATP, especially in the intestinal tract, since MUTYH can excise 2-hydroxyadenine opposite guanine in genomic DNA and the repair activity is selectively impaired by a mutation found in patients with autosomal recessive colorectal adenomatous polyposis.	2-hydroxydeoxyadenosine triphosphate	92-101	mutY DNA glycosylase	Homo sapiens	0-5
16606334-7	2006	MUTYH deficiency may also increase G:C to T:A transversions through the misincorporation of 2-OH-dATP, especially in the intestinal tract, since MUTYH can excise 2-hydroxyadenine opposite guanine in genomic DNA and the repair activity is selectively impaired by a mutation found in patients with autosomal recessive colorectal adenomatous polyposis.	isoguanine	162-178	mutY DNA glycosylase	Homo sapiens	0-5
16606334-7	2006	MUTYH deficiency may also increase G:C to T:A transversions through the misincorporation of 2-OH-dATP, especially in the intestinal tract, since MUTYH can excise 2-hydroxyadenine opposite guanine in genomic DNA and the repair activity is selectively impaired by a mutation found in patients with autosomal recessive colorectal adenomatous polyposis.	Guanine	188-195	mutY DNA glycosylase	Homo sapiens	0-5
16292541-2	2006	Subjects with inflammatory liver disease and one non-functional allele of the base excision repair gene, MYH, may be more susceptible to progression to cancer due to MYH haploinsufficiency in repairing oxidative damage caused by ROS.	Reactive Oxygen Species	229-232	mutY DNA glycosylase	Homo sapiens	105-108
16081110-9	2005	Here, we review the polymorphic forms of OGG1, MUTYH and MTH1 involved in repair of 8-OH-G and 8-OH-dGTP, and discuss the significance of the polymorphisms in the maintenance of genomic integrity.	8-oh-g	84-90	mutY DNA glycosylase	Homo sapiens	47-52
16425850-2	2005	The MutYH protein is a base excision repair glycosylase which is involved in the repair of damage caused by the oxidation ofa guanine leading to 8-oxo-7,8-dihydroguanine.	Guanine	126-133	mutY DNA glycosylase	Homo sapiens	4-9
16425850-2	2005	The MutYH protein is a base excision repair glycosylase which is involved in the repair of damage caused by the oxidation ofa guanine leading to 8-oxo-7,8-dihydroguanine.	8-hydroxyguanine	145-169	mutY DNA glycosylase	Homo sapiens	4-9
16793363-1	2006	The base excision repair carried out by the bacterial MutY DNA glycosylase and eukaryotic MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite 7,8-dihydro-8-oxo-guanines (8-oxoG), thereby preventing G:C to T:A mutations.	Adenine	137-145	mutY DNA glycosylase	Homo sapiens	104-107
16793363-1	2006	The base excision repair carried out by the bacterial MutY DNA glycosylase and eukaryotic MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite 7,8-dihydro-8-oxo-guanines (8-oxoG), thereby preventing G:C to T:A mutations.	7,8-dihydro-8-oxoguanine	180-206	mutY DNA glycosylase	Homo sapiens	104-107
16793363-1	2006	The base excision repair carried out by the bacterial MutY DNA glycosylase and eukaryotic MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite 7,8-dihydro-8-oxo-guanines (8-oxoG), thereby preventing G:C to T:A mutations.	7,8-dihydro-8-oxoguanine	208-214	mutY DNA glycosylase	Homo sapiens	104-107
16793363-2	2006	MutY and MYH can also remove adenines from A/G and A/C and can remove guanines from G/8-oxoG mismatches at reduced rates.	Adenine	29-37	mutY DNA glycosylase	Homo sapiens	9-12
16793363-2	2006	MutY and MYH can also remove adenines from A/G and A/C and can remove guanines from G/8-oxoG mismatches at reduced rates.	Guanine	70-78	mutY DNA glycosylase	Homo sapiens	9-12
16081110-9	2005	Here, we review the polymorphic forms of OGG1, MUTYH and MTH1 involved in repair of 8-OH-G and 8-OH-dGTP, and discuss the significance of the polymorphisms in the maintenance of genomic integrity.	8-hydroxy-2'-deoxyguanosine 5'-triphosphate	95-104	mutY DNA glycosylase	Homo sapiens	47-52
15987719-4	2005	Mutant MUTYH proteins in these four cell lines possess significantly lowered binding and cleavage activities with heteroduplex oligonucleotides containing A.8-oxoG and 8-oxoA.G mispairs.	Oligonucleotides	127-143	mutY DNA glycosylase	Homo sapiens	7-12
15987719-4	2005	Mutant MUTYH proteins in these four cell lines possess significantly lowered binding and cleavage activities with heteroduplex oligonucleotides containing A.8-oxoG and 8-oxoA.G mispairs.	8-oxog	157-163	mutY DNA glycosylase	Homo sapiens	7-12
15987719-4	2005	Mutant MUTYH proteins in these four cell lines possess significantly lowered binding and cleavage activities with heteroduplex oligonucleotides containing A.8-oxoG and 8-oxoA.G mispairs.	8-hydroxyadenine	168-174	mutY DNA glycosylase	Homo sapiens	7-12
15673720-1	2005	The base excision repair DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite guanine or 7,8-dihydro-8-oxo-guanine (8-oxoG), thereby preventing G:C to T:A mutations.	Adenine	88-96	mutY DNA glycosylase	Homo sapiens	55-58
16234049-1	2005	BACKGROUND & AIMS: Affected individuals with biallelic MYH mutations are believed to display multiple adenomatous polyps without evidence of vertical transmission.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	59-62
15673720-1	2005	The base excision repair DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite guanine or 7,8-dihydro-8-oxo-guanine (8-oxoG), thereby preventing G:C to T:A mutations.	Guanine	131-138	mutY DNA glycosylase	Homo sapiens	55-58
15673720-1	2005	The base excision repair DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite guanine or 7,8-dihydro-8-oxo-guanine (8-oxoG), thereby preventing G:C to T:A mutations.	7,8-dihydro-8-oxoguanine	142-167	mutY DNA glycosylase	Homo sapiens	55-58
15673720-1	2005	The base excision repair DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated into DNA opposite guanine or 7,8-dihydro-8-oxo-guanine (8-oxoG), thereby preventing G:C to T:A mutations.	7,8-dihydro-8-oxoguanine	169-175	mutY DNA glycosylase	Homo sapiens	55-58
15180946-1	2004	The MYH gene encodes a DNA glycosylase involved in the excision repair of adenines paired with 8-hydroxyguanines, a major component of oxidative DNA damage, and bi-allelic germline MYH mutations have been reported to predispose individuals to multiple colorectal adenomas and carcinoma.	Adenine	74-82	mutY DNA glycosylase	Homo sapiens	4-7
15681617-4	2005	Mutant mMUTYH with G365D amino acid substitution, corresponding to a G382D germline mutation of human MUTYH found in familial adenomatous polyposis patients, almost completely retained its DNA glycosylase activity excising adenine opposite 8-oxoG; however, it possessed 1.5% of the wild-type activity excising 2-OH-A opposite guanine.	Adenine	223-230	mutY DNA glycosylase	Homo sapiens	8-13
15681617-4	2005	Mutant mMUTYH with G365D amino acid substitution, corresponding to a G382D germline mutation of human MUTYH found in familial adenomatous polyposis patients, almost completely retained its DNA glycosylase activity excising adenine opposite 8-oxoG; however, it possessed 1.5% of the wild-type activity excising 2-OH-A opposite guanine.	2-oh-a	310-316	mutY DNA glycosylase	Homo sapiens	8-13
15681617-4	2005	Mutant mMUTYH with G365D amino acid substitution, corresponding to a G382D germline mutation of human MUTYH found in familial adenomatous polyposis patients, almost completely retained its DNA glycosylase activity excising adenine opposite 8-oxoG; however, it possessed 1.5% of the wild-type activity excising 2-OH-A opposite guanine.	Guanine	326-333	mutY DNA glycosylase	Homo sapiens	8-13
15681617-5	2005	Our results imply that the reduced repair capacity of the mutant hMUTYH(G382D), which inefficiently excises 2-OH-A opposite guanine, results in an increased occurrence of somatic G:C to T:A transversion mutations in the APC gene as well as tumorigenesis in the colon.	2-oh-a	108-114	mutY DNA glycosylase	Homo sapiens	65-71
15681617-5	2005	Our results imply that the reduced repair capacity of the mutant hMUTYH(G382D), which inefficiently excises 2-OH-A opposite guanine, results in an increased occurrence of somatic G:C to T:A transversion mutations in the APC gene as well as tumorigenesis in the colon.	Guanine	124-131	mutY DNA glycosylase	Homo sapiens	65-71
15533944-1	2005	The DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated opposite DNA strands containing guanine or 7,8-dihydro-8-oxoguanine by base excision repair thereby preventing G:C to T:A mutations.	Adenine	67-75	mutY DNA glycosylase	Homo sapiens	34-37
15533944-1	2005	The DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated opposite DNA strands containing guanine or 7,8-dihydro-8-oxoguanine by base excision repair thereby preventing G:C to T:A mutations.	Guanine	124-131	mutY DNA glycosylase	Homo sapiens	34-37
15533944-1	2005	The DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated opposite DNA strands containing guanine or 7,8-dihydro-8-oxoguanine by base excision repair thereby preventing G:C to T:A mutations.	7,8-dihydro-8-oxoguanine	135-159	mutY DNA glycosylase	Homo sapiens	34-37
15231485-3	2004	The mammalian homolog of the bacterial DNA mismatch repair enzyme MutY (MYH) removes A*8-oxoG from nuclear and mtDNA, reduces 8-oxoG accumulation, and restores genomic stability after ROS exposure.	Reactive Oxygen Species	184-187	mutY DNA glycosylase	Homo sapiens	72-75
15180946-10	2004	These results suggested that the ability to repair 8-hydroxyguanine in nuclear DNA may differ among Japanese individuals due to the splicing abnormality based on the MYH IVS10-2A > G variant, and that the bi-allelic IVS10-2A > G variation may be responsible for the occurrence of GC.	8-hydroxyguanine	51-67	mutY DNA glycosylase	Homo sapiens	166-169
15180946-1	2004	The MYH gene encodes a DNA glycosylase involved in the excision repair of adenines paired with 8-hydroxyguanines, a major component of oxidative DNA damage, and bi-allelic germline MYH mutations have been reported to predispose individuals to multiple colorectal adenomas and carcinoma.	8-hydroxyguanine	95-112	mutY DNA glycosylase	Homo sapiens	4-7
15293549-5	2004	MUTYH excises adenine opposite 8-oxoG, and thus suppresses 8-oxoG-induced mutagenesis.	Adenine	14-21	mutY DNA glycosylase	Homo sapiens	0-5
15450125-9	2004	RESULTS: Cell killing assays demonstrated cells over-expressing hMYH had improved survival to both increased oxygen and IR.	Oxygen	109-115	mutY DNA glycosylase	Homo sapiens	64-68
15450125-13	2004	CONCLUSION: Increased expression of the DNA glycosylase repair enzyme hMYH in A549 cells exposed to O2 and IR leads to improvements in cell survival.	Oxygen	100-102	mutY DNA glycosylase	Homo sapiens	70-74
15236166-1	2004	BACKGROUND & AIMS: MYH-associated polyposis is a recently described disease that is characterized by multiple colorectal adenomas and a recessive pattern of inheritance.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	23-26
15310837-2	2004	The mammalian homolog of the Escherichia coli MutY DNA glycosylase (MYH) cleaves adenine residues paired with either oxidized or non-modified guanines.	Adenine	81-88	mutY DNA glycosylase	Homo sapiens	68-71
15310837-2	2004	The mammalian homolog of the Escherichia coli MutY DNA glycosylase (MYH) cleaves adenine residues paired with either oxidized or non-modified guanines.	Guanine	142-150	mutY DNA glycosylase	Homo sapiens	68-71
15034862-1	2004	Biallelic germ-line variants of the 8-hydroxyguanine repair gene MYH have been associated with multiple colorectal adenomas that display somatic G:C-->T:A transversions in APC.	8-hydroxyguanine	36-52	mutY DNA glycosylase	Homo sapiens	65-68
15293549-5	2004	MUTYH excises adenine opposite 8-oxoG, and thus suppresses 8-oxoG-induced mutagenesis.	8-oxog	31-37	mutY DNA glycosylase	Homo sapiens	0-5
15293549-5	2004	MUTYH excises adenine opposite 8-oxoG, and thus suppresses 8-oxoG-induced mutagenesis.	8-oxog	59-65	mutY DNA glycosylase	Homo sapiens	0-5
15293549-6	2004	MUTYH also possesses a 2-OH-A DNA glycosylase activity for excising 2-OH-A incorporated into the cellular genomes.	2-oh-a	23-29	mutY DNA glycosylase	Homo sapiens	0-5
15056851-5	2004	Unlike these enzymes, hMYH removes intact A misincorporated opposite template 8-oxoguanine during DNA replication.	8-hydroxyguanine	78-90	mutY DNA glycosylase	Homo sapiens	22-26
15056851-8	2004	For cleavage of the N-glycosidic bond, bifunctional DNA glycosylases (hNTH1, hNEIL1, hNEIL2, and hOGG1) use Lys or Pro for direct attack on sugar C1", whereas monofunctional DNA glycosylases (hSMUG1 and hMYH) use an activated water molecule.	Proline	115-118	mutY DNA glycosylase	Homo sapiens	203-207
12807753-7	2003	These results indicate that OGG1 and MYH function as suppressors for G:C to T:A transversions by 8OHG but not by BPDE in human cells.	8ohg	97-101	mutY DNA glycosylase	Homo sapiens	37-40
12917422-1	2003	To evaluate the antimutagenic role of a mammalian mutY homolog, namely the Mutyh gene, which encodes adenine DNA glycosylase excising adenine misincorporated opposite 8-oxoguanine in the template DNA, we generated MUTYH-null mouse embryonic stem (ES) cells.	Adenine	101-108	mutY DNA glycosylase	Homo sapiens	75-80
12917422-1	2003	To evaluate the antimutagenic role of a mammalian mutY homolog, namely the Mutyh gene, which encodes adenine DNA glycosylase excising adenine misincorporated opposite 8-oxoguanine in the template DNA, we generated MUTYH-null mouse embryonic stem (ES) cells.	Adenine	101-108	mutY DNA glycosylase	Homo sapiens	214-219
12917422-1	2003	To evaluate the antimutagenic role of a mammalian mutY homolog, namely the Mutyh gene, which encodes adenine DNA glycosylase excising adenine misincorporated opposite 8-oxoguanine in the template DNA, we generated MUTYH-null mouse embryonic stem (ES) cells.	8-hydroxyguanine	167-179	mutY DNA glycosylase	Homo sapiens	75-80
12807753-0	2003	Suppressive activities of OGG1 and MYH proteins against G:C to T:A mutations caused by 8-hydroxyguanine but not by benzo[a]pyrene diol epoxide in human cells in vivo.	8-hydroxyguanine	87-103	mutY DNA glycosylase	Homo sapiens	35-38
12807753-2	2003	In this study, we assessed the abilities of OGG1, MYH and APE1 proteins, which are components of a base excision repair pathway, to suppress G:C to T:A transversions caused by 8OHG or BPDE by a bacterial suppressor tRNA (supF) forward mutation assay using a shuttle plasmid, pMY189.	8ohg	176-180	mutY DNA glycosylase	Homo sapiens	50-53
14579148-1	2004	The base excision repair gene MYH protects against damage to DNA from reactive oxygen species, which are commonly found in cigarette smoke.	Reactive Oxygen Species	70-93	mutY DNA glycosylase	Homo sapiens	30-33
12628248-2	2003	The Escherichia coli adenine glycosylase MutY and its human homolog (hMYH) play an important role in the prevention of mutations associated with OG by removing misincorporated adenine residues from OG:A mismatches.	8-ohdg	145-147	mutY DNA glycosylase	Homo sapiens	69-73
12807753-2	2003	In this study, we assessed the abilities of OGG1, MYH and APE1 proteins, which are components of a base excision repair pathway, to suppress G:C to T:A transversions caused by 8OHG or BPDE by a bacterial suppressor tRNA (supF) forward mutation assay using a shuttle plasmid, pMY189.	7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide	184-188	mutY DNA glycosylase	Homo sapiens	50-53
12628248-2	2003	The Escherichia coli adenine glycosylase MutY and its human homolog (hMYH) play an important role in the prevention of mutations associated with OG by removing misincorporated adenine residues from OG:A mismatches.	Adenine	21-28	mutY DNA glycosylase	Homo sapiens	69-73
12062055-6	2002	The Myh DNA glycosylase removes mismatched adenines incorporated opposite 8-oxoG during replication.	Adenine	43-51	mutY DNA glycosylase	Homo sapiens	4-7
12079537-3	2002	Recent studies have shown that 2-ohA is removed from DNA by a human MutY homolog, MYH protein, in vitro.	2-oha	31-36	mutY DNA glycosylase	Homo sapiens	82-85
12056405-1	2002	BACKGROUND: Adenine paired with 8-hydroxyguanine, a major oxidatively damaged DNA lesion, is excised by mutY homologue (MYH) base excision repair protein in human cells.	Adenine	12-19	mutY DNA glycosylase	Homo sapiens	120-123
12056405-1	2002	BACKGROUND: Adenine paired with 8-hydroxyguanine, a major oxidatively damaged DNA lesion, is excised by mutY homologue (MYH) base excision repair protein in human cells.	8-hydroxyguanine	32-48	mutY DNA glycosylase	Homo sapiens	120-123
11554292-8	2001	Major substrates of these enzymes, a uracil opposite an adenine for UNG2 and an adenine opposite an 8-oxoguanine for MYH, are formed during DNA replication.	Uracil	37-43	mutY DNA glycosylase	Homo sapiens	117-120
11805113-1	2002	The MutY homolog (MYH) is responsible for removing adenines misincorporated on a template DNA strand containing G or 7,8-dihydro-8-oxoguanine (8-oxoG) and thus preventing G:C to T:A mutations.	Adenine	51-59	mutY DNA glycosylase	Homo sapiens	18-21
11805113-1	2002	The MutY homolog (MYH) is responsible for removing adenines misincorporated on a template DNA strand containing G or 7,8-dihydro-8-oxoguanine (8-oxoG) and thus preventing G:C to T:A mutations.	7,8-dihydro-8-oxoguanine	117-141	mutY DNA glycosylase	Homo sapiens	18-21
11801590-2	2002	The human MutY homolog (hMYH), a DNA glycosylase, removes adenines from these mismatches.	Adenine	58-66	mutY DNA glycosylase	Homo sapiens	24-28
11801590-6	2002	The hMutSalpha binding site is mapped to amino acid residues 232-254 of hMYH, a region conserved in the MutY family.	hmutsalpha	4-14	mutY DNA glycosylase	Homo sapiens	72-76
11801590-7	2002	Moreover, the binding and glycosylase activities of hMYH with an A/7,8-dihydro-8-oxo-deoxyguanine mismatch are enhanced by hMutSalpha.	7,8-dihydro-8-oxo-deoxyguanine	67-97	mutY DNA glycosylase	Homo sapiens	52-56
11535925-0	2001	Alteration of DNA base excision repair enzymes hMYH and hOGG1 in hydrogen peroxide resistant transformed human breast cells.	Hydrogen Peroxide	65-82	mutY DNA glycosylase	Homo sapiens	47-51
11864576-0	2002	Replication-associated repair of adenine:8-oxoguanine mispairs by MYH.	Adenine	33-40	mutY DNA glycosylase	Homo sapiens	66-69
11864576-0	2002	Replication-associated repair of adenine:8-oxoguanine mispairs by MYH.	8-hydroxyguanine	41-53	mutY DNA glycosylase	Homo sapiens	66-69
11864576-4	2002	MYH, a mammalian homolog of Escherichia coli MutY, is a DNA glycosylase responsible for initiating base excision repair of such a mispair by excising the adenine opposite 8-oxoG.	Adenine	154-161	mutY DNA glycosylase	Homo sapiens	0-3
11433026-0	2001	hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs.	Adenine	152-159	mutY DNA glycosylase	Homo sapiens	0-4
11433026-0	2001	hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs.	8-hydroxyguanine	160-172	mutY DNA glycosylase	Homo sapiens	0-4
11433026-1	2001	The human MutY homolog, hMYH, is an adenine-specific DNA glycosylase that removes adenines or 2-hydroxyadenines mispaired with guanines or 8-oxoguanines.	Adenine	82-90	mutY DNA glycosylase	Homo sapiens	24-28
11433026-1	2001	The human MutY homolog, hMYH, is an adenine-specific DNA glycosylase that removes adenines or 2-hydroxyadenines mispaired with guanines or 8-oxoguanines.	isoguanine	94-111	mutY DNA glycosylase	Homo sapiens	24-28
11433026-1	2001	The human MutY homolog, hMYH, is an adenine-specific DNA glycosylase that removes adenines or 2-hydroxyadenines mispaired with guanines or 8-oxoguanines.	Guanine	127-135	mutY DNA glycosylase	Homo sapiens	24-28
11433026-1	2001	The human MutY homolog, hMYH, is an adenine-specific DNA glycosylase that removes adenines or 2-hydroxyadenines mispaired with guanines or 8-oxoguanines.	8-hydroxyguanine	139-152	mutY DNA glycosylase	Homo sapiens	24-28
11410677-1	2001	Human MutY homolog (hMYH), an adenine DNA glycosylase, can effectively remove misincorporated adenines opposite template G or 8-oxoG bases, thereby preventing G:C-->T:A transversions.	Adenine	94-102	mutY DNA glycosylase	Homo sapiens	20-24
11410677-5	2001	Moreover, the protein-DNA complex of bacterially expressed hMYH migrates much faster than that of native hMYH in a non-denaturing polyacrylamide gel.	polyacrylamide	130-144	mutY DNA glycosylase	Homo sapiens	59-63
11410677-5	2001	Moreover, the protein-DNA complex of bacterially expressed hMYH migrates much faster than that of native hMYH in a non-denaturing polyacrylamide gel.	polyacrylamide	130-144	mutY DNA glycosylase	Homo sapiens	105-109
11376687-11	2001	There is a significant homology between MTH1 protein and the C-terminal half of human MYH protein, which may be involved in the recognition of 8-oxoguanine and 2-hydroxyadenine.	8-hydroxyguanine	143-155	mutY DNA glycosylase	Homo sapiens	86-89
11376687-11	2001	There is a significant homology between MTH1 protein and the C-terminal half of human MYH protein, which may be involved in the recognition of 8-oxoguanine and 2-hydroxyadenine.	isoguanine	160-176	mutY DNA glycosylase	Homo sapiens	86-89
11092888-1	2001	The human MutY homolog (hMYH) is a DNA glycosylase involved in the removal of adenines or 2-hydroxyadenines misincorporated with template guanines or 7,8-dihydro-8-oxodeoxyguanines.	Adenine	78-86	mutY DNA glycosylase	Homo sapiens	24-28
11092888-1	2001	The human MutY homolog (hMYH) is a DNA glycosylase involved in the removal of adenines or 2-hydroxyadenines misincorporated with template guanines or 7,8-dihydro-8-oxodeoxyguanines.	isoguanine	90-107	mutY DNA glycosylase	Homo sapiens	24-28
11092888-1	2001	The human MutY homolog (hMYH) is a DNA glycosylase involved in the removal of adenines or 2-hydroxyadenines misincorporated with template guanines or 7,8-dihydro-8-oxodeoxyguanines.	Guanine	138-146	mutY DNA glycosylase	Homo sapiens	24-28
11092888-1	2001	The human MutY homolog (hMYH) is a DNA glycosylase involved in the removal of adenines or 2-hydroxyadenines misincorporated with template guanines or 7,8-dihydro-8-oxodeoxyguanines.	7,8-dihydro-8-oxodeoxyguanines	150-180	mutY DNA glycosylase	Homo sapiens	24-28
11092888-5	2001	A peptide consisting of residues 505-527 of hMYH that contains a conserved PCNA-binding motif binds PCNA, and subsequent amino acid substitution identified Phe-518 and Phe-519 as essential residues required for PCNA binding.	Phenylalanine	156-159	mutY DNA glycosylase	Homo sapiens	44-48
11092888-5	2001	A peptide consisting of residues 505-527 of hMYH that contains a conserved PCNA-binding motif binds PCNA, and subsequent amino acid substitution identified Phe-518 and Phe-519 as essential residues required for PCNA binding.	Phenylalanine	168-171	mutY DNA glycosylase	Homo sapiens	44-48
11160897-5	2001	After removal of adenine by the Myh glycosylase activity, intact AP DNA remains due to lack of an efficient Myh AP lyase activity.	Adenine	17-24	mutY DNA glycosylase	Homo sapiens	32-35
11121482-0	2000	Adenine excisional repair function of MYH protein on the adenine:8-hydroxyguanine base pair in double-stranded DNA.	Adenine	0-7	mutY DNA glycosylase	Homo sapiens	38-41
11121482-0	2000	Adenine excisional repair function of MYH protein on the adenine:8-hydroxyguanine base pair in double-stranded DNA.	Adenine	57-64	mutY DNA glycosylase	Homo sapiens	38-41
11121482-0	2000	Adenine excisional repair function of MYH protein on the adenine:8-hydroxyguanine base pair in double-stranded DNA.	8-hydroxyguanine	65-81	mutY DNA glycosylase	Homo sapiens	38-41
11554292-8	2001	Major substrates of these enzymes, a uracil opposite an adenine for UNG2 and an adenine opposite an 8-oxoguanine for MYH, are formed during DNA replication.	Adenine	56-63	mutY DNA glycosylase	Homo sapiens	117-120
11121482-1	2000	Adenine paired with 8-hydroxyguanine (oh(8)G), a major component of oxidative DNA damage, is excised by MYH base excision repair protein in human cells.	Adenine	0-7	mutY DNA glycosylase	Homo sapiens	104-107
11121482-1	2000	Adenine paired with 8-hydroxyguanine (oh(8)G), a major component of oxidative DNA damage, is excised by MYH base excision repair protein in human cells.	8-hydroxyguanine	20-36	mutY DNA glycosylase	Homo sapiens	104-107
11121482-8	2000	These results indicate that human MYH protein specifically catalyzes the glycosylase reaction on A:oh(8)G under physiological salt concentrations.	Salts	126-130	mutY DNA glycosylase	Homo sapiens	34-37
11554292-8	2001	Major substrates of these enzymes, a uracil opposite an adenine for UNG2 and an adenine opposite an 8-oxoguanine for MYH, are formed during DNA replication.	Adenine	80-87	mutY DNA glycosylase	Homo sapiens	117-120
11554292-8	2001	Major substrates of these enzymes, a uracil opposite an adenine for UNG2 and an adenine opposite an 8-oxoguanine for MYH, are formed during DNA replication.	8-hydroxyguanine	100-112	mutY DNA glycosylase	Homo sapiens	117-120
19394335-1	2009	BACKGROUND & AIMS: MUTYH-associated polyposis (MAP) is an autosomal recessive disorder caused by mutations in the MUTYH gene.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	23-28
10684930-0	2000	Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria.	isoguanine	67-83	mutY DNA glycosylase	Homo sapiens	38-42
19394335-1	2009	BACKGROUND & AIMS: MUTYH-associated polyposis (MAP) is an autosomal recessive disorder caused by mutations in the MUTYH gene.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	118-123
34479993-3	2021	We showed that increased levels of C > A substitutions correlate with copy number loss (CNL) of OGG1 or MUTYH Both genes encode DNA glycosylases that recognize 8-oxo-guanine (8-oxoG) lesions as a first step of 8-oxoG repair.	8-hydroxyguanine	160-173	mutY DNA glycosylase	Homo sapiens	104-109
34970419-4	2021	MUTYH with adenine DNA glycosylase activity excises adenine inserted opposite 8-oxoguanine in DNA.	Adenine	11-18	mutY DNA glycosylase	Homo sapiens	0-5
34970419-4	2021	MUTYH with adenine DNA glycosylase activity excises adenine inserted opposite 8-oxoguanine in DNA.	Adenine	52-59	mutY DNA glycosylase	Homo sapiens	0-5
34970419-4	2021	MUTYH with adenine DNA glycosylase activity excises adenine inserted opposite 8-oxoguanine in DNA.	8-hydroxyguanine	78-90	mutY DNA glycosylase	Homo sapiens	0-5
34086966-5	2021	When 8-oxoG is nevertheless incorporated opposite N6mA, the methylation inhibits N6mA excision from the template (correct) strand by the adenine DNA glycosylase (MYH), implying that the methylation decreases inappropriate misrepair.	8-hydroxyguanine	5-11	mutY DNA glycosylase	Homo sapiens	137-160
34086966-5	2021	When 8-oxoG is nevertheless incorporated opposite N6mA, the methylation inhibits N6mA excision from the template (correct) strand by the adenine DNA glycosylase (MYH), implying that the methylation decreases inappropriate misrepair.	8-hydroxyguanine	5-11	mutY DNA glycosylase	Homo sapiens	162-165
34086966-5	2021	When 8-oxoG is nevertheless incorporated opposite N6mA, the methylation inhibits N6mA excision from the template (correct) strand by the adenine DNA glycosylase (MYH), implying that the methylation decreases inappropriate misrepair.	6-methyladenine	50-54	mutY DNA glycosylase	Homo sapiens	137-160
34086966-5	2021	When 8-oxoG is nevertheless incorporated opposite N6mA, the methylation inhibits N6mA excision from the template (correct) strand by the adenine DNA glycosylase (MYH), implying that the methylation decreases inappropriate misrepair.	6-methyladenine	50-54	mutY DNA glycosylase	Homo sapiens	162-165
34086966-5	2021	When 8-oxoG is nevertheless incorporated opposite N6mA, the methylation inhibits N6mA excision from the template (correct) strand by the adenine DNA glycosylase (MYH), implying that the methylation decreases inappropriate misrepair.	6-methyladenine	81-85	mutY DNA glycosylase	Homo sapiens	137-160
34086966-5	2021	When 8-oxoG is nevertheless incorporated opposite N6mA, the methylation inhibits N6mA excision from the template (correct) strand by the adenine DNA glycosylase (MYH), implying that the methylation decreases inappropriate misrepair.	6-methyladenine	81-85	mutY DNA glycosylase	Homo sapiens	162-165
34479993-3	2021	We showed that increased levels of C > A substitutions correlate with copy number loss (CNL) of OGG1 or MUTYH Both genes encode DNA glycosylases that recognize 8-oxo-guanine (8-oxoG) lesions as a first step of 8-oxoG repair.	8-hydroxyguanine	175-181	mutY DNA glycosylase	Homo sapiens	104-109
34142156-1	2021	Mammalian MutY homologue (MUTYH) is an adenine DNA glycosylase that excises adenine inserted opposite 8-oxoguanine (8-oxoG).	Adenine	39-46	mutY DNA glycosylase	Homo sapiens	26-31
34142156-1	2021	Mammalian MutY homologue (MUTYH) is an adenine DNA glycosylase that excises adenine inserted opposite 8-oxoguanine (8-oxoG).	Adenine	76-83	mutY DNA glycosylase	Homo sapiens	26-31
34142156-1	2021	Mammalian MutY homologue (MUTYH) is an adenine DNA glycosylase that excises adenine inserted opposite 8-oxoguanine (8-oxoG).	8-hydroxyguanine	102-114	mutY DNA glycosylase	Homo sapiens	26-31
34142156-1	2021	Mammalian MutY homologue (MUTYH) is an adenine DNA glycosylase that excises adenine inserted opposite 8-oxoguanine (8-oxoG).	8-hydroxyguanine	116-122	mutY DNA glycosylase	Homo sapiens	26-31
34142156-4	2021	It is also reported that MUTYH has a Zn-binding motif in a unique interdomain connector (IDC) region, which interacts with Rad9-Rad1-Hus1 complex (9-1-1) in DNA damage response, and with apurinic/apyrimidinic endonuclease 1 (APE1) in BER.	Zinc	37-39	mutY DNA glycosylase	Homo sapiens	25-30
34142156-9	2021	The IDC, including the Zn-binding motif, is exposed on the MUTYH surface, suggesting its interaction modes with 9-1-1 and APE1, respectively.	Zinc	23-25	mutY DNA glycosylase	Homo sapiens	59-64
33574380-10	2021	These findings suggest that MUTYH deficiency is associated with hepatocarcinogenesis in patients with NASH with hepatic iron accumulation.	Iron	120-124	mutY DNA glycosylase	Homo sapiens	28-33
35098839-0	2022	Mutyh deficiency downregulates mitochondrial fusion proteins and causes cardiac dysfunction via alpha-ketoglutaric acid reduction with oxidative stress.	Ketoglutaric Acids	96-119	mutY DNA glycosylase	Homo sapiens	0-5
35098839-1	2022	MutY homolog (MUTYH), an important protein in base excision repair (BER) system, excises adenine in the nascent strand opposite 8-oxoguanine in template DNA and restores G:C base-pair to maintain the fidelity of DNA replication.	Adenine	89-96	mutY DNA glycosylase	Homo sapiens	14-19
35098839-1	2022	MutY homolog (MUTYH), an important protein in base excision repair (BER) system, excises adenine in the nascent strand opposite 8-oxoguanine in template DNA and restores G:C base-pair to maintain the fidelity of DNA replication.	8-hydroxyguanine	128-140	mutY DNA glycosylase	Homo sapiens	14-19
35098839-3	2022	Here we demonstrate that Mutyh deficiency alters mitochondrial structure and impairs mitochondrial function through downregulation of mitochondrial fusion protein Mfn2 and alteration of the ratio of L-Opa1/S-Opa1 accompanied by reduction of alpha-ketoglutaric acid (alpha-KG) under oxidative stress condition.	Ketoglutaric Acids	241-264	mutY DNA glycosylase	Homo sapiens	25-30
35098839-3	2022	Here we demonstrate that Mutyh deficiency alters mitochondrial structure and impairs mitochondrial function through downregulation of mitochondrial fusion protein Mfn2 and alteration of the ratio of L-Opa1/S-Opa1 accompanied by reduction of alpha-ketoglutaric acid (alpha-KG) under oxidative stress condition.	Ketoglutaric Acids	266-274	mutY DNA glycosylase	Homo sapiens	25-30
32991318-1	2020	In the base excision repair pathway, MYH/MUTYH DNA glycosylase prevents mutations by removing adenine mispaired with 8-oxoG, a frequent oxidative lesion.	Adenine	94-101	mutY DNA glycosylase	Homo sapiens	37-40
33145410-0	2020	Designer Fluorescent Adenines Enable Real-Time Monitoring of MUTYH Activity.	Adenine	21-29	mutY DNA glycosylase	Homo sapiens	61-66
33145410-1	2020	The human DNA base excision repair enzyme MUTYH (MutY homolog DNA glycosylase) excises undamaged adenine that has been misincorporated opposite the oxidatively damaged 8-oxoG, preventing transversion mutations and serving as an important defense against the deleterious effects of this damage.	Adenine	97-104	mutY DNA glycosylase	Homo sapiens	42-47
33145410-5	2020	Herein, we synthesize and identify novel fluorescent adenine derivatives that can act as direct substrates for excision by MUTYH as well as bacterial MutY.	Adenine	53-60	mutY DNA glycosylase	Homo sapiens	123-128
32991318-1	2020	In the base excision repair pathway, MYH/MUTYH DNA glycosylase prevents mutations by removing adenine mispaired with 8-oxoG, a frequent oxidative lesion.	Adenine	94-101	mutY DNA glycosylase	Homo sapiens	41-46
32991318-8	2020	The formation of MYH/SIRT6/9-1-1 complex is of biological significance as interrupting their interactions can increase cell"s sensitivity to H2O2 and/or elevate cellular 8-oxoG levels after H2O2 treatment.	Hydrogen Peroxide	141-145	mutY DNA glycosylase	Homo sapiens	17-20
32991318-8	2020	The formation of MYH/SIRT6/9-1-1 complex is of biological significance as interrupting their interactions can increase cell"s sensitivity to H2O2 and/or elevate cellular 8-oxoG levels after H2O2 treatment.	Hydrogen Peroxide	190-194	mutY DNA glycosylase	Homo sapiens	17-20
32821650-1	2020	MUTYH is a base excision repair enzyme, it plays a crucial role in the correction of DNA errors from guanine oxidation and may be considered a cell protective factor.	Guanine	101-108	mutY DNA glycosylase	Homo sapiens	0-5
33024574-5	2020	We postulate that monoallelic MUTYH mutations may manifest in the presence of cooperative non-genetic mechanisms, in this case possibly magnesium deficiency from Gitelman syndrome.	Magnesium	136-145	mutY DNA glycosylase	Homo sapiens	30-35
32664726-0	2020	Detection of OG:A lesion mispairs by MutY relies on a single His residue and the 2-amino group of 8-oxoguanine.	Histidine	61-64	mutY DNA glycosylase	Homo sapiens	37-41
32664726-0	2020	Detection of OG:A lesion mispairs by MutY relies on a single His residue and the 2-amino group of 8-oxoguanine.	8-hydroxyguanine	98-110	mutY DNA glycosylase	Homo sapiens	37-41
32664726-1	2020	MutY glycosylase excises adenines misincorporated opposite the oxidatively damaged lesion, 8-oxo-7,8-dihydroguanine (OG), to initiate base excision repair and prevent G to T transversion mutations.	Adenine	25-33	mutY DNA glycosylase	Homo sapiens	0-4
32664726-1	2020	MutY glycosylase excises adenines misincorporated opposite the oxidatively damaged lesion, 8-oxo-7,8-dihydroguanine (OG), to initiate base excision repair and prevent G to T transversion mutations.	8-hydroxyguanine	91-115	mutY DNA glycosylase	Homo sapiens	0-4
32664726-1	2020	MutY glycosylase excises adenines misincorporated opposite the oxidatively damaged lesion, 8-oxo-7,8-dihydroguanine (OG), to initiate base excision repair and prevent G to T transversion mutations.	8-hydroxyguanine	117-119	mutY DNA glycosylase	Homo sapiens	0-4
32664726-3	2020	Herein we use a combination of in vitro and bacterial cell repair assays with single molecule fluorescence microscopy to demonstrate that both a C-terminal domain histidine residue and the 2-amino group of OG base are critical for MutY detection of OG:A sites.	Histidine	163-172	mutY DNA glycosylase	Homo sapiens	231-235
32821650-2	2020	In humans it is an adenine DNA glycosylase that removes adenine misincorporated in 7,8-dihydro-8-oxoguanine (8-oxoG) pairs, inducing G:C to T:A transversions.	7,8-dihydro-8-oxoguanine	83-107	mutY DNA glycosylase	Homo sapiens	19-42
32821650-2	2020	In humans it is an adenine DNA glycosylase that removes adenine misincorporated in 7,8-dihydro-8-oxoguanine (8-oxoG) pairs, inducing G:C to T:A transversions.	7,8-dihydro-8-oxoguanine	109-115	mutY DNA glycosylase	Homo sapiens	19-42
32821650-3	2020	MUTYH functionally cooperates with OGG1 that eliminates 8-oxodG derived from excessive reactive oxygen species production.	8-ohdg	56-63	mutY DNA glycosylase	Homo sapiens	0-5
32821650-3	2020	MUTYH functionally cooperates with OGG1 that eliminates 8-oxodG derived from excessive reactive oxygen species production.	Reactive Oxygen Species	87-110	mutY DNA glycosylase	Homo sapiens	0-5
31875995-9	2020	DNA repair proteins (OGG1, Ape-1, and MyH) involved in the base excision repair pathway, as well as p53 protein levels were down-regulated in all of the bisphenol-exposed groups.	bis(4-hydroxyphenyl)sulfone	153-162	mutY DNA glycosylase	Homo sapiens	38-41
32183600-5	2020	Multiple distinct mechanisms work together to decrease the genomic level of 8-OHdG through the enzymatic activities of Mutyh, Ogg1 and Mth1.	8-ohdg	76-82	mutY DNA glycosylase	Homo sapiens	119-124
32001618-0	2020	The DNA repair enzyme MUTYH potentiates cytotoxicity of the alkylating agent MNNG by interacting with abasic sites.	Methylnitronitrosoguanidine	77-81	mutY DNA glycosylase	Homo sapiens	22-27
32001618-1	2020	Higher expression of the human DNA repair enzyme MUTYH has previously been shown to be strongly associated with reduced survival in a panel of 24 human lymphoblastoid cell lines exposed to the alkylating agent N-methyl-N"-nitro-N-nitrosoguanidine (MNNG).	Methylnitronitrosoguanidine	210-246	mutY DNA glycosylase	Homo sapiens	49-54
32001618-1	2020	Higher expression of the human DNA repair enzyme MUTYH has previously been shown to be strongly associated with reduced survival in a panel of 24 human lymphoblastoid cell lines exposed to the alkylating agent N-methyl-N"-nitro-N-nitrosoguanidine (MNNG).	Methylnitronitrosoguanidine	248-252	mutY DNA glycosylase	Homo sapiens	49-54
32001618-2	2020	The molecular mechanism of MUTYH-enhanced MNNG cytotoxicity is unclear, since MUTYH has a well-established role in the repair of oxidative DNA lesions.	Methylnitronitrosoguanidine	42-46	mutY DNA glycosylase	Homo sapiens	27-32
32059490-3	2020	Within clustered DNA lesions, they pose a serious problem for repair proteins, especially for iron-sulfur glycosylases (MutyH), which can recognize them by the electron-transfer process.	Sulfur	94-105	mutY DNA glycosylase	Homo sapiens	120-125
32085439-15	2020	Consequently, SUMO3, ALC1, POLE4, PCBP4, MUTYH expression correlated with the higher RBE of carbon ions.	Carbon	92-98	mutY DNA glycosylase	Homo sapiens	41-46
32072083-2	2019	Faulty MUTYH protein activity causes the accumulation of G T transversions due to unrepaired 8-oxoG:A mismatches.	5-hydroxy-8-oxo-7,8-dihydroguanosine	93-99	mutY DNA glycosylase	Homo sapiens	7-12
31285513-3	2019	Certainly, it is known that APC and MUTYH are high penetrance predisposition genes for adenomatous polyposis, but they only account for 5-10% of AAP.	aap	145-148	mutY DNA glycosylase	Homo sapiens	36-41
31578574-0	2019	Downregulation of MUTYH contributes to cisplatin-resistance of esophageal squamous cell carcinoma cells by promoting Twist-mediated EMT.	Cisplatin	39-48	mutY DNA glycosylase	Homo sapiens	18-23
31578574-3	2019	In the present study, a CDDP-resistant ESCC cell line EC109/CDDP was established by culturing parental EC109 cells in increasing concentrations of CDDP, and it was demonstrated that MutY homolog (MUTYH), a critical base excision repair gene, was significantly downregulated in the resistant EC109/CDDP cells compared with that noted in the parental cells.	Cisplatin	24-28	mutY DNA glycosylase	Homo sapiens	196-201
31578574-3	2019	In the present study, a CDDP-resistant ESCC cell line EC109/CDDP was established by culturing parental EC109 cells in increasing concentrations of CDDP, and it was demonstrated that MutY homolog (MUTYH), a critical base excision repair gene, was significantly downregulated in the resistant EC109/CDDP cells compared with that noted in the parental cells.	Cisplatin	60-64	mutY DNA glycosylase	Homo sapiens	196-201
31578574-3	2019	In the present study, a CDDP-resistant ESCC cell line EC109/CDDP was established by culturing parental EC109 cells in increasing concentrations of CDDP, and it was demonstrated that MutY homolog (MUTYH), a critical base excision repair gene, was significantly downregulated in the resistant EC109/CDDP cells compared with that noted in the parental cells.	Cisplatin	60-64	mutY DNA glycosylase	Homo sapiens	196-201
31578574-3	2019	In the present study, a CDDP-resistant ESCC cell line EC109/CDDP was established by culturing parental EC109 cells in increasing concentrations of CDDP, and it was demonstrated that MutY homolog (MUTYH), a critical base excision repair gene, was significantly downregulated in the resistant EC109/CDDP cells compared with that noted in the parental cells.	Cisplatin	60-64	mutY DNA glycosylase	Homo sapiens	196-201
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	107-111	mutY DNA glycosylase	Homo sapiens	22-27
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	107-111	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	107-111	mutY DNA glycosylase	Homo sapiens	66-71
29209987-0	2019	Genetic Investigation of Polymorphic OGG1 and MUTYH Genes Towards Increased Susceptibility in Lung Adenocarcinoma and its Impact on Overall Survival of Lung Cancer Patients Treated with Platinum Based Chemotherapy.	Platinum	186-194	mutY DNA glycosylase	Homo sapiens	46-51
29209987-3	2019	MUTYH complements OGG1 as it particularly remove adenine mispaired with 8-oxo-G.	Adenine	49-56	mutY DNA glycosylase	Homo sapiens	0-5
29209987-3	2019	MUTYH complements OGG1 as it particularly remove adenine mispaired with 8-oxo-G.	8-oxo-g	72-79	mutY DNA glycosylase	Homo sapiens	0-5
31203172-1	2019	MUTYH is a base-excision repair glycosylase that removes adenine opposite 8-oxoguanine (OG).	Adenine	57-64	mutY DNA glycosylase	Homo sapiens	0-5
31203172-1	2019	MUTYH is a base-excision repair glycosylase that removes adenine opposite 8-oxoguanine (OG).	8-hydroxyguanine	74-86	mutY DNA glycosylase	Homo sapiens	0-5
31203172-1	2019	MUTYH is a base-excision repair glycosylase that removes adenine opposite 8-oxoguanine (OG).	8-hydroxyguanine	88-90	mutY DNA glycosylase	Homo sapiens	0-5
31203172-7	2019	Studies that suggest MUTYH inhibits the repair of alkyl-DNA damage and cyclopyrimidine dimers (CPDs) is reviewed, and evidence of a synthetic lethal interaction with mismatch repair (MMR) is summarized.	cyclopyrimidine	71-86	mutY DNA glycosylase	Homo sapiens	21-26
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	107-111	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	107-111	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	22-27
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	monooxyethylene trimethylolpropane tristearate	347-350	mutY DNA glycosylase	Homo sapiens	22-27
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	monooxyethylene trimethylolpropane tristearate	347-350	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	monooxyethylene trimethylolpropane tristearate	347-350	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	monooxyethylene trimethylolpropane tristearate	347-350	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	monooxyethylene trimethylolpropane tristearate	347-350	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	22-27
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	66-71
31578574-4	2019	Ectopic expression of MUTYH by transient transfection of pcDNA3.1-MUTYH plasmid significantly enhanced the CDDP-mediated inhibitory effect on resistant cell proliferation and induction of apoptosis, while silencing of MUTYH by transiently transfecting MUTYH-targeted siRNA in parental cells led to decreased sensitivity to CDDP as demonstrated by MTT assay, suggesting the crucial involvement of MUTYH in CDDP resistance.	Cisplatin	323-327	mutY DNA glycosylase	Homo sapiens	66-71
31578574-5	2019	Further experiments demonstrated that the CDDP-resistant cells went through epithelial-mesenchymal transition (EMT) driven by its master regulator Twist, and MUTYH overexpression significantly reduced the Twist expression level and reversed the phenotype of EMT as detected by western blot analysis and RT-qPCR assays, suggesting that downregulation of MUTYH contributed to the Twist-mediated EMT.	Cisplatin	42-46	mutY DNA glycosylase	Homo sapiens	158-163
31578574-5	2019	Further experiments demonstrated that the CDDP-resistant cells went through epithelial-mesenchymal transition (EMT) driven by its master regulator Twist, and MUTYH overexpression significantly reduced the Twist expression level and reversed the phenotype of EMT as detected by western blot analysis and RT-qPCR assays, suggesting that downregulation of MUTYH contributed to the Twist-mediated EMT.	Cisplatin	42-46	mutY DNA glycosylase	Homo sapiens	353-358
31578574-7	2019	MUTYH acted as a positive regulator of reactive oxygen species (ROS) that showed a low level in resistant cells via flow cytometry assay, as demonstrated by increased ROS production in response to MUTYH overexpression.	Reactive Oxygen Species	39-62	mutY DNA glycosylase	Homo sapiens	0-5
31578574-7	2019	MUTYH acted as a positive regulator of reactive oxygen species (ROS) that showed a low level in resistant cells via flow cytometry assay, as demonstrated by increased ROS production in response to MUTYH overexpression.	Reactive Oxygen Species	39-62	mutY DNA glycosylase	Homo sapiens	197-202
31578574-7	2019	MUTYH acted as a positive regulator of reactive oxygen species (ROS) that showed a low level in resistant cells via flow cytometry assay, as demonstrated by increased ROS production in response to MUTYH overexpression.	Reactive Oxygen Species	64-67	mutY DNA glycosylase	Homo sapiens	0-5
31578574-7	2019	MUTYH acted as a positive regulator of reactive oxygen species (ROS) that showed a low level in resistant cells via flow cytometry assay, as demonstrated by increased ROS production in response to MUTYH overexpression.	Reactive Oxygen Species	64-67	mutY DNA glycosylase	Homo sapiens	197-202
31578574-7	2019	MUTYH acted as a positive regulator of reactive oxygen species (ROS) that showed a low level in resistant cells via flow cytometry assay, as demonstrated by increased ROS production in response to MUTYH overexpression.	Reactive Oxygen Species	167-170	mutY DNA glycosylase	Homo sapiens	0-5
31578574-7	2019	MUTYH acted as a positive regulator of reactive oxygen species (ROS) that showed a low level in resistant cells via flow cytometry assay, as demonstrated by increased ROS production in response to MUTYH overexpression.	Reactive Oxygen Species	167-170	mutY DNA glycosylase	Homo sapiens	197-202
31578574-9	2019	In conclusion, the present data demonstrated that EMT activation mediated by MUTYH downregulation, by both enhancing Twist transcription and blocking its degradation, is one of the mechanisms for acquisition of CDDP resistance in ESCC.	Cisplatin	211-215	mutY DNA glycosylase	Homo sapiens	77-82
31207142-6	2019	The family based evaluation of the variants showed that the variant, c.714T > G (p.Tyr238Ter), in the CLEC7A gene in first family; the variant, c.55C > T (p.Arg19Ter), in the APOC3 gene and the variant, c.1171C > T (p.Gln391Ter), in the MUTYH gene in second family; and the variant, c.211G > A (p.Gly71Arg), in the UGT1A1 gene in the third family, were found statistically significant (p < 0.05).	arg19ter	157-165	mutY DNA glycosylase	Homo sapiens	237-242
30208271-0	2018	The Zinc Linchpin Motif in the DNA Repair Glycosylase MUTYH: Identifying the Zn2+ Ligands and Roles in Damage Recognition and Repair.	Zinc	77-81	mutY DNA glycosylase	Homo sapiens	54-59
31027119-8	2019	These findings clearly highlight associations between the MUTYH Gln324His (CAG/CAC) polymorphism and susceptibility to CSCC, HR-HPV infection and specific prognostic factors, supporting the utility of this variant as an early indicator for patients at high risk of cervical carcinoma.	GUANOSINE 5'-TRIPHOSPHATE P3-[1-(2-NITROPHENYL)ETHYL ESTER]	75-78	mutY DNA glycosylase	Homo sapiens	58-63
30208271-1	2018	The DNA base excision repair (BER) glycosylase MUTYH prevents DNA mutations by catalyzing adenine (A) excision from inappropriately formed 8-oxoguanine (8-oxoG):A mismatches.	Adenine	90-97	mutY DNA glycosylase	Homo sapiens	47-52
30208271-1	2018	The DNA base excision repair (BER) glycosylase MUTYH prevents DNA mutations by catalyzing adenine (A) excision from inappropriately formed 8-oxoguanine (8-oxoG):A mismatches.	8-hydroxyguanine	139-151	mutY DNA glycosylase	Homo sapiens	47-52
30208271-1	2018	The DNA base excision repair (BER) glycosylase MUTYH prevents DNA mutations by catalyzing adenine (A) excision from inappropriately formed 8-oxoguanine (8-oxoG):A mismatches.	8-hydroxyguanine	153-159	mutY DNA glycosylase	Homo sapiens	47-52
30208271-4	2018	One of these cofactors, found in nearly all MUTYH orthologs, is a [4Fe-4S]2+ cluster coordinated by four Cys residues located in the N-terminal catalytic domain.	Cysteine	105-108	mutY DNA glycosylase	Homo sapiens	44-49
30208271-5	2018	We recently uncovered a second functionally relevant metal cofactor site present only in higher eukaryotic MUTYH orthologs: a Zn2+ ion coordinated by three Cys residues located within the extended interdomain connector (IDC) region of MUTYH that connects the N-terminal adenine excision and C-terminal 8-oxoG recognition domains.	Metals	53-58	mutY DNA glycosylase	Homo sapiens	107-112
30208271-5	2018	We recently uncovered a second functionally relevant metal cofactor site present only in higher eukaryotic MUTYH orthologs: a Zn2+ ion coordinated by three Cys residues located within the extended interdomain connector (IDC) region of MUTYH that connects the N-terminal adenine excision and C-terminal 8-oxoG recognition domains.	Metals	53-58	mutY DNA glycosylase	Homo sapiens	235-240
30208271-5	2018	We recently uncovered a second functionally relevant metal cofactor site present only in higher eukaryotic MUTYH orthologs: a Zn2+ ion coordinated by three Cys residues located within the extended interdomain connector (IDC) region of MUTYH that connects the N-terminal adenine excision and C-terminal 8-oxoG recognition domains.	Zinc	126-130	mutY DNA glycosylase	Homo sapiens	107-112
30208271-5	2018	We recently uncovered a second functionally relevant metal cofactor site present only in higher eukaryotic MUTYH orthologs: a Zn2+ ion coordinated by three Cys residues located within the extended interdomain connector (IDC) region of MUTYH that connects the N-terminal adenine excision and C-terminal 8-oxoG recognition domains.	Zinc	126-130	mutY DNA glycosylase	Homo sapiens	235-240
30208271-5	2018	We recently uncovered a second functionally relevant metal cofactor site present only in higher eukaryotic MUTYH orthologs: a Zn2+ ion coordinated by three Cys residues located within the extended interdomain connector (IDC) region of MUTYH that connects the N-terminal adenine excision and C-terminal 8-oxoG recognition domains.	Cysteine	156-159	mutY DNA glycosylase	Homo sapiens	107-112
30208271-5	2018	We recently uncovered a second functionally relevant metal cofactor site present only in higher eukaryotic MUTYH orthologs: a Zn2+ ion coordinated by three Cys residues located within the extended interdomain connector (IDC) region of MUTYH that connects the N-terminal adenine excision and C-terminal 8-oxoG recognition domains.	Cysteine	156-159	mutY DNA glycosylase	Homo sapiens	235-240
30208271-5	2018	We recently uncovered a second functionally relevant metal cofactor site present only in higher eukaryotic MUTYH orthologs: a Zn2+ ion coordinated by three Cys residues located within the extended interdomain connector (IDC) region of MUTYH that connects the N-terminal adenine excision and C-terminal 8-oxoG recognition domains.	Adenine	270-277	mutY DNA glycosylase	Homo sapiens	107-112
30208271-5	2018	We recently uncovered a second functionally relevant metal cofactor site present only in higher eukaryotic MUTYH orthologs: a Zn2+ ion coordinated by three Cys residues located within the extended interdomain connector (IDC) region of MUTYH that connects the N-terminal adenine excision and C-terminal 8-oxoG recognition domains.	Adenine	270-277	mutY DNA glycosylase	Homo sapiens	235-240
29915346-1	2018	The human DNA repair enzyme MUTYH excises mispaired adenine residues in oxidized DNA.	Adenine	52-59	mutY DNA glycosylase	Homo sapiens	28-33
29923053-7	2018	MTS assays showed that knockdown of DNA repair genes LIG1, POLD1, PNKP, RAD54L and MUTYH significantly inhibited recovery in response to temozolomide when compared with control group (p &lt; 0.001).	Temozolomide	137-149	mutY DNA glycosylase	Homo sapiens	83-88
29915346-3	2018	We report a MUTYH variant, p.C306W (c.918C&gt;G), with a tryptophan residue in place of native cysteine, that ligates the [4Fe4S] cluster in a patient with colonic polyposis and family history of early age colon cancer.	Tryptophan	57-67	mutY DNA glycosylase	Homo sapiens	12-17
29915346-3	2018	We report a MUTYH variant, p.C306W (c.918C&gt;G), with a tryptophan residue in place of native cysteine, that ligates the [4Fe4S] cluster in a patient with colonic polyposis and family history of early age colon cancer.	Cysteine	95-103	mutY DNA glycosylase	Homo sapiens	12-17
30008864-1	2018	Oxidative stress, demonstrated by an accumulation of 8-hydroxy-2"-deoxyguanosine (8-OHdG), results in DNA damage, which is normally repaired by base excision repair enzymes including 8-OHdG DNA glycosylase (OGG1) and human MutY homolog (MUTYH), in addition to nucleotide pool sanitizing enzymes including MutT Homolog 1 (MTH1).	8-ohdg	53-80	mutY DNA glycosylase	Homo sapiens	237-242
30008864-1	2018	Oxidative stress, demonstrated by an accumulation of 8-hydroxy-2"-deoxyguanosine (8-OHdG), results in DNA damage, which is normally repaired by base excision repair enzymes including 8-OHdG DNA glycosylase (OGG1) and human MutY homolog (MUTYH), in addition to nucleotide pool sanitizing enzymes including MutT Homolog 1 (MTH1).	8-ohdg	82-88	mutY DNA glycosylase	Homo sapiens	237-242
30008864-1	2018	Oxidative stress, demonstrated by an accumulation of 8-hydroxy-2"-deoxyguanosine (8-OHdG), results in DNA damage, which is normally repaired by base excision repair enzymes including 8-OHdG DNA glycosylase (OGG1) and human MutY homolog (MUTYH), in addition to nucleotide pool sanitizing enzymes including MutT Homolog 1 (MTH1).	8-ohdg	183-189	mutY DNA glycosylase	Homo sapiens	237-242
28665322-4	2017	In 8-oxo-G:A mispairs generated by the incorporation of A opposite unrepaired 8-oxo-G, A is removed by MutYH (MYH) for post-replicative repair, and other oxidized base lesions must be repaired prior to replication in order to prevent mutation fixation.	8-oxo-	3-9	mutY DNA glycosylase	Homo sapiens	103-108
29746250-0	2018	Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs.	Iron	33-37	mutY DNA glycosylase	Homo sapiens	90-95
29746250-1	2018	Many DNA repair enzymes, including the human adenine glycosylase MUTYH, require iron-sulfur (Fe-S) cluster cofactors for DNA damage recognition and subsequent repair.	ferrous sulfide	80-91	mutY DNA glycosylase	Homo sapiens	65-70
29746250-1	2018	Many DNA repair enzymes, including the human adenine glycosylase MUTYH, require iron-sulfur (Fe-S) cluster cofactors for DNA damage recognition and subsequent repair.	Iron	93-97	mutY DNA glycosylase	Homo sapiens	65-70
29746250-2	2018	MUTYH prokaryotic and eukaryotic homologs are a family of adenine (A) glycosylases that cleave A when mispaired with the oxidatively damaged guanine lesion, 8-oxo-7,8-dihydroguanine (OG).	Adenine	58-65	mutY DNA glycosylase	Homo sapiens	0-5
29746250-2	2018	MUTYH prokaryotic and eukaryotic homologs are a family of adenine (A) glycosylases that cleave A when mispaired with the oxidatively damaged guanine lesion, 8-oxo-7,8-dihydroguanine (OG).	Guanine	141-148	mutY DNA glycosylase	Homo sapiens	0-5
29746250-2	2018	MUTYH prokaryotic and eukaryotic homologs are a family of adenine (A) glycosylases that cleave A when mispaired with the oxidatively damaged guanine lesion, 8-oxo-7,8-dihydroguanine (OG).	8-hydroxyguanine	157-181	mutY DNA glycosylase	Homo sapiens	0-5
29149600-6	2017	Acetohexamide exerted this protective function by antagonizing expression of the DNA glycosylase, MUTYH.	Acetohexamide	0-13	mutY DNA glycosylase	Homo sapiens	98-103
29746241-4	2018	However, in the two decades subsequent to the initial discovery, purification and in vitro analysis of bacterial MutYs and mammalian homologs, such as human MUTYH and mouse Mutyh, have demonstrated that proper Fe-S cluster coordination is required for OG:A substrate recognition and adenine excision.	Iron	210-214	mutY DNA glycosylase	Homo sapiens	157-162
29746241-4	2018	However, in the two decades subsequent to the initial discovery, purification and in vitro analysis of bacterial MutYs and mammalian homologs, such as human MUTYH and mouse Mutyh, have demonstrated that proper Fe-S cluster coordination is required for OG:A substrate recognition and adenine excision.	Adenine	283-290	mutY DNA glycosylase	Homo sapiens	157-162
29746241-8	2018	The methods described herein have not only been leveraged to provide insight into the roles of the MutY Fe-S cluster but have also been provided crucial information needed to delineate the impact of inherited variants of the human homolog MUTYH associated with a colorectal cancer syndrome known as MUTYH-associated polyposis or MAP.	Iron	104-108	mutY DNA glycosylase	Homo sapiens	239-244
29746241-9	2018	Notably, many MAP-associated variants have been found adjacent to the Fe-S cluster further underscoring the intimate relationship between the cofactor, MUTYH-mediated DNA repair, and disease.	Iron	70-74	mutY DNA glycosylase	Homo sapiens	152-157
28665322-4	2017	In 8-oxo-G:A mispairs generated by the incorporation of A opposite unrepaired 8-oxo-G, A is removed by MutYH (MYH) for post-replicative repair, and other oxidized base lesions must be repaired prior to replication in order to prevent mutation fixation.	8-oxo-	3-9	mutY DNA glycosylase	Homo sapiens	110-113
28665322-4	2017	In 8-oxo-G:A mispairs generated by the incorporation of A opposite unrepaired 8-oxo-G, A is removed by MutYH (MYH) for post-replicative repair, and other oxidized base lesions must be repaired prior to replication in order to prevent mutation fixation.	oxo	5-8	mutY DNA glycosylase	Homo sapiens	103-108
28665322-4	2017	In 8-oxo-G:A mispairs generated by the incorporation of A opposite unrepaired 8-oxo-G, A is removed by MutYH (MYH) for post-replicative repair, and other oxidized base lesions must be repaired prior to replication in order to prevent mutation fixation.	oxo	5-8	mutY DNA glycosylase	Homo sapiens	110-113
27890638-6	2017	Mismatch-specific adenine- and thymine-DNA glycosylases (MutY/MUTYH and TDG/MBD4, respectively) initiated BER and mismatch repair (MMR) pathways can recognize and remove normal DNA bases in mismatched DNA duplexes.	Adenine	18-25	mutY DNA glycosylase	Homo sapiens	62-67
28551381-2	2017	When operating normally, the MUTYH DNA glycosylase prevents 8-oxoguanine-related mutagenesis by excising the incorporated adenine.	Adenine	122-129	mutY DNA glycosylase	Homo sapiens	29-34
28551381-2	2017	When operating normally, the MUTYH DNA glycosylase prevents 8-oxoguanine-related mutagenesis by excising the incorporated adenine.	8-hydroxyguanine	60-72	mutY DNA glycosylase	Homo sapiens	29-34
28087410-2	2017	8-Oxo-7,8-dihydroguanine (8-oxoG) is one of the most prevalent DNA lesions formed by RONS and is repaired through the base excision repair (BER) pathway involving the DNA repair glycosylases OGG1 and MUTYH in eukaryotes.	8-hydroxyguanine	0-24	mutY DNA glycosylase	Homo sapiens	200-205
27890638-6	2017	Mismatch-specific adenine- and thymine-DNA glycosylases (MutY/MUTYH and TDG/MBD4, respectively) initiated BER and mismatch repair (MMR) pathways can recognize and remove normal DNA bases in mismatched DNA duplexes.	Thymine	31-38	mutY DNA glycosylase	Homo sapiens	62-67
28087410-2	2017	8-Oxo-7,8-dihydroguanine (8-oxoG) is one of the most prevalent DNA lesions formed by RONS and is repaired through the base excision repair (BER) pathway involving the DNA repair glycosylases OGG1 and MUTYH in eukaryotes.	8-hydroxyguanine	26-32	mutY DNA glycosylase	Homo sapiens	200-205
28340109-3	2017	The MYH and MTH1 genes play important roles in preventing mutations induced by 8-hydroxy-guanine, which is an oxidised product of guanine.	8-hydroxyguanine	79-96	mutY DNA glycosylase	Homo sapiens	4-7
28087410-3	2017	MUTYH removes adenine (A) from 8-oxoG:A mispairs, thus mitigating the potential of G:C to T:A transversion mutations from occurring in the genome.	Adenine	14-21	mutY DNA glycosylase	Homo sapiens	0-5
28340109-3	2017	The MYH and MTH1 genes play important roles in preventing mutations induced by 8-hydroxy-guanine, which is an oxidised product of guanine.	Guanine	89-96	mutY DNA glycosylase	Homo sapiens	4-7
28340109-10	2017	MTH1 together with MYH plays an important role in protection against mutations induced by modified dNTPs during chronic oxidative stress.	dntps	99-104	mutY DNA glycosylase	Homo sapiens	19-22
29098062-4	2017	We found that both the SMUG1 protein and the TDG protein exhibit DNA glycosylase activity against thymine mispaired with 8BrG and that the MUTYH protein exhibits DNA glycosylase activity against adenine mispaired with 8BrG.	8-bromoguanine	121-125	mutY DNA glycosylase	Homo sapiens	139-144
27253753-1	2017	8-Hydroxyguanine (8OHG), a major oxidative DNA lesion, is known to accumulate in prostate cancer; however, the status of one of its repair enzymes, MUTYH, in prostate cancer remains to be elucidated.	8-hydroxyguanine	0-16	mutY DNA glycosylase	Homo sapiens	148-153
27253753-6	2017	Both the capacities to cleave DNA containing adenine:8OHG mispairs and to suppress mutations caused by 8OHG were significantly lower in prostatic cell lines with lower MUTYH expression than in prostatic cell lines with higher MUTYH expression.	Adenine	45-52	mutY DNA glycosylase	Homo sapiens	168-173
27253753-6	2017	Both the capacities to cleave DNA containing adenine:8OHG mispairs and to suppress mutations caused by 8OHG were significantly lower in prostatic cell lines with lower MUTYH expression than in prostatic cell lines with higher MUTYH expression.	8ohg	53-57	mutY DNA glycosylase	Homo sapiens	168-173
27253753-6	2017	Both the capacities to cleave DNA containing adenine:8OHG mispairs and to suppress mutations caused by 8OHG were significantly lower in prostatic cell lines with lower MUTYH expression than in prostatic cell lines with higher MUTYH expression.	8ohg	103-107	mutY DNA glycosylase	Homo sapiens	168-173
28141798-1	2017	BACKGROUND: A compromised base excision repair (BER) promotes carcinogenesis by accumulating oxidative DNA-damaged products as observed in MUTYH-associated polyposis, a hereditary colorectal cancer syndrome marked by adenomas and cancers with an accumulation of 8-oxoguanine.	8-hydroxyguanine	262-274	mutY DNA glycosylase	Homo sapiens	139-144
29098062-4	2017	We found that both the SMUG1 protein and the TDG protein exhibit DNA glycosylase activity against thymine mispaired with 8BrG and that the MUTYH protein exhibits DNA glycosylase activity against adenine mispaired with 8BrG.	Adenine	195-202	mutY DNA glycosylase	Homo sapiens	139-144
29098062-4	2017	We found that both the SMUG1 protein and the TDG protein exhibit DNA glycosylase activity against thymine mispaired with 8BrG and that the MUTYH protein exhibits DNA glycosylase activity against adenine mispaired with 8BrG.	8-bromoguanine	218-222	mutY DNA glycosylase	Homo sapiens	139-144
27481934-2	2016	In order to maintain genomic integrity, post-replicative 8-oxo-dG:dA mispairs are removed through DNA polymerase lambda (Pol lambda)-dependent MUTYH-initiated base excision repair (BER).	8-ohdg	57-65	mutY DNA glycosylase	Homo sapiens	143-148
27918552-9	2016	NEIL1 DNA glycosylase, involved in repair of oxidized nucleosides, was found to be significantly downregulated as a cellular response to MTH1-MYH co-suppression.	Nucleosides	54-65	mutY DNA glycosylase	Homo sapiens	142-145
26905905-1	2016	BACKGROUND &amp; AIMS: MUTYH-associated polyposis (MAP) is similar to familial adenomatous polyposis (FAP), in that it increases the risk for duodenal adenomas and cancer.	Adenosine Monophosphate	12-15	mutY DNA glycosylase	Homo sapiens	23-28
26377631-1	2015	MUTYH is a base excision repair (BER) enzyme that prevents mutations in DNA associated with 8-oxoguanine (OG) by catalyzing the removal of adenine from inappropriately formed OG:A base-pairs.	8-hydroxyguanine	92-104	mutY DNA glycosylase	Homo sapiens	0-5
26673696-1	2016	MutY adenine glycosylases prevent DNA mutations by excising adenine from promutagenic 8-oxo-7,8-dihydroguanine (OG):A mismatches.	Adenine	5-12	mutY DNA glycosylase	Homo sapiens	0-4
26673696-1	2016	MutY adenine glycosylases prevent DNA mutations by excising adenine from promutagenic 8-oxo-7,8-dihydroguanine (OG):A mismatches.	8-hydroxyguanine	86-110	mutY DNA glycosylase	Homo sapiens	0-4
26673696-1	2016	MutY adenine glycosylases prevent DNA mutations by excising adenine from promutagenic 8-oxo-7,8-dihydroguanine (OG):A mismatches.	8-hydroxyguanine	112-114	mutY DNA glycosylase	Homo sapiens	0-4
26673696-2	2016	Here, we describe structural features of the MutY active site bound to an azaribose transition state analog which indicate a catalytic role for Tyr126 and approach of the water nucleophile on the same side as the departing adenine base.	azaribose	74-83	mutY DNA glycosylase	Homo sapiens	45-49
26673696-2	2016	Here, we describe structural features of the MutY active site bound to an azaribose transition state analog which indicate a catalytic role for Tyr126 and approach of the water nucleophile on the same side as the departing adenine base.	Water	171-176	mutY DNA glycosylase	Homo sapiens	45-49
26673696-2	2016	Here, we describe structural features of the MutY active site bound to an azaribose transition state analog which indicate a catalytic role for Tyr126 and approach of the water nucleophile on the same side as the departing adenine base.	Adenine	223-230	mutY DNA glycosylase	Homo sapiens	45-49
26673696-4	2016	NMR analysis of MutY methanolysis products corroborates a mechanism for adenine removal with retention of stereochemistry.	Adenine	72-79	mutY DNA glycosylase	Homo sapiens	16-20
26338705-8	2015	In particular, MUTYH activity on 8-oxodG:rA mispairs is fully inhibited, although its binding capacity is retained.	8-ohdg	33-40	mutY DNA glycosylase	Homo sapiens	15-20
26377631-1	2015	MUTYH is a base excision repair (BER) enzyme that prevents mutations in DNA associated with 8-oxoguanine (OG) by catalyzing the removal of adenine from inappropriately formed OG:A base-pairs.	8-hydroxyguanine	106-108	mutY DNA glycosylase	Homo sapiens	0-5
26377631-1	2015	MUTYH is a base excision repair (BER) enzyme that prevents mutations in DNA associated with 8-oxoguanine (OG) by catalyzing the removal of adenine from inappropriately formed OG:A base-pairs.	Adenine	139-146	mutY DNA glycosylase	Homo sapiens	0-5
26377631-5	2015	P281L MUTYH was found to be severely compromised both in DNA binding and base excision activity, consistent with the location of this variation in the iron-sulfur cluster (FCL) DNA binding motif of MUTYH.	Iron	151-155	mutY DNA glycosylase	Homo sapiens	6-11
26377631-5	2015	P281L MUTYH was found to be severely compromised both in DNA binding and base excision activity, consistent with the location of this variation in the iron-sulfur cluster (FCL) DNA binding motif of MUTYH.	Iron	151-155	mutY DNA glycosylase	Homo sapiens	198-203
26377631-5	2015	P281L MUTYH was found to be severely compromised both in DNA binding and base excision activity, consistent with the location of this variation in the iron-sulfur cluster (FCL) DNA binding motif of MUTYH.	Sulfur	156-162	mutY DNA glycosylase	Homo sapiens	6-11
26377631-5	2015	P281L MUTYH was found to be severely compromised both in DNA binding and base excision activity, consistent with the location of this variation in the iron-sulfur cluster (FCL) DNA binding motif of MUTYH.	Sulfur	156-162	mutY DNA glycosylase	Homo sapiens	198-203
26377631-6	2015	Both R295C and R520Q MUTYH were found to have low fractions of active enzyme, compromised affinity for damaged DNA, and reduced rates for adenine excision.	Adenine	138-145	mutY DNA glycosylase	Homo sapiens	21-26
26056729-12	2015	Additionally, the analysis of the 324 Gln/His MUTYH polymorphism gene distribution in the patient group according to RNFL factor showed that it might decrease the progression of POAG (OR 0.47; 95% CI 0.30-0.82 P = 0.005).	Glutamine	38-41	mutY DNA glycosylase	Homo sapiens	46-51
26312135-2	2015	The human mutY homolog (hMYH) is a base excision repair DNA glycosylase that excises adenines or 2-hydroxyadenines that are mispaired with guanine or 7,8-dihydro-8-oxoguanine (8-oxoG).	Adenine	85-93	mutY DNA glycosylase	Homo sapiens	10-29
26312135-2	2015	The human mutY homolog (hMYH) is a base excision repair DNA glycosylase that excises adenines or 2-hydroxyadenines that are mispaired with guanine or 7,8-dihydro-8-oxoguanine (8-oxoG).	isoguanine	97-114	mutY DNA glycosylase	Homo sapiens	10-29
26312135-2	2015	The human mutY homolog (hMYH) is a base excision repair DNA glycosylase that excises adenines or 2-hydroxyadenines that are mispaired with guanine or 7,8-dihydro-8-oxoguanine (8-oxoG).	Guanine	139-146	mutY DNA glycosylase	Homo sapiens	10-29
26312135-2	2015	The human mutY homolog (hMYH) is a base excision repair DNA glycosylase that excises adenines or 2-hydroxyadenines that are mispaired with guanine or 7,8-dihydro-8-oxoguanine (8-oxoG).	7,8-dihydro-8-oxoguanine	150-174	mutY DNA glycosylase	Homo sapiens	10-29
26312135-2	2015	The human mutY homolog (hMYH) is a base excision repair DNA glycosylase that excises adenines or 2-hydroxyadenines that are mispaired with guanine or 7,8-dihydro-8-oxoguanine (8-oxoG).	7,8-dihydro-8-oxoguanine	176-182	mutY DNA glycosylase	Homo sapiens	10-29
26312135-5	2015	RESULTS: We documented the interaction between hTopBP1 and hMYH and showed that this interaction increased in a hydroxyurea-dependent manner.	Hydroxyurea	112-123	mutY DNA glycosylase	Homo sapiens	59-63
25127721-0	2014	Visualization of the physical and functional interaction between hMYH and hRad9 by Dronpa bimolecular fluorescence complementation.	dronpa	83-89	mutY DNA glycosylase	Homo sapiens	65-69
25800745-0	2015	Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria.	isoguanine	67-83	mutY DNA glycosylase	Homo sapiens	38-42
25638157-0	2015	MUTYH mediates the toxicity of combined DNA 6-thioguanine and UVA radiation.	Thioguanine	44-57	mutY DNA glycosylase	Homo sapiens	0-5
25638157-5	2015	Surprisingly, Mutyh-null MEFs were more resistant than wild-type MEFs, despite accumulating higher levels of DNA 8-oxo-7,8-dihydroguanine (8-oxoG).Their enhanced 6-TG/UVA resistance reflected the absence of the MUTYH protein and MEFs expressing enzymatically-dead human variants were as sensitive as wild-type cells.	8-hydroxyguanine	113-137	mutY DNA glycosylase	Homo sapiens	14-19
25638157-5	2015	Surprisingly, Mutyh-null MEFs were more resistant than wild-type MEFs, despite accumulating higher levels of DNA 8-oxo-7,8-dihydroguanine (8-oxoG).Their enhanced 6-TG/UVA resistance reflected the absence of the MUTYH protein and MEFs expressing enzymatically-dead human variants were as sensitive as wild-type cells.	Thioguanine	163-166	mutY DNA glycosylase	Homo sapiens	14-19
26576226-1	2015	MUTYH is a DNA repair enzyme that initiates a base excision repair (BER) by recognizing and removing 8-Oxoguanine (8-oxoG) and its paired adenine.	8-hydroxyguanine	101-113	mutY DNA glycosylase	Homo sapiens	0-5
26576226-1	2015	MUTYH is a DNA repair enzyme that initiates a base excision repair (BER) by recognizing and removing 8-Oxoguanine (8-oxoG) and its paired adenine.	8-hydroxyguanine	115-121	mutY DNA glycosylase	Homo sapiens	0-5
26576226-1	2015	MUTYH is a DNA repair enzyme that initiates a base excision repair (BER) by recognizing and removing 8-Oxoguanine (8-oxoG) and its paired adenine.	Adenine	138-145	mutY DNA glycosylase	Homo sapiens	0-5
25310643-2	2014	We previously reported that 8-oxoguanine (8-oxoG) accumulation in nuclear DNA (nDNA) and mitochondrial DNA triggers two distinct caspase-independent cell death through buildup of single-strand DNA breaks by MutY homolog (MUTYH), an adenine DNA glycosylase.	8-hydroxyguanine	28-40	mutY DNA glycosylase	Homo sapiens	221-226
25310643-2	2014	We previously reported that 8-oxoguanine (8-oxoG) accumulation in nuclear DNA (nDNA) and mitochondrial DNA triggers two distinct caspase-independent cell death through buildup of single-strand DNA breaks by MutY homolog (MUTYH), an adenine DNA glycosylase.	8-hydroxyguanine	42-48	mutY DNA glycosylase	Homo sapiens	221-226
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	Adenine	101-109	mutY DNA glycosylase	Homo sapiens	31-34
24443563-4	2014	The MutY DNA glycosylase homologue (MutYH) recognizes A:8-oxo-G mispairs and removes the mispaired A giving way to the canonical base excision repair that ultimately restores undamaged guanine (G).	Guanine	185-192	mutY DNA glycosylase	Homo sapiens	36-41
24443563-7	2014	Mutation of five lysine residues in this region significantly stabilizes MutYH, suggesting that these are the target sites for ubiquitination.	Lysine	17-23	mutY DNA glycosylase	Homo sapiens	73-78
24569162-1	2014	The MUTYH DNA glycosylase counteracts mutagenesis by removing adenine misincorporated opposite DNA 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxodG).	Adenine	62-69	mutY DNA glycosylase	Homo sapiens	4-9
24569162-1	2014	The MUTYH DNA glycosylase counteracts mutagenesis by removing adenine misincorporated opposite DNA 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxodG).	8-ohdg	99-134	mutY DNA glycosylase	Homo sapiens	4-9
24569162-1	2014	The MUTYH DNA glycosylase counteracts mutagenesis by removing adenine misincorporated opposite DNA 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-oxodG).	8-ohdg	136-143	mutY DNA glycosylase	Homo sapiens	4-9
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	8-hydroxyguanine	154-178	mutY DNA glycosylase	Homo sapiens	38-43
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	8-hydroxyguanine	180-187	mutY DNA glycosylase	Homo sapiens	31-34
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	8-hydroxyguanine	180-187	mutY DNA glycosylase	Homo sapiens	38-43
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	Adenine	101-109	mutY DNA glycosylase	Homo sapiens	38-43
24315136-4	2014	MYH knockdown human HeLa cells are more sensitive to the killing effects of H2O2 than the control cells.	Hydrogen Peroxide	76-80	mutY DNA glycosylase	Homo sapiens	0-3
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	isoguanine	113-130	mutY DNA glycosylase	Homo sapiens	31-34
24315136-7	2014	Moreover, hMYH knockdown cells contain higher levels of 8-oxo-G lesions than the control cells following H2O2 treatment.	Hydrogen Peroxide	105-109	mutY DNA glycosylase	Homo sapiens	10-14
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	isoguanine	113-130	mutY DNA glycosylase	Homo sapiens	38-43
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	Guanine	143-150	mutY DNA glycosylase	Homo sapiens	31-34
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	Guanine	143-150	mutY DNA glycosylase	Homo sapiens	38-43
24315136-1	2014	MutY DNA glycosylase homologs (MYH or MUTYH) reduce G:C to T:A mutations by removing misincorporated adenines or 2-hydroxyadenines paired with guanine or 8-oxo-7,8-dihydroguanine (8-oxo-G).	8-hydroxyguanine	154-178	mutY DNA glycosylase	Homo sapiens	31-34
23936466-2	2013	The polymorphic AluYb8 insertion in the 15(th) intron of the MUTYH gene (AluYb8MUTYH) has been shown to associate with an aggregated 8-hydroxy-2"-deoxyguanosine (8-OH-dG) lesion in genomic DNA and to serve as a risk factor for age-related diseases.	8-ohdg	133-160	mutY DNA glycosylase	Homo sapiens	61-66
24799981-0	2014	Impaired 8-hydroxyguanine repair activity of MUTYH variant p.Arg109Trp found in a Japanese patient with early-onset colorectal cancer.	8-hydroxyguanine	9-25	mutY DNA glycosylase	Homo sapiens	45-50
24799981-1	2014	PURPOSE: The biallelic inactivation of the 8-hydroxyguanine repair gene MUTYH leads to MUTYH-associated polyposis (MAP), which is characterized by colorectal multiple polyps and carcinoma(s).	8-hydroxyguanine	43-59	mutY DNA glycosylase	Homo sapiens	72-77
24799981-1	2014	PURPOSE: The biallelic inactivation of the 8-hydroxyguanine repair gene MUTYH leads to MUTYH-associated polyposis (MAP), which is characterized by colorectal multiple polyps and carcinoma(s).	8-hydroxyguanine	43-59	mutY DNA glycosylase	Homo sapiens	87-92
24209961-1	2013	MutY homologue (MYH) is a DNA glycosylase which excises adenine paired with the oxidative lesion 7,8-dihydro-8-oxoguanine (8-oxoG, or G(o)) during base excision repair (BER).	Adenine	56-63	mutY DNA glycosylase	Homo sapiens	16-19
24209961-1	2013	MutY homologue (MYH) is a DNA glycosylase which excises adenine paired with the oxidative lesion 7,8-dihydro-8-oxoguanine (8-oxoG, or G(o)) during base excision repair (BER).	7,8-dihydro-8-oxoguanine	97-121	mutY DNA glycosylase	Homo sapiens	16-19
24209961-1	2013	MutY homologue (MYH) is a DNA glycosylase which excises adenine paired with the oxidative lesion 7,8-dihydro-8-oxoguanine (8-oxoG, or G(o)) during base excision repair (BER).	7,8-dihydro-8-oxoguanine	123-129	mutY DNA glycosylase	Homo sapiens	16-19
24209961-2	2013	Base excision by MYH results in an apurinic/apyrimidinic (AP) site in the DNA where the DNA sugar-phosphate backbone remains intact.	Sugar Phosphates	92-107	mutY DNA glycosylase	Homo sapiens	17-20
23108399-1	2013	The DNA glycosylase MUTYH (mutY homolog (Escherichia coli)) counteracts the mutagenic effects of 8-oxo-7,8-dihydroguanine (8-oxodG) by removing adenine (A) misincorporated opposite the oxidized purine.	8-hydroxyguanine	97-121	mutY DNA glycosylase	Homo sapiens	20-25
23108399-1	2013	The DNA glycosylase MUTYH (mutY homolog (Escherichia coli)) counteracts the mutagenic effects of 8-oxo-7,8-dihydroguanine (8-oxodG) by removing adenine (A) misincorporated opposite the oxidized purine.	8-hydroxyguanine	123-130	mutY DNA glycosylase	Homo sapiens	20-25
23108399-1	2013	The DNA glycosylase MUTYH (mutY homolog (Escherichia coli)) counteracts the mutagenic effects of 8-oxo-7,8-dihydroguanine (8-oxodG) by removing adenine (A) misincorporated opposite the oxidized purine.	Adenine	144-151	mutY DNA glycosylase	Homo sapiens	20-25
23108399-1	2013	The DNA glycosylase MUTYH (mutY homolog (Escherichia coli)) counteracts the mutagenic effects of 8-oxo-7,8-dihydroguanine (8-oxodG) by removing adenine (A) misincorporated opposite the oxidized purine.	purine	194-200	mutY DNA glycosylase	Homo sapiens	20-25
23108399-8	2013	They were also hypermutable by KBrO3--a source of DNA 8-oxodG--indicating that the relatively modest spontaneous mutator phenotype associated with MUTYH loss can be significantly enhanced by conditions of oxidative stress.	kbro3	31-36	mutY DNA glycosylase	Homo sapiens	147-152
23108399-8	2013	They were also hypermutable by KBrO3--a source of DNA 8-oxodG--indicating that the relatively modest spontaneous mutator phenotype associated with MUTYH loss can be significantly enhanced by conditions of oxidative stress.	8-hydroxyguanine	54-61	mutY DNA glycosylase	Homo sapiens	147-152
23108399-9	2013	These observations identify accumulation of DNA 8-oxodG and a mutator phenotype as likely contributors to the pathogenesis of MUTYH variants.	8-hydroxyguanine	48-55	mutY DNA glycosylase	Homo sapiens	126-131
23936466-2	2013	The polymorphic AluYb8 insertion in the 15(th) intron of the MUTYH gene (AluYb8MUTYH) has been shown to associate with an aggregated 8-hydroxy-2"-deoxyguanosine (8-OH-dG) lesion in genomic DNA and to serve as a risk factor for age-related diseases.	8-ohdg	162-169	mutY DNA glycosylase	Homo sapiens	61-66
23450852-7	2013	MUTYH can remove the mispaired A from an A:8-oxo-G, giving way to the canonical base-excision repair (BER) that ultimately restores undamaged Guanine (G).	Guanine	142-149	mutY DNA glycosylase	Homo sapiens	0-5
23499241-12	2013	In addition, the presence of the 326His allele of the MUTYH gene may increase the risk for POAG progression, according to the VF parameter (OR 2.57; 95% CI, 1.47-4.57, P=0.0001).	326his	33-39	mutY DNA glycosylase	Homo sapiens	54-59
23507534-1	2013	MUTYH, a human ortholog of MutY, is a post-replicative DNA glycosylase, highly conserved throughout evolution, involved in the correction of mismatches resulting from a faulty replication of the oxidized base 8-hydroxyguanine (8-oxodG).	8-hydroxyguanine	209-225	mutY DNA glycosylase	Homo sapiens	0-5
23507534-1	2013	MUTYH, a human ortholog of MutY, is a post-replicative DNA glycosylase, highly conserved throughout evolution, involved in the correction of mismatches resulting from a faulty replication of the oxidized base 8-hydroxyguanine (8-oxodG).	8-ohdg	227-234	mutY DNA glycosylase	Homo sapiens	0-5
23507534-2	2013	In particular removal of adenine from A:8-oxodG mispairs by MUTYH activity is followed by error-free base excision repair (BER) events, leading to the formation of C:8-oxodG base pairs.	Adenine	25-32	mutY DNA glycosylase	Homo sapiens	60-65
23507534-2	2013	In particular removal of adenine from A:8-oxodG mispairs by MUTYH activity is followed by error-free base excision repair (BER) events, leading to the formation of C:8-oxodG base pairs.	8-ohdg	40-47	mutY DNA glycosylase	Homo sapiens	60-65
23507534-2	2013	In particular removal of adenine from A:8-oxodG mispairs by MUTYH activity is followed by error-free base excision repair (BER) events, leading to the formation of C:8-oxodG base pairs.	Carbon	164-165	mutY DNA glycosylase	Homo sapiens	60-65
23507534-2	2013	In particular removal of adenine from A:8-oxodG mispairs by MUTYH activity is followed by error-free base excision repair (BER) events, leading to the formation of C:8-oxodG base pairs.	8-ohdg	166-173	mutY DNA glycosylase	Homo sapiens	60-65
23677194-9	2012	The genetic study identified a homozygous mutation of the MUTYH gene, called c.340T &gt; C, that produces an amino acid change of tyrosine for histidine called p.Y114H.	Tyrosine	130-138	mutY DNA glycosylase	Homo sapiens	58-63
24377541-1	2013	PURPOSE: Biallelic germline variants of the 8-hydroxyguanine (8-OG) repair gene MYH have been associated with colorectal neoplasms that display somatic G:C?T:A transversions.	8-hydroxyguanine	44-60	mutY DNA glycosylase	Homo sapiens	80-83
24377541-1	2013	PURPOSE: Biallelic germline variants of the 8-hydroxyguanine (8-OG) repair gene MYH have been associated with colorectal neoplasms that display somatic G:C?T:A transversions.	8-hydroxyguanine	62-66	mutY DNA glycosylase	Homo sapiens	80-83
23322991-1	2012	AIM: To investigate the suppressive activity of MUTYH variant proteins against mutations caused by oxidative lesion, 8-hydroxyguanine (8OHG), in human cells.	8-hydroxyguanine	117-133	mutY DNA glycosylase	Homo sapiens	48-53
23322991-1	2012	AIM: To investigate the suppressive activity of MUTYH variant proteins against mutations caused by oxidative lesion, 8-hydroxyguanine (8OHG), in human cells.	8ohg	135-139	mutY DNA glycosylase	Homo sapiens	48-53
23322991-10	2012	The mutation frequency (4.7 x 10(-3)) of supF in the 8OHG-containing pMY189 plasmid in cells overexpressing WT MUTYH was significantly lower than in the empty vector cells (P &lt; 0.01).	8ohg	53-57	mutY DNA glycosylase	Homo sapiens	111-116
23038810-3	2012	The involvement of UNG and MYH is likely the result of a TMZ-induced burst of reactive oxygen species.	Temozolomide	57-60	mutY DNA glycosylase	Homo sapiens	27-30
23038810-3	2012	The involvement of UNG and MYH is likely the result of a TMZ-induced burst of reactive oxygen species.	Reactive Oxygen Species	78-101	mutY DNA glycosylase	Homo sapiens	27-30
23226797-1	2012	Etoposide (ETP) treatment of ataxia telangiectasia mutated (ATM) and Rad3-related protein (ATR)-, topoisomerase-binding protein-1 (TopBP1) and human MutY homolog (hMYH)-depleted cells results in a significant reduction in apoptotic signaling.	Etoposide	0-9	mutY DNA glycosylase	Homo sapiens	163-167
23226797-3	2012	In hMYH knockdown cells, the interaction between ATR and TopBP1 decreased following ETP treatment.	Etoposide	84-87	mutY DNA glycosylase	Homo sapiens	3-7
23226797-4	2012	We suggest that hMYH functions as a sensor of ETP-induced apoptosis.	Etoposide	46-49	mutY DNA glycosylase	Homo sapiens	16-20
22926731-2	2012	MUTYH removes adenine misincorporated opposite the DNA oxidation product, 8-oxoguanine (OG), thereby preventing accumulation of G:C to T:A transversion mutations.	Adenine	14-21	mutY DNA glycosylase	Homo sapiens	0-5
22926731-2	2012	MUTYH removes adenine misincorporated opposite the DNA oxidation product, 8-oxoguanine (OG), thereby preventing accumulation of G:C to T:A transversion mutations.	8-hydroxyguanine	74-86	mutY DNA glycosylase	Homo sapiens	0-5
22926731-2	2012	MUTYH removes adenine misincorporated opposite the DNA oxidation product, 8-oxoguanine (OG), thereby preventing accumulation of G:C to T:A transversion mutations.	8-hydroxyguanine	88-90	mutY DNA glycosylase	Homo sapiens	0-5
22926731-3	2012	The most common cancer-associated MUTYH variant proteins when expressed in bacteria exhibit reduced OG:A mismatch affinity and adenine removal activity.	Adenine	127-134	mutY DNA glycosylase	Homo sapiens	34-39
23677194-9	2012	The genetic study identified a homozygous mutation of the MUTYH gene, called c.340T &gt; C, that produces an amino acid change of tyrosine for histidine called p.Y114H.	Histidine	143-152	mutY DNA glycosylase	Homo sapiens	58-63
22641385-1	2012	The base excision repair gene MUTYH encodes glycosylase which removes adenine             residues mispaired with 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-OHG).	Adenine	70-77	mutY DNA glycosylase	Homo sapiens	30-35
22641385-1	2012	The base excision repair gene MUTYH encodes glycosylase which removes adenine             residues mispaired with 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-OHG).	8-ohdg	114-149	mutY DNA glycosylase	Homo sapiens	30-35
22641385-1	2012	The base excision repair gene MUTYH encodes glycosylase which removes adenine             residues mispaired with 8-oxo-7,8-dihydro-2"-deoxyguanosine (8-OHG).	8-ohdg	151-156	mutY DNA glycosylase	Homo sapiens	30-35
22753033-2	2012	8-oxo-G:A mispairs arising during DNA replication are eliminated by base excision repair initiated by the MutY DNA glycosylase homologue (MUTYH).	7,8-dihydro-8-oxoguanine	0-7	mutY DNA glycosylase	Homo sapiens	106-136
22753033-2	2012	8-oxo-G:A mispairs arising during DNA replication are eliminated by base excision repair initiated by the MutY DNA glycosylase homologue (MUTYH).	7,8-dihydro-8-oxoguanine	0-7	mutY DNA glycosylase	Homo sapiens	138-143
22753033-6	2012	Cell viability assays reveal that depletion of MUTYH suppresses the hypersensitivity of cells lacking WRN and/or Pollambda to oxidative stress.	pollambda	113-122	mutY DNA glycosylase	Homo sapiens	47-52
22753033-8	2012	Our results suggest that WRN promotes long-patch DNA repair synthesis by Pollambda during MUTYH-initiated repair of 8-oxo-G:A mispairs.	7,8-dihydro-8-oxoguanine	116-123	mutY DNA glycosylase	Homo sapiens	90-95
22641385-8	2012	Investigation of quantitative allelic             imbalance at SNP rs3219489 of MUTYH showed that CRC cases with C allele dominance             (minor type corresponding to His) were more frequently detected with G:C T:A transversions             than in those with G allele dominance (major type corresponding to Gln).	Glutamine	314-317	mutY DNA glycosylase	Homo sapiens	80-85
22449827-10	2012	In addition, the expression levels of base excision enzymes that are involved in hOGG1, hMTH1, and MYH in MeT-5A cells remained unchanged for 24 h after carbon nanotube exposure.	Carbon	153-159	mutY DNA glycosylase	Homo sapiens	99-102
22469746-4	2012	The DNA glycosylases encoded by the hOGG1 and MUTYH genes initiate this pathway by recognizing and removing 8-oxoguanine and adenine paired with 8-oxoguanine, respectively.	8-hydroxyguanine	108-120	mutY DNA glycosylase	Homo sapiens	46-51
22469746-4	2012	The DNA glycosylases encoded by the hOGG1 and MUTYH genes initiate this pathway by recognizing and removing 8-oxoguanine and adenine paired with 8-oxoguanine, respectively.	Adenine	125-132	mutY DNA glycosylase	Homo sapiens	46-51
22469746-4	2012	The DNA glycosylases encoded by the hOGG1 and MUTYH genes initiate this pathway by recognizing and removing 8-oxoguanine and adenine paired with 8-oxoguanine, respectively.	8-hydroxyguanine	145-157	mutY DNA glycosylase	Homo sapiens	46-51
22444586-1	2012	MutY and its human ortholog, MUTYH, repair a specific form of DNA damage: adenine mis-paired with the oxidatively modified form of deoxyguanosine, 8-oxo-7,8-dihydro-2"-deoxyguanosine.	Adenine	74-81	mutY DNA glycosylase	Homo sapiens	29-34
22444586-1	2012	MutY and its human ortholog, MUTYH, repair a specific form of DNA damage: adenine mis-paired with the oxidatively modified form of deoxyguanosine, 8-oxo-7,8-dihydro-2"-deoxyguanosine.	Deoxyguanosine	131-145	mutY DNA glycosylase	Homo sapiens	29-34
22444586-1	2012	MutY and its human ortholog, MUTYH, repair a specific form of DNA damage: adenine mis-paired with the oxidatively modified form of deoxyguanosine, 8-oxo-7,8-dihydro-2"-deoxyguanosine.	8-ohdg	147-182	mutY DNA glycosylase	Homo sapiens	29-34
21826668-0	2011	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.	8-hydroxyguanine	82-98	mutY DNA glycosylase	Homo sapiens	22-27
22977630-2	2011	To investigate the correlation between expression of the DNA repair enzyme MYH in esophageal squamous cell carcinoma and 8-oxoguanine (8-oxoG) oxidative damage, as well as the clinical significance of altered MYH expression, tissues from 175 esophageal carcinoma cases were investigated in the present study.	8-hydroxyguanine	121-133	mutY DNA glycosylase	Homo sapiens	75-78
22977630-2	2011	To investigate the correlation between expression of the DNA repair enzyme MYH in esophageal squamous cell carcinoma and 8-oxoguanine (8-oxoG) oxidative damage, as well as the clinical significance of altered MYH expression, tissues from 175 esophageal carcinoma cases were investigated in the present study.	8-hydroxyguanine	135-141	mutY DNA glycosylase	Homo sapiens	75-78
22720119-5	2012	The average 8-OHdG/10(6) dG value was significantly higher in patients with the OGG1 c.977G, MUTYH c.972G or AluYb8MUTYH alleles (P &lt; 0.001 via ANOVA).	8-ohdg	12-18	mutY DNA glycosylase	Homo sapiens	93-98
22720119-6	2012	Further analysis showed that combination of MUTYH c.972GG with OGG1 c.977GG or AluYb8MUTYH increased both the risk for ESRD and leukocyte DNA 8-OHdG levels in HD patients.	8-ohdg	142-148	mutY DNA glycosylase	Homo sapiens	44-49
21826668-1	2011	The MUTYH gene encodes a DNA glycosylase that can initiate the excision repair of adenine mispaired with 8-hydroxyguanine (8OHG) and is responsible for a susceptibility to multiple colorectal adenomas and carcinomas.	Adenine	82-89	mutY DNA glycosylase	Homo sapiens	4-9
21826668-1	2011	The MUTYH gene encodes a DNA glycosylase that can initiate the excision repair of adenine mispaired with 8-hydroxyguanine (8OHG) and is responsible for a susceptibility to multiple colorectal adenomas and carcinomas.	8-hydroxyguanine	105-121	mutY DNA glycosylase	Homo sapiens	4-9
21826668-1	2011	The MUTYH gene encodes a DNA glycosylase that can initiate the excision repair of adenine mispaired with 8-hydroxyguanine (8OHG) and is responsible for a susceptibility to multiple colorectal adenomas and carcinomas.	8ohg	123-127	mutY DNA glycosylase	Homo sapiens	4-9
21826668-8	2011	MUTYH-over-expressing stable clones of the gastric cancer cell line AGS showed: (a) higher DNA cleavage activity towards adenine:8OHG mispair-containing substrates; (b) higher suppressive activity against mutations caused by 8OHG in a supF forward mutation assay; and (c) higher suppressive activity for cellular proliferation than empty vector-transfected AGS clones.	Adenine	121-128	mutY DNA glycosylase	Homo sapiens	0-5
21826668-8	2011	MUTYH-over-expressing stable clones of the gastric cancer cell line AGS showed: (a) higher DNA cleavage activity towards adenine:8OHG mispair-containing substrates; (b) higher suppressive activity against mutations caused by 8OHG in a supF forward mutation assay; and (c) higher suppressive activity for cellular proliferation than empty vector-transfected AGS clones.	8ohg	129-133	mutY DNA glycosylase	Homo sapiens	0-5
21826668-8	2011	MUTYH-over-expressing stable clones of the gastric cancer cell line AGS showed: (a) higher DNA cleavage activity towards adenine:8OHG mispair-containing substrates; (b) higher suppressive activity against mutations caused by 8OHG in a supF forward mutation assay; and (c) higher suppressive activity for cellular proliferation than empty vector-transfected AGS clones.	8ohg	225-229	mutY DNA glycosylase	Homo sapiens	0-5
21826668-9	2011	These results suggested that MUTYH is a suppressor of mutations caused by 8OHG in gastric cells and that its reduced expression is associated with a poor prognosis in gastric cancer.	8ohg	74-78	mutY DNA glycosylase	Homo sapiens	29-34
21279954-1	2011	MUTYH glycosylase recognizes the 8-oxoG:A mismatch and is able to excise the adenine base using proofreading mechanisms.	Adenine	77-84	mutY DNA glycosylase	Homo sapiens	0-5
21615992-0	2011	Knock-down of human MutY homolog (hMYH) decreases phosphorylation of checkpoint kinase 1 (Chk1) induced by hydroxyurea and UV treatment.	Hydroxyurea	107-118	mutY DNA glycosylase	Homo sapiens	34-38
21615992-1	2011	The effect of human MutY homolog (hMYH) on the activation of checkpoint proteins in response to hydroxyurea (HU) and ultraviolet (UV) treatment was investigated in hMYH-disrupted HEK293 cells.	Hydroxyurea	96-107	mutY DNA glycosylase	Homo sapiens	34-38
21235684-2	2011	Adenine DNA glycosylase, encoded by the human mutY homolog gene, MUTYH, excises adenine in the nascent strand when inserted opposite 8-oxoguanine in template DNA, and thus suppresses mutagenesis caused by 8-oxoguanine that has accumulated in DNA due to oxidative stress.	Adenine	80-87	mutY DNA glycosylase	Homo sapiens	0-23
21235684-2	2011	Adenine DNA glycosylase, encoded by the human mutY homolog gene, MUTYH, excises adenine in the nascent strand when inserted opposite 8-oxoguanine in template DNA, and thus suppresses mutagenesis caused by 8-oxoguanine that has accumulated in DNA due to oxidative stress.	Adenine	80-87	mutY DNA glycosylase	Homo sapiens	65-70
21235684-2	2011	Adenine DNA glycosylase, encoded by the human mutY homolog gene, MUTYH, excises adenine in the nascent strand when inserted opposite 8-oxoguanine in template DNA, and thus suppresses mutagenesis caused by 8-oxoguanine that has accumulated in DNA due to oxidative stress.	8-hydroxyguanine	133-145	mutY DNA glycosylase	Homo sapiens	0-23
21235684-2	2011	Adenine DNA glycosylase, encoded by the human mutY homolog gene, MUTYH, excises adenine in the nascent strand when inserted opposite 8-oxoguanine in template DNA, and thus suppresses mutagenesis caused by 8-oxoguanine that has accumulated in DNA due to oxidative stress.	8-hydroxyguanine	133-145	mutY DNA glycosylase	Homo sapiens	65-70
21235684-2	2011	Adenine DNA glycosylase, encoded by the human mutY homolog gene, MUTYH, excises adenine in the nascent strand when inserted opposite 8-oxoguanine in template DNA, and thus suppresses mutagenesis caused by 8-oxoguanine that has accumulated in DNA due to oxidative stress.	8-hydroxyguanine	205-217	mutY DNA glycosylase	Homo sapiens	0-23
21235684-2	2011	Adenine DNA glycosylase, encoded by the human mutY homolog gene, MUTYH, excises adenine in the nascent strand when inserted opposite 8-oxoguanine in template DNA, and thus suppresses mutagenesis caused by 8-oxoguanine that has accumulated in DNA due to oxidative stress.	8-hydroxyguanine	205-217	mutY DNA glycosylase	Homo sapiens	65-70
21235684-7	2011	Our findings indicate that MUTYH-induced cell death due to oxidative stress results in an efficient elimination of mutagenic cells that have accumulated high levels of 8-oxoguanine in their DNAs.	8-hydroxyguanine	168-180	mutY DNA glycosylase	Homo sapiens	27-32
21235684-8	2011	It is most likely that loss of function of MUTYH in stem or progenitor cells in the intestinal epithelium of MUTYH-associated polyposis patients results in escape from programmed cell death; however, accumulated 8-oxoguanine causes various mutations in APC or KRAS genes in these proliferative cells, thereby promoting tumorigenesis.	8-hydroxyguanine	212-224	mutY DNA glycosylase	Homo sapiens	43-48
21615992-1	2011	The effect of human MutY homolog (hMYH) on the activation of checkpoint proteins in response to hydroxyurea (HU) and ultraviolet (UV) treatment was investigated in hMYH-disrupted HEK293 cells.	Hydroxyurea	96-107	mutY DNA glycosylase	Homo sapiens	164-168
21112374-0	2011	AluYb8 insertion in the MUTYH gene is related to increased 8-OHdG in genomic DNA and could be a risk factor for type 2 diabetes in a Chinese population.	8-ohdg	59-65	mutY DNA glycosylase	Homo sapiens	24-29
20816984-1	2010	The DNA glycosylase MutY homologue (MYH or MUTYH) removes adenines misincorporated opposite 8-oxoguanine as part of the base excision repair pathway.	Adenine	58-66	mutY DNA glycosylase	Homo sapiens	36-39
20816984-5	2010	The interdomain connector (IDC, residues 295-350) between the catalytic domain and the 8-oxoguanine recognition domain of hMYH is a critical element that maintains interactions with the 9-1-1 complex.	8-hydroxyguanine	87-99	mutY DNA glycosylase	Homo sapiens	122-126
20848659-5	2010	These results should be of great value in accurately diagnosing MAP and in fully understanding the mechanism by which MUTYH repairs DNA in which adenine is mispaired with 8-hydroxyguanine.	Adenine	145-152	mutY DNA glycosylase	Homo sapiens	118-123
20848659-5	2010	These results should be of great value in accurately diagnosing MAP and in fully understanding the mechanism by which MUTYH repairs DNA in which adenine is mispaired with 8-hydroxyguanine.	8-hydroxyguanine	171-187	mutY DNA glycosylase	Homo sapiens	118-123
20816984-1	2010	The DNA glycosylase MutY homologue (MYH or MUTYH) removes adenines misincorporated opposite 8-oxoguanine as part of the base excision repair pathway.	8-hydroxyguanine	92-104	mutY DNA glycosylase	Homo sapiens	36-39
20418187-1	2010	The MUTYH DNA glycosylase specifically removes adenine misincorporated by replicative polymerases opposite the oxidized purine 8-oxo-7,8-dihydroguanine (8-oxoG).	8-hydroxyguanine	153-159	mutY DNA glycosylase	Homo sapiens	4-9
20724227-0	2010	Ser 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): a mismatch recognition.	Serine	0-3	mutY DNA glycosylase	Homo sapiens	37-42
20724227-0	2010	Ser 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): a mismatch recognition.	8-hydroxyguanine	85-87	mutY DNA glycosylase	Homo sapiens	37-42
20724227-2	2010	MUTYH is a DNA glycosylase that removes adenine (A) misinserted opposite 8-oxo-7,8-dihydro-2"-deoxyguanosine (OG).	Adenine	40-47	mutY DNA glycosylase	Homo sapiens	0-5
20724227-2	2010	MUTYH is a DNA glycosylase that removes adenine (A) misinserted opposite 8-oxo-7,8-dihydro-2"-deoxyguanosine (OG).	8-ohdg	73-108	mutY DNA glycosylase	Homo sapiens	0-5
20724227-2	2010	MUTYH is a DNA glycosylase that removes adenine (A) misinserted opposite 8-oxo-7,8-dihydro-2"-deoxyguanosine (OG).	8-hydroxyguanine	110-112	mutY DNA glycosylase	Homo sapiens	0-5
20418187-1	2010	The MUTYH DNA glycosylase specifically removes adenine misincorporated by replicative polymerases opposite the oxidized purine 8-oxo-7,8-dihydroguanine (8-oxoG).	Adenine	47-54	mutY DNA glycosylase	Homo sapiens	4-9
20373040-10	2010	Furthermore, complemented Dronpa, induced by the interaction between hMYH-LDN and DCL-hHus1, showed almost identical photoswitching activity as that of native Dronpa.	dronpa	26-32	mutY DNA glycosylase	Homo sapiens	69-73
20373040-10	2010	Furthermore, complemented Dronpa, induced by the interaction between hMYH-LDN and DCL-hHus1, showed almost identical photoswitching activity as that of native Dronpa.	dronpa	159-165	mutY DNA glycosylase	Homo sapiens	69-73
20434453-8	2010	Of the APC/MUTYH-mutation-negative families, 2 (9%) had ASE imbalance, which might cause the disease.	ase	56-59	mutY DNA glycosylase	Homo sapiens	11-16
20418187-1	2010	The MUTYH DNA glycosylase specifically removes adenine misincorporated by replicative polymerases opposite the oxidized purine 8-oxo-7,8-dihydroguanine (8-oxoG).	purine	120-126	mutY DNA glycosylase	Homo sapiens	4-9
20436219-3	2010	The aim of the present study was to compare the effects of two different bile salts, deoxycholic acid (DCA) and ursodeoxycholic acid (UDCA) on the expression of COX-2, CDX-2 and DNA repair enzymes (MUTYH, OGG-1) in the Barrett epithelial cancer cells (OE-19).	Deoxycholic Acid	85-101	mutY DNA glycosylase	Homo sapiens	198-203
20418187-1	2010	The MUTYH DNA glycosylase specifically removes adenine misincorporated by replicative polymerases opposite the oxidized purine 8-oxo-7,8-dihydroguanine (8-oxoG).	8-hydroxyguanine	127-151	mutY DNA glycosylase	Homo sapiens	4-9
20197241-5	2010	The knock-down of MUTYH resulted in a reduction in A:T--&gt;C:G transversions induced by 8-oxo-dGTP and the 8-oxo-Gua:A pair, but the knockdown of OGG1, NTH1, and NEIL1 had no effect on mutagenesis.	8-oxodeoxyguanosine triphosphate	89-99	mutY DNA glycosylase	Homo sapiens	18-23
20197241-5	2010	The knock-down of MUTYH resulted in a reduction in A:T--&gt;C:G transversions induced by 8-oxo-dGTP and the 8-oxo-Gua:A pair, but the knockdown of OGG1, NTH1, and NEIL1 had no effect on mutagenesis.	8-hydroxyguanine	108-117	mutY DNA glycosylase	Homo sapiens	18-23
20197241-7	2010	In contrast, it appears that MUTYH enhances A:T--&gt;C:G mutations caused by 8-oxo-dGTP.	8-oxodeoxyguanosine triphosphate	77-87	mutY DNA glycosylase	Homo sapiens	29-34
20436219-3	2010	The aim of the present study was to compare the effects of two different bile salts, deoxycholic acid (DCA) and ursodeoxycholic acid (UDCA) on the expression of COX-2, CDX-2 and DNA repair enzymes (MUTYH, OGG-1) in the Barrett epithelial cancer cells (OE-19).	Bile Acids and Salts	73-83	mutY DNA glycosylase	Homo sapiens	198-203
20436219-3	2010	The aim of the present study was to compare the effects of two different bile salts, deoxycholic acid (DCA) and ursodeoxycholic acid (UDCA) on the expression of COX-2, CDX-2 and DNA repair enzymes (MUTYH, OGG-1) in the Barrett epithelial cancer cells (OE-19).	Deoxycholic Acid	103-106	mutY DNA glycosylase	Homo sapiens	198-203
20436219-3	2010	The aim of the present study was to compare the effects of two different bile salts, deoxycholic acid (DCA) and ursodeoxycholic acid (UDCA) on the expression of COX-2, CDX-2 and DNA repair enzymes (MUTYH, OGG-1) in the Barrett epithelial cancer cells (OE-19).	Ursodeoxycholic Acid	112-132	mutY DNA glycosylase	Homo sapiens	198-203
20436219-6	2010	After incubation of OE-19 cells with bile salts, the expression of mRNA of COX-2, DNA repair enzymes (MUTYH, OGG-1) and caudal-related homebox transcription factor CDX-2 were measured by quantitative RT-PCR.	Bile Acids and Salts	37-47	mutY DNA glycosylase	Homo sapiens	102-107
20436219-12	2010	DCA caused stronger downregulation of mRNA for DNA repair enzymes MUTYH and OGG-1 than UDCA.	Deoxycholic Acid	0-3	mutY DNA glycosylase	Homo sapiens	66-71
19836313-0	2009	Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer.	Adenine	0-7	mutY DNA glycosylase	Homo sapiens	86-91
19932167-1	2010	We describe a common mutation of the MYH gene, which is involved in the repair of oxidative damage to DNA, and its relationship to age, levels of 8-OHdG, and circulating levels of interleukin-1.	8-ohdg	146-152	mutY DNA glycosylase	Homo sapiens	37-40
19932167-5	2010	Because the MYH gene is involved in DNA repair we assessed whether homozygous carriage of this gene was associated with increased levels of 8-OHdG in the leukocytic DNA of carriers.	8-ohdg	140-146	mutY DNA glycosylase	Homo sapiens	12-15
19836313-2	2009	The MUTYH glycosylase plays an important role in preventing mutations associated with 8-oxoguanine (OG) by removing adenine residues that have been misincorporated opposite OG.	8-hydroxyguanine	86-98	mutY DNA glycosylase	Homo sapiens	4-9
19836313-2	2009	The MUTYH glycosylase plays an important role in preventing mutations associated with 8-oxoguanine (OG) by removing adenine residues that have been misincorporated opposite OG.	8-hydroxyguanine	100-102	mutY DNA glycosylase	Homo sapiens	4-9
19836313-2	2009	The MUTYH glycosylase plays an important role in preventing mutations associated with 8-oxoguanine (OG) by removing adenine residues that have been misincorporated opposite OG.	Adenine	116-123	mutY DNA glycosylase	Homo sapiens	4-9
19836313-6	2009	Using these methods, the rate constants for steps involved in the adenine removal process were determined for the MAP variants Y165C, G382D, P391L and Q324R MUTYH.	Adenine	66-73	mutY DNA glycosylase	Homo sapiens	157-162
19836313-7	2009	Under single-turnover conditions, the rate of adenine removal for these four variants was found to be 30-40% of WT MUTYH.	Adenine	46-53	mutY DNA glycosylase	Homo sapiens	115-120
19836313-8	2009	In addition, the ability of MUTYH and the variants to suppress mutations and complement for the absence of MutY in Escherichia coli was assessed using rifampicin resistance assays.	Rifampin	151-161	mutY DNA glycosylase	Homo sapiens	28-33
19479711-2	2009	The human mutY homologue (MUTYH) excises adenine misincorporated opposite 8-OH-G during replication and suppresses mutations caused by reactive oxygen species.	Adenine	41-48	mutY DNA glycosylase	Homo sapiens	10-24
19479711-2	2009	The human mutY homologue (MUTYH) excises adenine misincorporated opposite 8-OH-G during replication and suppresses mutations caused by reactive oxygen species.	Adenine	41-48	mutY DNA glycosylase	Homo sapiens	26-31
19479711-2	2009	The human mutY homologue (MUTYH) excises adenine misincorporated opposite 8-OH-G during replication and suppresses mutations caused by reactive oxygen species.	8-oh-g	74-80	mutY DNA glycosylase	Homo sapiens	10-24
19479711-2	2009	The human mutY homologue (MUTYH) excises adenine misincorporated opposite 8-OH-G during replication and suppresses mutations caused by reactive oxygen species.	8-oh-g	74-80	mutY DNA glycosylase	Homo sapiens	26-31
19479711-2	2009	The human mutY homologue (MUTYH) excises adenine misincorporated opposite 8-OH-G during replication and suppresses mutations caused by reactive oxygen species.	Reactive Oxygen Species	135-158	mutY DNA glycosylase	Homo sapiens	10-24
19479711-2	2009	The human mutY homologue (MUTYH) excises adenine misincorporated opposite 8-OH-G during replication and suppresses mutations caused by reactive oxygen species.	Reactive Oxygen Species	135-158	mutY DNA glycosylase	Homo sapiens	26-31
19820168-0	2009	An 8-oxo-guanine repair pathway coordinated by MUTYH glycosylase and DNA polymerase lambda.	8-hydroxyguanine	3-16	mutY DNA glycosylase	Homo sapiens	47-52
19820168-4	2009	Here, we show by immunofluorescence experiments, in cells exposed to ROS, the involvement of MutY glycosylase homologue (MUTYH) and DNA pol lambda in the repair of A:8-oxo-G mispairs.	Reactive Oxygen Species	69-72	mutY DNA glycosylase	Homo sapiens	121-126
19443904-7	2009	The hMYH R260Q mutant had severe defect in adenine DNA glycosylase activity, whereas hMYH H434D could excise adenines from A:8oxoG pairs but not from A:G mispairs.	Adenine	109-117	mutY DNA glycosylase	Homo sapiens	4-8
19443904-7	2009	The hMYH R260Q mutant had severe defect in adenine DNA glycosylase activity, whereas hMYH H434D could excise adenines from A:8oxoG pairs but not from A:G mispairs.	Adenine	109-117	mutY DNA glycosylase	Homo sapiens	85-89