PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 22926731-3 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 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 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 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 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 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 21826668-8 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 11864576-0 2002 Replication-associated repair of adenine:8-oxoguanine mispairs by MYH. Adenine 33-40 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 11433026-1 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 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 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 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 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 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 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 11121482-1 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 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 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 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 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 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 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 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 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 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 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 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 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 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 30208271-5 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 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 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 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 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 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 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 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 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 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 26673696-2 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 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 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 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