897:
526:
enzymes responsible for the repair of the U:G mispairs caused by spontaneous cytosine deamination, whereas uracil arising in DNA through dU misincorporation is mainly dealt with by UNG. MBD4 is thought to correct T:G mismatches that arise from deamination of 5-methylcytosine to thymine in CpG sites. MBD4 mutant mice develop normally and do not show increased cancer susceptibility or reduced survival. But they acquire more C T mutations at CpG sequences in epithelial cells of the small intestine.
436:
1019:
3818:
3113:
543:
1152:
hypermethylation, and of the 145 DNA repair genes evaluated, NEIL1 had the most significantly different frequency of methylation. Furthermore, the hypermethylation corresponded to a decrease in NEIL1 mRNA expression. Further work with 135 tumor and 38 normal tissues also showed that 71% of HNSCC tissue samples had elevated NEIL1 promoter methylation.
2657:
Tricarico R, Cortellino S, Riccio A, Jagmohan-Changur S, Van der Klift H, Wijnen J, Turner D, Ventura A, Rovella V, Percesepe A, Lucci-Cordisco E, Radice P, Bertario L, Pedroni M, Ponz de Leon M, Mancuso P, Devarajan K, Cai KQ, Klein-Szanto AJ, Neri G, Møller P, Viel A, Genuardi M, Fodde R, Bellacosa
925:
recognizes adenine mispaired with 8-oxoG but excises the A, leaving the 8-oxoG intact. OGG1 knockout mice do not show an increased tumor incidence, but accumulate 8-oxoG in the liver as they age. A similar phenotype is observed with the inactivation of MYH, but simultaneous inactivation of both MYH
2362:
Osorio, A; Milne, R. L.; Kuchenbaecker, K; VaclovĂĄ, T; Pita, G; Alonso, R; Peterlongo, P; Blanco, I; de la Hoya, M; Duran, M; DĂez, O; RamĂłn y Cajal, T; Konstantopoulou, I; MartĂnez-Bouzas, C; AndrĂŠs
Conejero, R; Soucy, P; McGuffog, L; Barrowdale, D; Lee, A; Swe-Brca; Arver, B; Rantala, J; Loman, N;
525:
bearing an oxidized group at ring C5. TDG and MBD4 are strictly specific for double-stranded DNA. TDG can remove thymine glycol when present opposite guanine, as well as derivatives of U with modifications at carbon 5. Current evidence suggests that, in human cells, TDG and SMUG1 are the major
102:
of a DNA glycosylase was obtained for E. coli Nth. This structure revealed that the enzyme flips the damaged base out of the double helix into an active site pocket in order to excise it. Other glycosylases have since been found to follow the same general paradigm, including human UNG pictured
2291:
Russo, Maria Teresa; De Luca, Gabriele; Degan, Paolo; Parlanti, Eleonora; Dogliotti, Eugenia; Barnes, Deborah E.; Lindahl, Tomas; Yang, Hanjing; Miller, Jeffrey H.; Bignami, Margherita; et al. (2004). "Accumulation of the
Oxidative Base Lesion 8-Hydroxyguanine in DNA of Tumor-Prone Mice
1148:, though the mechanism of reduction was not known. This study also found that 4% of gastric cancers had mutations in the NEIL1 gene. The authors suggested that low NEIL1 activity arising from reduced expression and/or mutation of the NEIL1 gene was often involved in gastric carcinogenesis.
1106:
Nei-like (NEIL) 1 is a DNA glycosylase of the Nei family (which also contains NEIL2 and NEIL3). NEIL1 is a component of the DNA replication complex needed for surveillance of oxidized bases before replication, and appears to act as a âcowcatcherâ to slow replication until NEIL1 can act as a
1151:
A screen of 145 DNA repair genes for aberrant promoter methylation was performed on head and neck squamous cell carcinoma (HNSCC) tissues from 20 patients and from head and neck mucosa samples from 5 non-cancer patients. This screen showed that the NEIL1 gene had substantially increased
90:. β-Elimination of an AP site by a glycosylase-lyase yields a 3' ι,β-unsaturated aldehyde adjacent to a 5' phosphate, which differs from the AP endonuclease cleavage product. Some glycosylase-lyases can further perform δ-elimination, which converts the 3' aldehyde to a 3' phosphate.
529:
The structure of human UNG in complex with DNA revealed that, like other glycosylases, it flips the target nucleotide out of the double helix and into the active site pocket. UDG undergoes a conformational change from an ââopenââ unbound state to a ââclosedââ DNA-bound state.
912:
A variety of glycosylases have evolved to recognize oxidized bases, which are commonly formed by reactive oxygen species generated during cellular metabolism. The most abundant lesions formed at guanine residues are 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and
735:. The polypeptide topology of UDG is that of a classic alpha/beta protein. The structure consists primarily of a central, four-stranded, all parallel beta sheet surrounded on either side by a total of eight alpha helices and is termed a parallel doubly wound beta sheet.
1159:(NSCLC) tumors, 42% were hypermethylated in the NEIL1 promoter region. This was the most frequent DNA repair abnormality found among the 8 DNA repair genes tested. NEIL1 was also one of six DNA repair genes found to be hypermethylated in their promoter regions in
1048:
single base pair mutations in human cancers occur in CpG dinucleotides and are the result of G:C to A:T transitions. These transitions comprise the most frequent mutations in human cancer. For example, nearly 50% of somatic mutations of the tumor suppressor gene
1141:. NEIL1 is also capable of removing lesions from single-stranded DNA as well as from bubble and forked DNA structures. A deficiency in NEIL1 causes increased mutagenesis at the site of an 8-oxo-Gua:C pair, with most mutations being G:C to T:A transversions.
521:. They vary in substrate specificity and subcellular localization. SMUG1 prefers single-stranded DNA as substrate, but also removes U from double-stranded DNA. In addition to unmodified uracil, SMUG1 can excise 5-hydroxyuracil, 5-hydroxymethyluracil and
103:
below. To cleave the N-glycosidic bond, monofunctional glycosylases use an activated water molecule to attack carbon 1 of the substrate. Bifunctional glycosylases, instead, use an amine residue as a nucleophile to attack the same carbon, going through a
69:
and other plants by active demethylation. 5-methylcytosine residues are excised and replaced with unmethylated cytosines allowing access to the chromatin structure of the enzymes and proteins necessary for transcription and subsequent translation.
44:
are removed and replaced. DNA glycosylases catalyze the first step of this process. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an
60:
Glycosylases were first discovered in bacteria, and have since been found in all kingdoms of life. In addition to their role in base excision repair, DNA glycosylase enzymes have been implicated in the repression of gene silencing in
999:
alterations (epimutations) in DNA glycosylase genes have only recently begun to be evaluated in a few cancers, compared to the numerous previous studies of epimutations in genes acting in other DNA repair pathways (such as
3059:
Farkas SA, Vymetalkova V, Vodickova L, Vodicka P, Nilsson TK (Apr 2014). "DNA methylation changes in genes frequently mutated in sporadic colorectal cancer and in the DNA repair and Wnt/β-catenin signaling pathway genes".
505:. The prototypical member of this family is E. coli UDG, which was among the first glycosylases discovered. Four different uracil-DNA glycosylase activities have been identified in mammalian cells, including
917:. Due to mispairing with adenine during replication, 8-oxoG is highly mutagenic, resulting in G to T transversions. Repair of this lesion is initiated by the bifunctional DNA glycosylase
78:
There are two main classes of glycosylases: monofunctional and bifunctional. Monofunctional glycosylases have only glycosylase activity, whereas bifunctional glycosylases also possess
137:
A wide variety of glycosylases have evolved to recognize different damaged bases. The table below summarizes the properties of known glycosylases in commonly studied model organisms.
2327:
Moe E, Hall DR, Leiros I, Monsen VT, Timmins J, McSweeney S (2012). "Structure-function studies of an unusual 3-methyladenine DNA glycosylase II (AlkA) from
Deinococcus radiodurans".
3177:
2864:
Suzuki T, Harashima H, Kamiya H (2010). "Effects of base excision repair proteins on mutagenesis by 8-oxo-7,8-dihydroguanine (8-hydroxyguanine) paired with cytosine and adenine".
2710:
Xiong XD, Luo XP, Liu X, Jing X, Zeng LQ, Lei M, Hong XS, Chen Y (2012). "The MBD4 Glu346Lys polymorphism is associated with the risk of cervical cancer in a
Chinese population".
1944:
Slupphaug G, Mol CD, Kavli B, Arvai AS, Krokan HE, Tainer JA. (1996). A nucleotide-flipping mechanism from the structure of human uracilâDNA glycosylase bound to DNA. 384: 87-92.
2961:
Chaisaingmongkol J, Popanda O, Warta R, Dyckhoff G, Herpel E, Geiselhart L, Claus R, Lasitschka F, Campos B, Oakes CC, Bermejo JL, Herold-Mende C, Plass C, Schmezer P (2012).
954:
This group includes E. coli AlkA and related proteins in higher eukaryotes. These glycosylases are monofunctional and recognize methylated bases, such as 3-methyladenine.
926:
and OGG1 causes 8-oxoG accumulation in multiple tissues including lung and small intestine. In humans, mutations in MYH are associated with increased risk of developing
666:
2416:"Solution structure and intramolecular exchange of methyl-cytosine binding domain protein 4 (MBD4) on DNA suggests a mechanism to scan for mCpG/TpG mismatches"
1037:
to thymine, producing G:U and G:T base pairs. If the improper uracils or thymines in these base pairs are not removed before DNA replication, they will cause
1079:
A majority of histologically normal fields surrounding neoplastic growths (adenomas and colon cancers) in the colon also show reduced MBD4 mRNA expression (a
1044:. MBD4 specifically catalyzes the removal of T and U paired with guanine (G) within CpG sites. This is an important repair function since about 1/3 of all
884:
There are two UDG families, named Family 1 and Family 2. Family 1 is active against uracil in ssDNA and dsDNA. Family 2 excise uracil from mismatches with
1029:(methyl-CpG-binding domain protein 4) is a glycosylase employed in an initial step of base excision repair. MBD4 protein binds preferentially to fully
1373:
Kuo CF, McRee DE, Fisher CL, O'Handley SF, Cunningham RP, Tainer JA (October 1992). "Atomic structure of the DNA repair enzyme endonuclease III".
1788:"Mismatch repair in methylated DNA. Structure and activity of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4"
494:
uracil-DNA glycosylase, G:T/U mismatch-specific DNA glycosylase (Mug), and single-strand selective monofunctional uracil-DNA glycosylase (SMUG1).
3489:
2181:
Savva R, McAuley-Hecht K, Brown T, Pearl L (February 1995). "The structural basis of specific base-excision repair by uracil-DNA glycosylase".
1954:
Kavli B, Otterlei M, Slupphaug G, Krokan HE (April 2007). "Uracil in DNA--general mutagen, but normal intermediate in acquired immunity".
2963:"Epigenetic screen of human DNA repair genes identifies aberrant promoter methylation of NEIL1 in head and neck squamous cell carcinoma"
3155:
2758:"Prereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins"
1459:"Biochemical characterization and DNA repair pathway interactions of Mag1-mediated base excision repair in Schizosaccharomyces pombe"
1083:) compared to histologically normal tissue from individuals who never had a colonic neoplasm. This finding suggests that epigenetic
946:. These are homologous to bacterial Nei, and their presence likely explains the mild phenotypes of the OGG1 and MYH knockout mice.
921:, which recognizes 8-oxoG paired with C. hOGG1 is a bifunctional glycosylase that belongs to the helix-hairpin-helix (HhH) family.
1098:
was associated with about a 50% reduced risk of cervical cancer, suggesting that alterations in MBD4 is important in this cancer.
1005:
255:
227:
118:
of many glycosylases have been solved. Based on structural similarity, glycosylases are grouped into four superfamilies. The
1199:
602:
1304:"Identification of tobacco genes encoding proteins possessing removal activity of 5-methylcytosines from intact tobacco DNA"
686:
501:
from DNA, which can arise either by spontaneous deamination of cytosine or by the misincorporation of dU opposite dA during
2608:
Howard JH, Frolov A, Tzeng CW, Stewart A, Midzak A, Majmundar A, Godwin A, Heslin M, Bellacosa A, Arnoletti JP (Jan 2009).
2365:"DNA Glycosylases Involved in Base Excision Repair May Be Associated with Cancer Risk in BRCA1 and BRCA2 Mutation Carriers"
1649:"Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions"
1551:"Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis"
2232:
Klungland A; Rosewell I; Hollenbach S; Larsen E; Daly G; Epe A; Seeberg E; Lindahl T; Barnes D. E.; et al. (1999).
1008:
in direct reversal). Two examples of epimutations in DNA glycosylase genes that occur in cancers are summarized below.
963:
3537:
1989:
Hagen L; PeĂąa-Diaz J; Kavli B; Otterlei M; Slupphaug G; Krokan HE (August 2006). "Genomic uracil and human disease".
3117:
3419:
2363:
Ehrencrona, H; Olopade, O. I.; Beattie, M. S.; Domchek, S. M.; Nathanson, K; Rebbeck, T. R.; et al. (2014).
1057:
are G:C to A:T transitions within CpG sites. Thus, a decrease in expression of MBD4 could cause an increase in
3148:
1095:
819:
2659:
1600:"Thermostable uracil-DNA glycosylase from Thermotoga maritima a member of a novel class of DNA repair enzymes"
1033:. These altered bases arise from the frequent hydrolysis of cytosine to uracil (see image) and hydrolysis of
674:
3693:
3431:
1845:
Wong E; Yang K; Kuraguchi M; Werling U; Avdievich E; Fan K; Fazzari M; Jin B; Brown M.C; et al. (1995).
1156:
1030:
2024:
Slupphaug G, Markussen FH, Olsen LC, Aasland R, Aarsaether N, Bakke O, Krokan HE, Helland DE (June 1993).
3278:
869:
3808:
1138:
670:
1739:"Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase"
3794:
3781:
3768:
3755:
3742:
3729:
3716:
3678:
3141:
1786:
Wu, Peiying; Qiu, Chen; Sohail, Anjum; Zhang, Xing; Bhagwat, Ashok S.; Cheng, Xiaodong (2003-02-14).
622:
615:
2756:
Hegde ML, Hegde PM, Bellot LJ, Mandal SM, Hazra TK, Li GM, Boldogh I, Tomkinson AE, Mitra S (2013).
1847:"Mbd4 inactivation increases CâT transition mutations and promotes gastrointestinal tumor formation"
1229:
627:
3838:
3688:
3642:
3585:
3168:
3127:
3004:"A critical re-assessment of DNA repair gene promoter methylation in non-small cell lung carcinoma"
160:
33:
3590:
3341:
514:
2234:"Accumulation of premutagenic DNA lesions in mice defective in removal of oxidative base damage"
1338:
Fromme JC, Banerjee A, Verdine GL (February 2004). "DNA glycosylase recognition and catalysis".
3504:
3249:
2465:"Role of base excision repair in maintaining the genetic and epigenetic integrity of CpG sites"
865:
506:
452:
2917:
Shinmura K, Tao H, Goto M, Igarashi H, Taniguchi T, Maekawa M, Takezaki T, Sugimura H (2004).
2026:"Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene"
1137:
lesions, guanidinohydantoin, and spiroiminodihydantoin that are further oxidation products of
3611:
3530:
2610:"Epigenetic downregulation of the DNA repair gene MED1/MBD4 in colorectal and ovarian cancer"
1038:
3123:
1076:
region of MBD4. Also MBD4 is deficient due to mutation in about 4% of colorectal cancers,
896:
3683:
3463:
3414:
3015:
2769:
2245:
2190:
2135:
1382:
1256:
976:
755:
653:
427:
DNA glycosylases can be grouped into the following categories based on their substrate(s):
37:
29:
1144:
A study in 2004 found that 46% of primary gastric cancers had reduced expression of NEIL1
8:
3843:
3647:
3358:
3346:
3181:
2075:"Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme"
1647:
Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH (January 1998).
858:
751:
732:
83:
3019:
2773:
2249:
2194:
2139:
1386:
1260:
3580:
3402:
3397:
3375:
3363:
3202:
3133:
3036:
3003:
2919:"Inactivating mutations of the human base excision repair gene NEIL1 in gastric cancer"
2899:
2841:
2816:
2792:
2757:
2735:
2687:
2634:
2609:
2587:
2562:
Cooper DN, Youssoufian H (Feb 1988). "The CpG dinucleotide and human genetic disease".
2539:
2518:
2489:
2464:
2440:
2415:
2391:
2364:
2214:
2090:
1927:
1822:
1787:
1678:
1629:
1580:
1279:
1244:
1217:
1069:
934:. In addition to OGG1 and MYH, human cells contain three additional DNA glycosylases,
851:
815:
811:
2099:
2074:
2050:
2025:
1873:
1846:
1763:
1738:
1714:
1697:
1665:
1648:
1616:
1599:
1524:
1483:
1458:
1320:
1303:
1065:
719:
The function of UDG is to remove mutations in DNA, more specifically removing uracil.
3848:
3370:
3244:
3077:
3041:
2984:
2940:
2903:
2891:
2846:
2797:
2727:
2692:
2639:
2579:
2544:
2494:
2445:
2396:
2344:
2309:
2273:
2268:
2233:
2206:
2163:
2158:
2123:
2104:
2055:
2006:
1971:
1919:
1914:
1897:
1878:
1827:
1809:
1768:
1719:
1670:
1621:
1572:
1567:
1550:
1549:
Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, Krokan HE, Tainer JA (March 1995).
1528:
1511:
Pearl LH (2000). "Structure and function in the uracil-DNA glycosylase superfamily".
1488:
1439:
1398:
1355:
1284:
1205:
1195:
1160:
1054:
661:
607:
50:
2832:
2591:
1931:
1633:
1584:
571:
486:
This entry represents various uracil-DNA glycosylases and related DNA glycosylases (
3626:
3621:
3595:
3523:
3380:
3266:
3069:
3031:
3023:
2974:
2930:
2881:
2873:
2836:
2828:
2787:
2777:
2719:
2682:
2674:
2629:
2621:
2571:
2534:
2526:
2484:
2476:
2435:
2427:
2386:
2376:
2336:
2301:
2263:
2253:
2218:
2198:
2153:
2143:
2094:
2086:
2045:
2037:
1998:
1963:
1909:
1868:
1858:
1817:
1799:
1758:
1750:
1709:
1682:
1660:
1611:
1562:
1520:
1478:
1470:
1429:
1390:
1347:
1315:
1274:
1264:
1187:
1034:
927:
649:
440:
2739:
2519:"MBD4 and TDG: multifaceted DNA glycosylases with ever expanding biological roles"
2305:
1698:"The cap-binding protein complex in uninfected and poliovirus-infected HeLa cells"
3673:
3657:
3570:
3100:
2877:
2723:
2530:
2480:
2381:
1967:
1191:
1121:
via β,δ elimination, leaving 3Ⲡand 5Ⲡphosphate ends. NEIL1 recognizes oxidized
1080:
708:
583:
502:
115:
99:
87:
54:
2002:
1245:"Role of the Arabidopsis DNA glycosylase/lyase ROS1 in active DNA demethylation"
703:
Lindahl was the first to observe repair of uracil in DNA. UDG was purified from
3822:
3711:
3652:
3441:
3353:
3190:
1896:
Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, Krokan HE, Tainer JA (1995).
1737:
Matsubara M, Tanaka T, Terato H, Ohmae E, Izumi S, Katayanagi K, Ide H (2004).
1130:
1088:
1084:
1058:
522:
2340:
1351:
3832:
3616:
3575:
3387:
3316:
3299:
2678:
2660:"Involvement of MBD4 inactivation in mismatch repair-deficient tumorigenesis"
2258:
2041:
1813:
1179:
1145:
1114:
1073:
855:
843:
839:
827:
795:
3002:
Do H, Wong NC, Murone C, John T, Solomon B, Mitchell PL, Dobrovic A (2014).
2935:
2918:
2817:"Variant base excision repair proteins: contributors to genomic instability"
2782:
2148:
1394:
1269:
762:
to form mutagenic U:G mispairs, or through the incorporation of dUMP by DNA
3565:
3231:
3081:
3045:
2988:
2944:
2895:
2850:
2801:
2731:
2696:
2643:
2548:
2498:
2449:
2400:
2348:
2313:
2277:
2010:
1975:
1898:"Crystal structure and mutational analysis of human uracil-DNA glycosylase"
1882:
1863:
1831:
1804:
1772:
1625:
1532:
1492:
1443:
1359:
1288:
943:
931:
914:
799:
791:
787:
783:
491:
2583:
2210:
2167:
2108:
2059:
1923:
1723:
1674:
1576:
1418:"Human DNA glycosylases involved in the repair of oxidatively damaged DNA"
1402:
1209:
611:
435:
3789:
3724:
3560:
3458:
3424:
3392:
2979:
2962:
2656:
2625:
2431:
2231:
1754:
1474:
996:
464:
104:
547:
EpsteinâBarr virus uracil-dna glycosylase in complex with ugi from pbs-2
341:
U, hoU(5-hydroxyuracil), hmU(5-hydroxymethyluracil), fU(5-formyluracil)
3468:
3436:
2575:
2073:
Olsen LC, Aasland R, Wittwer CU, Krokan HE, Helland DE (October 1989).
1434:
1417:
1122:
835:
831:
823:
779:
763:
595:
476:
263:
Tg, hoU, hoC, urea, FapyG(2,6-diamino-4-hydroxy-5-formamidopyrimidine)
189:
53:
the damaged base out of the double helix followed by cleavage of the N-
3027:
2886:
3763:
3737:
3306:
3239:
3216:
3206:
3164:
3073:
2202:
2124:"Identification of a poxvirus gene encoding a uracil DNA glycosylase"
1134:
873:
767:
460:
154:
2960:
1018:
287:
Tg, hoU, hoC, urea, FapyG, FapyA(4,6-diamino-5-formamidopyrimidine)
3817:
3311:
3096:
1988:
1041:
830:. More distantly related uracil-DNA glycosylases are also found in
759:
758:
pathway. Uracil in DNA can arise either through the deamination of
578:
468:
79:
711:
connecting the base to the deoxyribose sugar of the DNA backbone.
3294:
3221:
3211:
3198:
3058:
1129:
residues oxidized at the methyl group, and both stereoisomers of
1126:
1118:
885:
847:
728:
590:
487:
448:
147:
46:
1844:
3776:
3546:
3112:
2361:
1094:
In a
Chinese population that was evaluated, the MBD4 Glu346Lys
1045:
748:
744:
681:
542:
498:
480:
472:
456:
86:
of DNA, creating a single-strand break without the need for an
73:
25:
2023:
3750:
3473:
3254:
1110:
984:
980:
939:
935:
922:
862:
510:
2180:
1953:
3451:
3446:
3407:
3336:
3331:
3326:
3321:
3271:
3259:
3092:
1646:
1372:
1026:
1012:
1001:
918:
754:
from DNA by cleaving the N-glycosydic bond, initiating the
643:
566:
518:
404:
233:
3515:
1736:
126:
families contain small, compact glycosylases, whereas the
2290:
2072:
1050:
41:
3163:
2607:
1133:. The best substrates for human NEIL1 appear to be the
850:
has not been directly demonstrated. The most N-terminal
134:
families comprise larger enzymes with multiple domains.
2916:
3091:
This article incorporates text from the public domain
2755:
2292:
Defective in Both the Myh and Ogg1 DNA Glycosylases".
1895:
1548:
1242:
3806:
2863:
2516:
1337:
1107:
glycosylase and remove the oxidatively damaged base.
991:
1064:
MBD4 expression is reduced in almost all colorectal
2956:
2954:
2326:
2121:
1597:
2814:
1457:Alseth I, Osman F, Korvald H, et al. (2005).
1456:
949:
2561:
1113:protein recognizes (targets) and removes certain
891:
475:. UDG repairs these mutations. UDG is crucial in
3830:
3001:
2951:
1785:
1695:
770:. These aberrant uracil residues are genotoxic.
2709:
2462:
1506:
1504:
1502:
1333:
1331:
3531:
3149:
1544:
1542:
439:Structure of the base-excision repair enzyme
2995:
2910:
2857:
2815:Nemec AA, Wallace SS, Sweasy JB (Oct 2010).
2808:
2703:
1982:
1947:
1591:
1301:
979:(BER) may be associated with cancer risk in
814:of uracil-DNA glycosylase is extremely well
74:Monofunctional vs. bifunctional glycosylases
3052:
2555:
2517:Sjolund AB, Senejani AG, Sweasy JB (2013).
2174:
2122:Upton C, Stuart DT, McFadden G (May 1993).
2115:
2066:
2017:
1689:
1640:
1499:
1450:
1409:
1328:
141:Glycosylases in bacteria, yeast and humans
40:is the mechanism by which damaged bases in
3538:
3524:
3156:
3142:
2512:
2510:
2508:
2413:
1539:
1366:
1182:(1986). "DNA Glycosylases in DNA Repair".
1155:When 8 DNA repair genes were evaluated in
541:
430:
3126:at the U.S. National Library of Medicine
3035:
2978:
2934:
2885:
2840:
2791:
2781:
2686:
2650:
2633:
2603:
2601:
2538:
2488:
2456:
2439:
2390:
2380:
2267:
2257:
2225:
2157:
2147:
2098:
2049:
1938:
1913:
1872:
1862:
1821:
1803:
1762:
1730:
1713:
1664:
1615:
1566:
1482:
1433:
1415:
1319:
1278:
1268:
782:cells, UNG activity is found in both the
479:, without it these mutations may lead to
2751:
2749:
1510:
1017:
895:
794:UNG1 protein is transported to both the
463:in DNA. The most common mutation is the
443:. The uracil residue is shown in yellow.
434:
110:
93:
18:Enzymes involved in base excision repair
2505:
1696:Buckley B, Ehrenfeld E (October 1987).
1598:Sandigursky M, Franklin WA (May 1999).
1243:Aguis, F.; Kapoor, A; Zhu, J-K (2006).
1178:
1087:of MBD4 is an early step in colorectal
743:Uracil-DNA glycosylases are DNA repair
3831:
2598:
82:activity that permits them to cut the
3519:
3137:
2746:
2284:
1340:Current Opinion in Structural Biology
1838:
1117:-damaged bases and then incises the
904:) in a Hoogsteen base pair with dA (
842:localization, but the presence of a
198:3-meA(3-alkyladenine), hypoxanthine
2463:Bellacosa A, Drohat AC (Aug 2015).
1889:
1792:The Journal of Biological Chemistry
1184:Mechanisms of DNA Damage and Repair
490:), such as uracil-DNA glycosylase,
13:
2091:10.1002/j.1460-2075.1989.tb08464.x
1779:
1186:. Vol. 38. pp. 335â340.
992:Epigenetic deficiencies in cancers
964:3-methyladenine DNA glycosylase II
861:which has been proposed, based on
14:
3860:
3105:
1321:10.5511/plantbiotechnology.24.339
192:(N-methylpurine DNA glycosylase)
3816:
3111:
1022:Hydrolysis of cytosine to uracil
838:of UNG1 seem to be required for
731:have a 3-layer alpha/beta/alpha
3420:Alpha-N-acetylgalactosaminidase
2833:10.1016/j.semcancer.2010.10.010
2407:
2355:
2320:
950:Glycosylases of alkylated bases
805:
773:
497:Uracil DNA glycosylases remove
1416:Ide H, Kotera M (April 2004).
1295:
1236:
1172:
892:Glycosylases of oxidized bases
1:
3432:Alpha-N-acetylglucosaminidase
2306:10.1158/0008-5472.can-04-0355
1715:10.1016/S0021-9258(19)76470-9
1666:10.1016/S0092-8674(00)80904-6
1617:10.1016/S0960-9822(99)80237-1
1525:10.1016/S0921-8777(00)00025-2
1302:Choi, C-S.; Sano, H. (2007).
1166:
975:DNA glycosylases involved in
638:Available protein structures:
241:8-oxoG (8-Oxoguanine), FapyG
2878:10.1016/j.dnarep.2010.02.004
2762:Proc. Natl. Acad. Sci. U.S.A
2724:10.1097/IGC.0b013e31826e22e4
2614:Cancer Biology & Therapy
2531:10.1016/j.mrfmmm.2012.11.001
2481:10.1016/j.dnarep.2015.04.011
2382:10.1371/journal.pgen.1004256
2128:Proc. Natl. Acad. Sci. U.S.A
1968:10.1016/j.dnarep.2006.10.014
1915:10.1016/0092-8674(95)90290-2
1568:10.1016/0092-8674(95)90290-2
1249:Proc. Natl. Acad. Sci. U.S.A
1192:10.1007/978-1-4615-9462-8_36
969:
738:
722:
707:, and this hydrolysed the N-
7:
3545:
2003:10.1016/j.yexcr.2006.06.015
714:
139:
49:. This is accomplished by
10:
3865:
3090:
2821:Seminars in Cancer Biology
2414:Walavalkar, Ninad (2014).
1157:non-small cell lung cancer
698:
447:In molecular biology, the
3702:
3694:MichaelisâMenten kinetics
3666:
3635:
3604:
3553:
3488:
3287:
3230:
3189:
3176:
2341:10.1107/S090744491200947X
1352:10.1016/j.sbi.2004.01.003
879:
680:
660:
642:
637:
633:
621:
601:
589:
577:
565:
557:
552:
540:
535:
283:
277:
272:
262:
259:
253:
245:
174:
171:
168:
159:
152:
145:
3586:Diffusion-limited enzyme
3128:Medical Subject Headings
2679:10.18632/oncotarget.5740
2259:10.1073/pnas.96.23.13300
1125:, formamidopyrimidines,
1101:
3342:Bacterial neuraminidase
2783:10.1073/pnas.1304231110
2712:Int. J. Gynecol. Cancer
2149:10.1073/pnas.90.10.4518
1395:10.1126/science.1411536
1270:10.1073/pnas.0603563103
1011:
1004:in mismatch repair and
957:
431:Uracil DNA glycosylases
3505:Oxoguanine glycosylase
2420:Nucleic Acids Research
2042:10.1093/nar/21.11.2579
1864:10.1073/pnas.232579299
1805:10.1074/jbc.M210884200
1023:
909:
453:Uracil-DNA glycosylase
444:
441:uracil-DNA glycosylase
3679:EadieâHofstee diagram
3612:Allosteric regulation
2936:10.1093/carcin/bgh267
1021:
899:
438:
111:Types of glycosylases
94:Biochemical mechanism
3689:LineweaverâBurk plot
3494:N-Glycosyl compounds
3464:Maltase-glucoamylase
3415:Galactosylceramidase
3182:Glycoside hydrolases
3167:: sugar hydrolases (
3120:at Wikimedia Commons
2980:10.1038/onc.2011.660
2626:10.4161/cbt.8.1.7469
1031:methylated CpG sites
977:base excision repair
834:. The N-terminal 77
756:base excision repair
38:Base excision repair
30:base excision repair
3347:Viral neuraminidase
3020:2014NatSR...4E4186D
2774:2013PNAS..110E3090H
2426:(17): 11218â11232.
2250:1999PNAS...9613300K
2244:(23): 13300â13305.
2195:1995Natur.373..487S
2140:1993PNAS...90.4518U
1857:(23): 14937â14942.
1387:1992Sci...258..434K
1308:Plant Biotechnology
1261:2006PNAS..10311796A
1255:(31): 11796â11801.
874:catalytic mechanism
854:region contains an
142:
84:phosphodiester bond
32:, classified under
3648:Enzyme superfamily
3581:Enzyme promiscuity
3398:Glucosylceramidase
3279:Debranching enzyme
3203:Sucrase-isomaltase
3008:Scientific Reports
2866:DNA Repair (Amst.)
2576:10.1007/bf00278187
2525:. 743â744: 12â25.
2432:10.1093/nar/gku782
2329:Acta Crystallogr D
1956:DNA Repair (Amst.)
1755:10.1093/nar/gkh859
1475:10.1093/nar/gki259
1435:10.1248/bpb.27.480
1024:
987:mutation carriers.
910:
445:
140:
116:Crystal structures
3804:
3803:
3513:
3512:
3484:
3483:
3371:alpha-Mannosidase
3245:Alpha-glucosidase
3116:Media related to
3028:10.1038/srep04186
2673:(40): 42892â904.
2523:Mutation Research
2300:(13): 4411â4414.
2030:Nucleic Acids Res
1749:(17): 5291â5302.
1743:Nucleic Acids Res
1708:(28): 13599â606.
1463:Nucleic Acids Res
1422:Biol. Pharm. Bull
1201:978-1-4615-9464-2
1161:colorectal cancer
1055:colorectal cancer
696:
695:
692:
691:
687:structure summary
425:
424:
100:crystal structure
3856:
3821:
3820:
3812:
3684:HanesâWoolf plot
3627:Enzyme activator
3622:Enzyme inhibitor
3596:Enzyme catalysis
3540:
3533:
3526:
3517:
3516:
3501:DNA glycosylases
3267:Beta-glucosidase
3187:
3186:
3158:
3151:
3144:
3135:
3134:
3124:DNA+Glycosylases
3115:
3086:
3085:
3074:10.2217/epi.14.7
3056:
3050:
3049:
3039:
2999:
2993:
2992:
2982:
2958:
2949:
2948:
2938:
2914:
2908:
2907:
2889:
2861:
2855:
2854:
2844:
2812:
2806:
2805:
2795:
2785:
2753:
2744:
2743:
2707:
2701:
2700:
2690:
2664:
2654:
2648:
2647:
2637:
2605:
2596:
2595:
2559:
2553:
2552:
2542:
2514:
2503:
2502:
2492:
2460:
2454:
2453:
2443:
2411:
2405:
2404:
2394:
2384:
2359:
2353:
2352:
2324:
2318:
2317:
2288:
2282:
2281:
2271:
2261:
2229:
2223:
2222:
2203:10.1038/373487a0
2189:(6514): 487â93.
2178:
2172:
2171:
2161:
2151:
2119:
2113:
2112:
2102:
2070:
2064:
2063:
2053:
2021:
2015:
2014:
1986:
1980:
1979:
1951:
1945:
1942:
1936:
1935:
1917:
1893:
1887:
1886:
1876:
1866:
1842:
1836:
1835:
1825:
1807:
1798:(7): 5285â5291.
1783:
1777:
1776:
1766:
1734:
1728:
1727:
1717:
1693:
1687:
1686:
1668:
1644:
1638:
1637:
1619:
1595:
1589:
1588:
1570:
1546:
1537:
1536:
1508:
1497:
1496:
1486:
1454:
1448:
1447:
1437:
1413:
1407:
1406:
1381:(5081): 434â40.
1370:
1364:
1363:
1335:
1326:
1325:
1323:
1299:
1293:
1292:
1282:
1272:
1240:
1234:
1233:
1227:
1223:
1221:
1213:
1176:
1035:5-methylcytosine
705:Escherichia coli
635:
634:
545:
533:
532:
143:
24:are a family of
22:DNA glycosylases
3864:
3863:
3859:
3858:
3857:
3855:
3854:
3853:
3839:Protein domains
3829:
3828:
3827:
3815:
3807:
3805:
3800:
3712:Oxidoreductases
3698:
3674:Enzyme kinetics
3662:
3658:List of enzymes
3631:
3600:
3571:Catalytic triad
3549:
3544:
3514:
3509:
3493:
3480:
3283:
3226:
3172:
3162:
3118:DNA-glycosylase
3108:
3103:
3089:
3057:
3053:
3000:
2996:
2973:(49): 5108â16.
2959:
2952:
2915:
2911:
2862:
2858:
2813:
2809:
2768:(33): E3090â9.
2754:
2747:
2708:
2704:
2662:
2655:
2651:
2606:
2599:
2560:
2556:
2515:
2506:
2461:
2457:
2412:
2408:
2375:(4): e1004256.
2360:
2356:
2325:
2321:
2289:
2285:
2230:
2226:
2179:
2175:
2134:(10): 4518â22.
2120:
2116:
2071:
2067:
2036:(11): 2579â84.
2022:
2018:
1997:(14): 2666â72.
1987:
1983:
1952:
1948:
1943:
1939:
1894:
1890:
1843:
1839:
1784:
1780:
1735:
1731:
1694:
1690:
1645:
1641:
1596:
1592:
1547:
1540:
1519:(3â4): 165â81.
1509:
1500:
1455:
1451:
1414:
1410:
1371:
1367:
1336:
1329:
1300:
1296:
1241:
1237:
1225:
1224:
1215:
1214:
1202:
1177:
1173:
1169:
1104:
1016:
994:
972:
962:AlkA refers to
960:
952:
894:
882:
808:
776:
741:
725:
717:
709:glycosidic bond
701:
548:
503:DNA replication
433:
418:monofunctional
396:monofunctional
376:monofunctional
357:monofunctional
338:monofunctional
319:monofunctional
214:monofunctional
195:monofunctional
113:
96:
88:AP endonuclease
76:
55:glycosidic bond
19:
12:
11:
5:
3862:
3852:
3851:
3846:
3841:
3826:
3825:
3802:
3801:
3799:
3798:
3785:
3772:
3759:
3746:
3733:
3720:
3706:
3704:
3700:
3699:
3697:
3696:
3691:
3686:
3681:
3676:
3670:
3668:
3664:
3663:
3661:
3660:
3655:
3650:
3645:
3639:
3637:
3636:Classification
3633:
3632:
3630:
3629:
3624:
3619:
3614:
3608:
3606:
3602:
3601:
3599:
3598:
3593:
3588:
3583:
3578:
3573:
3568:
3563:
3557:
3555:
3551:
3550:
3543:
3542:
3535:
3528:
3520:
3511:
3510:
3508:
3507:
3497:
3495:
3486:
3485:
3482:
3481:
3479:
3478:
3477:
3476:
3466:
3461:
3456:
3455:
3454:
3449:
3442:Hexosaminidase
3439:
3434:
3429:
3428:
3427:
3417:
3412:
3411:
3410:
3405:
3395:
3390:
3385:
3384:
3383:
3373:
3368:
3367:
3366:
3361:
3354:Galactosidases
3351:
3350:
3349:
3344:
3339:
3334:
3329:
3324:
3314:
3309:
3304:
3303:
3302:
3291:
3289:
3285:
3284:
3282:
3281:
3276:
3275:
3274:
3264:
3263:
3262:
3257:
3252:
3242:
3236:
3234:
3228:
3227:
3225:
3224:
3219:
3214:
3209:
3195:
3193:
3191:Disaccharidase
3184:
3174:
3173:
3161:
3160:
3153:
3146:
3138:
3132:
3131:
3121:
3107:
3106:External links
3104:
3088:
3087:
3051:
2994:
2950:
2929:(12): 2311â7.
2923:Carcinogenesis
2909:
2856:
2807:
2745:
2702:
2658:A (Oct 2015).
2649:
2597:
2564:Human Genetics
2554:
2504:
2455:
2406:
2354:
2319:
2283:
2224:
2173:
2114:
2085:(10): 3121â5.
2065:
2016:
1981:
1946:
1937:
1908:(6): 869â878.
1888:
1837:
1778:
1729:
1688:
1639:
1590:
1538:
1498:
1469:(3): 1123â31.
1449:
1408:
1365:
1327:
1314:(3): 339â344.
1294:
1235:
1226:|journal=
1200:
1170:
1168:
1165:
1131:thymine glycol
1103:
1100:
1089:carcinogenesis
1015:
1010:
993:
990:
989:
988:
971:
968:
959:
956:
951:
948:
893:
890:
881:
878:
828:herpes viruses
826:as well as in
807:
804:
775:
772:
740:
737:
724:
721:
716:
713:
700:
697:
694:
693:
690:
689:
684:
678:
677:
664:
658:
657:
647:
640:
639:
631:
630:
625:
619:
618:
605:
599:
598:
593:
587:
586:
581:
575:
574:
569:
563:
562:
559:
555:
554:
550:
549:
546:
538:
537:
523:5-formyluracil
432:
429:
423:
422:
419:
416:
413:
410:
407:
401:
400:
397:
394:
391:
388:
385:
381:
380:
377:
374:
371:
368:
366:
362:
361:
358:
355:
352:
349:
347:
343:
342:
339:
336:
333:
330:
328:
324:
323:
320:
317:
314:
311:
309:
305:
304:
301:
297:
296:
293:
289:
288:
285:
282:
279:
276:
274:
270:
269:
265:
264:
261:
258:
252:
249:
247:
243:
242:
239:
236:
230:
225:
223:
219:
218:
215:
212:
209:
206:
204:
200:
199:
196:
193:
187:
184:
181:
177:
176:
173:
170:
167:
158:
151:
112:
109:
107:intermediate.
95:
92:
75:
72:
17:
9:
6:
4:
3:
2:
3861:
3850:
3847:
3845:
3842:
3840:
3837:
3836:
3834:
3824:
3819:
3814:
3813:
3810:
3796:
3792:
3791:
3786:
3783:
3779:
3778:
3773:
3770:
3766:
3765:
3760:
3757:
3753:
3752:
3747:
3744:
3740:
3739:
3734:
3731:
3727:
3726:
3721:
3718:
3714:
3713:
3708:
3707:
3705:
3701:
3695:
3692:
3690:
3687:
3685:
3682:
3680:
3677:
3675:
3672:
3671:
3669:
3665:
3659:
3656:
3654:
3653:Enzyme family
3651:
3649:
3646:
3644:
3641:
3640:
3638:
3634:
3628:
3625:
3623:
3620:
3618:
3617:Cooperativity
3615:
3613:
3610:
3609:
3607:
3603:
3597:
3594:
3592:
3589:
3587:
3584:
3582:
3579:
3577:
3576:Oxyanion hole
3574:
3572:
3569:
3567:
3564:
3562:
3559:
3558:
3556:
3552:
3548:
3541:
3536:
3534:
3529:
3527:
3522:
3521:
3518:
3506:
3502:
3499:
3498:
3496:
3492:: Hydrolysing
3491:
3487:
3475:
3472:
3471:
3470:
3467:
3465:
3462:
3460:
3457:
3453:
3450:
3448:
3445:
3444:
3443:
3440:
3438:
3435:
3433:
3430:
3426:
3423:
3422:
3421:
3418:
3416:
3413:
3409:
3408:non-lysosomal
3406:
3404:
3401:
3400:
3399:
3396:
3394:
3391:
3389:
3388:Hyaluronidase
3386:
3382:
3379:
3378:
3377:
3376:Glucuronidase
3374:
3372:
3369:
3365:
3362:
3360:
3357:
3356:
3355:
3352:
3348:
3345:
3343:
3340:
3338:
3335:
3333:
3330:
3328:
3325:
3323:
3320:
3319:
3318:
3317:Neuraminidase
3315:
3313:
3310:
3308:
3305:
3301:
3300:Alpha-amylase
3298:
3297:
3296:
3293:
3292:
3290:
3286:
3280:
3277:
3273:
3270:
3269:
3268:
3265:
3261:
3258:
3256:
3253:
3251:
3248:
3247:
3246:
3243:
3241:
3238:
3237:
3235:
3233:
3229:
3223:
3220:
3218:
3215:
3213:
3210:
3208:
3204:
3200:
3197:
3196:
3194:
3192:
3188:
3185:
3183:
3179:
3175:
3170:
3166:
3159:
3154:
3152:
3147:
3145:
3140:
3139:
3136:
3129:
3125:
3122:
3119:
3114:
3110:
3109:
3102:
3098:
3094:
3083:
3079:
3075:
3071:
3068:(2): 179â91.
3067:
3063:
3055:
3047:
3043:
3038:
3033:
3029:
3025:
3021:
3017:
3013:
3009:
3005:
2998:
2990:
2986:
2981:
2976:
2972:
2968:
2964:
2957:
2955:
2946:
2942:
2937:
2932:
2928:
2924:
2920:
2913:
2905:
2901:
2897:
2893:
2888:
2883:
2879:
2875:
2872:(5): 542â50.
2871:
2867:
2860:
2852:
2848:
2843:
2838:
2834:
2830:
2826:
2822:
2818:
2811:
2803:
2799:
2794:
2789:
2784:
2779:
2775:
2771:
2767:
2763:
2759:
2752:
2750:
2741:
2737:
2733:
2729:
2725:
2721:
2718:(9): 1552â6.
2717:
2713:
2706:
2698:
2694:
2689:
2684:
2680:
2676:
2672:
2668:
2661:
2653:
2645:
2641:
2636:
2631:
2627:
2623:
2620:(1): 94â100.
2619:
2615:
2611:
2604:
2602:
2593:
2589:
2585:
2581:
2577:
2573:
2569:
2565:
2558:
2550:
2546:
2541:
2536:
2532:
2528:
2524:
2520:
2513:
2511:
2509:
2500:
2496:
2491:
2486:
2482:
2478:
2474:
2470:
2466:
2459:
2451:
2447:
2442:
2437:
2433:
2429:
2425:
2421:
2417:
2410:
2402:
2398:
2393:
2388:
2383:
2378:
2374:
2370:
2369:PLOS Genetics
2366:
2358:
2350:
2346:
2342:
2338:
2335:(6): 703â12.
2334:
2330:
2323:
2315:
2311:
2307:
2303:
2299:
2295:
2287:
2279:
2275:
2270:
2265:
2260:
2255:
2251:
2247:
2243:
2239:
2235:
2228:
2220:
2216:
2212:
2208:
2204:
2200:
2196:
2192:
2188:
2184:
2177:
2169:
2165:
2160:
2155:
2150:
2145:
2141:
2137:
2133:
2129:
2125:
2118:
2110:
2106:
2101:
2096:
2092:
2088:
2084:
2080:
2076:
2069:
2061:
2057:
2052:
2047:
2043:
2039:
2035:
2031:
2027:
2020:
2012:
2008:
2004:
2000:
1996:
1992:
1991:Exp. Cell Res
1985:
1977:
1973:
1969:
1965:
1962:(4): 505â16.
1961:
1957:
1950:
1941:
1933:
1929:
1925:
1921:
1916:
1911:
1907:
1903:
1899:
1892:
1884:
1880:
1875:
1870:
1865:
1860:
1856:
1852:
1848:
1841:
1833:
1829:
1824:
1819:
1815:
1811:
1806:
1801:
1797:
1793:
1789:
1782:
1774:
1770:
1765:
1760:
1756:
1752:
1748:
1744:
1740:
1733:
1725:
1721:
1716:
1711:
1707:
1703:
1702:J. Biol. Chem
1699:
1692:
1684:
1680:
1676:
1672:
1667:
1662:
1659:(1): 117â29.
1658:
1654:
1650:
1643:
1635:
1631:
1627:
1623:
1618:
1613:
1610:(10): 531â4.
1609:
1605:
1601:
1594:
1586:
1582:
1578:
1574:
1569:
1564:
1561:(6): 869â78.
1560:
1556:
1552:
1545:
1543:
1534:
1530:
1526:
1522:
1518:
1514:
1507:
1505:
1503:
1494:
1490:
1485:
1480:
1476:
1472:
1468:
1464:
1460:
1453:
1445:
1441:
1436:
1431:
1427:
1423:
1419:
1412:
1404:
1400:
1396:
1392:
1388:
1384:
1380:
1376:
1369:
1361:
1357:
1353:
1349:
1345:
1341:
1334:
1332:
1322:
1317:
1313:
1309:
1305:
1298:
1290:
1286:
1281:
1276:
1271:
1266:
1262:
1258:
1254:
1250:
1246:
1239:
1231:
1219:
1211:
1207:
1203:
1197:
1193:
1189:
1185:
1181:
1175:
1171:
1164:
1162:
1158:
1153:
1149:
1147:
1142:
1140:
1136:
1132:
1128:
1124:
1120:
1116:
1112:
1108:
1099:
1097:
1092:
1090:
1086:
1082:
1077:
1075:
1071:
1067:
1062:
1060:
1056:
1052:
1047:
1043:
1040:
1036:
1032:
1028:
1020:
1014:
1009:
1007:
1003:
998:
986:
982:
978:
974:
973:
967:
965:
955:
947:
945:
941:
937:
933:
929:
924:
920:
916:
907:
903:
898:
889:
887:
877:
875:
871:
867:
864:
860:
857:
856:aspartic acid
853:
849:
845:
844:mitochondrial
841:
840:mitochondrial
837:
833:
829:
825:
821:
817:
813:
803:
801:
797:
793:
789:
785:
781:
771:
769:
765:
761:
757:
753:
750:
746:
736:
734:
730:
720:
712:
710:
706:
688:
685:
683:
679:
676:
672:
668:
665:
663:
659:
655:
651:
648:
645:
641:
636:
632:
629:
626:
624:
620:
617:
613:
609:
606:
604:
600:
597:
594:
592:
588:
585:
582:
580:
576:
573:
570:
568:
564:
560:
556:
551:
544:
539:
534:
531:
527:
524:
520:
516:
512:
508:
504:
500:
495:
493:
489:
484:
482:
478:
474:
470:
466:
462:
459:that reverts
458:
454:
450:
442:
437:
428:
420:
417:
414:
411:
408:
406:
403:
402:
398:
395:
392:
389:
386:
383:
382:
378:
375:
372:
369:
367:
364:
363:
359:
356:
353:
350:
348:
345:
344:
340:
337:
334:
331:
329:
326:
325:
321:
318:
315:
312:
310:
307:
306:
302:
299:
298:
295:AP site, hoU
294:
291:
290:
286:
284:bifunctional
280:
275:
271:
267:
266:
260:bifunctional
257:
250:
248:
244:
240:
238:bifunctional
237:
235:
231:
229:
226:
224:
221:
220:
216:
213:
210:
207:
205:
202:
201:
197:
194:
191:
188:
185:
182:
179:
178:
166:
164:
163:S. cerevisiae
157:
156:
150:
149:
144:
138:
135:
133:
129:
125:
121:
117:
108:
106:
101:
91:
89:
85:
81:
71:
68:
64:
58:
56:
52:
48:
43:
39:
35:
31:
27:
23:
16:
3790:Translocases
3787:
3774:
3761:
3748:
3735:
3725:Transferases
3722:
3709:
3566:Binding site
3500:
3232:Glucosidases
3065:
3061:
3054:
3011:
3007:
2997:
2970:
2966:
2926:
2922:
2912:
2869:
2865:
2859:
2827:(5): 320â8.
2824:
2820:
2810:
2765:
2761:
2715:
2711:
2705:
2670:
2666:
2652:
2617:
2613:
2570:(2): 151â5.
2567:
2563:
2557:
2522:
2472:
2468:
2458:
2423:
2419:
2409:
2372:
2368:
2357:
2332:
2328:
2322:
2297:
2293:
2286:
2241:
2237:
2227:
2186:
2182:
2176:
2131:
2127:
2117:
2082:
2078:
2068:
2033:
2029:
2019:
1994:
1990:
1984:
1959:
1955:
1949:
1940:
1905:
1901:
1891:
1854:
1850:
1840:
1795:
1791:
1781:
1746:
1742:
1732:
1705:
1701:
1691:
1656:
1652:
1642:
1607:
1603:
1593:
1558:
1554:
1516:
1512:
1466:
1462:
1452:
1428:(4): 480â5.
1425:
1421:
1411:
1378:
1374:
1368:
1343:
1339:
1311:
1307:
1297:
1252:
1248:
1238:
1183:
1174:
1154:
1150:
1143:
1109:
1105:
1096:polymorphism
1093:
1081:field defect
1078:
1063:
1059:carcinogenic
1025:
995:
961:
953:
932:colon cancer
928:colon polyps
915:8-oxoguanine
911:
905:
901:
883:
870:general base
868:to act as a
809:
806:Conservation
796:mitochondria
788:mitochondria
777:
774:Localisation
766:to form U:A
747:that excise
742:
726:
718:
704:
702:
528:
496:
492:thermophilic
485:
455:(UDG) is an
446:
426:
421:Alkylpurine
415:Not present
412:Not present
399:Alkylpurine
393:Not present
390:Not present
379:T:G mispair
370:Not present
365:Not present
360:T:G mispair
351:Not present
346:Not present
332:Not present
327:Not present
313:Not present
278:Not present
162:
153:
146:
136:
131:
127:
123:
119:
114:
97:
77:
66:
62:
59:
28:involved in
21:
20:
15:
3561:Active site
3459:Iduronidase
3393:Pullulanase
3062:Epigenomics
1346:(1): 43â9.
1180:Lindahl, T.
1123:pyrimidines
1119:abasic site
1115:oxidatively
1070:methylation
1061:mutations.
836:amino acids
553:Identifiers
465:deamination
175:Substrates
105:Schiff base
63:A. thaliana
3844:DNA repair
3833:Categories
3764:Isomerases
3738:Hydrolases
3605:Regulation
3469:Heparanase
3437:Fucosidase
3255:Neutral AB
2887:2115/43021
2667:Oncotarget
2469:DNA Repair
2294:Cancer Res
1604:Curr. Biol
1167:References
1046:intragenic
1039:transition
997:Epigenetic
866:structures
832:poxviruses
824:eukaryotes
780:eukaryotic
764:polymerase
650:structures
477:DNA repair
98:The first
67:N. tabacum
36:EC 3.2.2.
3643:EC number
3403:lysosomal
3307:Chitinase
3272:cytosolic
3260:Neutral C
3240:Cellulase
3217:Trehalase
3207:Invertase
3165:Hydrolase
3101:IPR005122
2904:207147128
2475:: 33â42.
1814:0021-9258
1513:Mutat Res
1228:ignored (
1218:cite book
1135:hydantoin
1085:silencing
1066:neoplasms
1042:mutations
970:Pathology
852:conserved
816:conserved
739:Mechanism
733:structure
723:Structure
596:PDOC00121
584:IPR005122
461:mutations
322:A:8-oxoG
155:B. cereus
34:EC number
3849:EC 3.2.2
3667:Kinetics
3591:Cofactor
3554:Activity
3312:Lysozyme
3097:InterPro
3082:24811787
3046:24569633
3014:: 4186.
2989:22286769
2967:Oncogene
2945:15319300
2896:20197241
2851:20955798
2802:23898192
2732:23027038
2697:26503472
2644:19127118
2592:41948691
2549:23195996
2499:26021671
2450:25183517
2401:24698998
2349:22683793
2314:15231648
2278:10557315
2011:16860315
1976:17116429
1932:14851787
1883:12417741
1832:12456671
1773:15466595
1634:32822653
1626:10339434
1585:14851787
1533:10946227
1493:15722486
1444:15056851
1360:15102448
1289:16864782
1074:promoter
900:8-oxoG (
846:transit
820:bacteria
812:sequence
798:and the
786:and the
760:cytosine
752:residues
729:proteins
715:Function
667:RCSB PDB
579:InterPro
469:cytosine
451:family,
303:unknown
128:MutM/Fpg
80:AP lyase
51:flipping
3823:Biology
3777:Ligases
3547:Enzymes
3295:Amylase
3222:Lactase
3212:Maltase
3199:Sucrase
3037:3935198
3016:Bibcode
2842:3254599
2793:3746843
2770:Bibcode
2688:4767479
2635:2683899
2584:3338800
2540:3661743
2490:4903958
2441:4176167
2392:3974638
2246:Bibcode
2219:4315434
2211:7845459
2191:Bibcode
2168:8389453
2136:Bibcode
2109:2555154
2060:8332455
1924:7697717
1823:2764232
1724:2820976
1683:9136303
1675:9489705
1577:7697717
1403:1411536
1383:Bibcode
1375:Science
1280:1544249
1257:Bibcode
1210:3527146
1127:thymine
1072:of the
1068:due to
886:guanine
872:in the
859:residue
848:peptide
800:nucleus
784:nucleus
745:enzymes
699:History
628:cd09593
591:PROSITE
572:PF03167
449:protein
335:hSMUG1
300:hNEIL3
292:hNEIL2
281:hNEIL1
217:uracil
161:Yeast (
148:E. coli
132:HhH-GPD
47:AP site
26:enzymes
3809:Portal
3751:Lyases
3381:Klotho
3130:(MeSH)
3080:
3044:
3034:
2987:
2943:
2902:
2894:
2849:
2839:
2800:
2790:
2740:788490
2738:
2730:
2695:
2685:
2642:
2632:
2590:
2582:
2547:
2537:
2497:
2487:
2448:
2438:
2399:
2389:
2347:
2312:
2276:
2266:
2217:
2209:
2183:Nature
2166:
2156:
2107:
2100:401392
2097:
2079:EMBO J
2058:
2051:309584
2048:
2009:
1974:
1930:
1922:
1881:
1874:137523
1871:
1830:
1820:
1812:
1771:
1764:521670
1761:
1722:
1681:
1673:
1632:
1624:
1583:
1575:
1531:
1491:
1484:549418
1481:
1442:
1401:
1358:
1287:
1277:
1208:
1198:
1139:8-oxoG
942:, and
880:Family
749:uracil
727:These
682:PDBsum
656:
646:
616:SUPFAM
558:Symbol
517:, and
499:uracil
481:cancer
473:uracil
457:enzyme
169:Human
3703:Types
3490:3.2.2
3474:HPSE2
3359:Alpha
3288:Other
3178:3.2.1
2900:S2CID
2736:S2CID
2663:(PDF)
2588:S2CID
2269:23942
2215:S2CID
2159:46543
1928:S2CID
1679:S2CID
1630:S2CID
1581:S2CID
1111:NEIL1
1102:NEIL1
985:BRCA2
981:BRCA1
944:NEIL3
940:NEIL2
936:NEIL1
863:X-ray
792:Human
768:pairs
612:SCOPe
603:SCOP2
511:SMUG1
409:AlkD
387:AlkC
384:AlkC
373:MBD4
316:hMYH
308:MutY
268:Ntg2
251:Ntg1
208:Ung1
186:Mag1
183:AlkE
180:AlkA
172:Type
3795:list
3788:EC7
3782:list
3775:EC6
3769:list
3762:EC5
3756:list
3749:EC4
3743:list
3736:EC3
3730:list
3723:EC2
3717:list
3710:EC1
3452:HEXB
3447:HEXA
3425:NAGA
3364:Beta
3337:NEU4
3332:NEU3
3327:NEU2
3322:NEU1
3250:Acid
3171:3.2)
3095:and
3093:Pfam
3078:PMID
3042:PMID
2985:PMID
2941:PMID
2892:PMID
2847:PMID
2798:PMID
2728:PMID
2693:PMID
2640:PMID
2580:PMID
2545:PMID
2495:PMID
2446:PMID
2397:PMID
2345:PMID
2310:PMID
2274:PMID
2238:PNAS
2207:PMID
2164:PMID
2105:PMID
2056:PMID
2007:PMID
1972:PMID
1920:PMID
1902:Cell
1879:PMID
1851:PNAS
1828:PMID
1810:ISSN
1769:PMID
1720:PMID
1671:PMID
1653:Cell
1622:PMID
1573:PMID
1555:Cell
1529:PMID
1489:PMID
1440:PMID
1399:PMID
1356:PMID
1285:PMID
1230:help
1206:PMID
1196:ISBN
1146:mRNA
1027:MBD4
1013:MBD4
1006:MGMT
1002:MLH1
983:and
958:AlkA
930:and
919:OGG1
906:anti
822:and
810:The
675:PDBj
671:PDBe
654:ECOD
644:Pfam
608:1udg
567:Pfam
519:MBD4
405:AlkD
354:TDG
273:Nei
256:NTH1
246:Nth
234:OGG1
228:Ogg1
222:Fpg
211:UNG
203:UDG
130:and
122:and
3070:doi
3032:PMC
3024:doi
2975:doi
2931:doi
2882:hdl
2874:doi
2837:PMC
2829:doi
2788:PMC
2778:doi
2766:110
2720:doi
2683:PMC
2675:doi
2630:PMC
2622:doi
2572:doi
2535:PMC
2527:doi
2485:PMC
2477:doi
2436:PMC
2428:doi
2387:PMC
2377:doi
2337:doi
2302:doi
2264:PMC
2254:doi
2199:doi
2187:373
2154:PMC
2144:doi
2095:PMC
2087:doi
2046:PMC
2038:doi
1999:doi
1995:312
1964:doi
1910:doi
1869:PMC
1859:doi
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