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Information on EC 3.2.2.23 - DNA-formamidopyrimidine glycosylase and Organism(s) Homo sapiens and UniProt Accession Q969S2
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3.2.2.23 DNA-formamidopyrimidine glycosylaseIUBMB Comments
May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
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Word Map
- 3.2.2.23
- strand
- comet
- glycosylases
-
genotoxic
- purine
-
single-stranded
-
abasic
- duplex
-
fpg-sensitive
- thymine
-
excises
- 7,8-dihydro-8-oxoguanine
- ape1
-
ring-opened
- 8-oxo-7,8-dihydroguanine
-
8-oxodg
- endonucleases
-
8-oxo-7,8-dihydro-2'-deoxyguanosine
- 5-hydroxyuracil
-
micronucleus
-
transversions
-
neils
-
alkali-labile
-
biomonitoring
-
3-methyladenine-dna
- mispairs
-
interstrand
-
lesion-specific
- spiroiminodihydantoin
- bromate
- medicine
- 2'-deoxyguanosine
-
klenow
- ap-endonuclease
-
uvrabc
-
miscoding
-
base-excision
-
apurinic
- 8-oxo-2'-deoxyguanosine
-
monoadducts
- dihydrouracil
-
enzyme-modified
-
unhook
-
mutyh
-
endoiii
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
neil1, neil3, fpg protein, formamidopyrimidine-dna glycosylase, formamidopyrimidine dna glycosylase, 8-oxoguanine-dna glycosylase, formamidopyrimidine glycosylase, fapy-dna glycosylase, fpg-1, fpg-l, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase
-
-
-
-
2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase
-
-
-
-
2,6-diamino-4-hydroxy-5N-methyl-formamidopyrimidine-DNA glycosylase
-
-
-
-
8-hydroxyguanine endonuclease
-
-
-
-
8-oxoguanine DNA glycosylase
-
-
-
-
deoxyribonucleate glycosidase
-
-
-
-
DNA glycohydrolase (releasing 2,6-diamino-4-hydroxy-5-(N-methyl)-formamidopyrimidine)
-
-
-
-
Fapy-DNA glycosylase
-
-
-
-
formamidopyrimidine-DNA glycosyl hydrolase
-
-
-
-
formamidopyrimidine-DNA glycosylase
-
-
-
-
FPG
Fpg protein
-
-
-
-
glycosidase, deoxyribonucleate formamidopyrimidine
-
-
-
-
MutM
-
-
-
-
NEIL1
additional information
-
the enzymes belong to the Fpg family of DNA glycosylases
FPG
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
DNA glycohydrolase [2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing]
May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
CAS REGISTRY NUMBER
COMMENTARY
78783-53-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt oligodeoxynucleotide + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt oligodeoxynucleotide
-
-
-
?
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt-DNA + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt-DNA
-
-
-
?
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide + H2O
8-oxo-7,8-dihydroguanine + Cyt oligodeoxynucleotide
-
-
-
?
8-oxo-7,8-dihydroguanine:Cyt-DNA + H2O
8-oxo-7,8-dihydroguanine + Cyt-DNA
-
-
-
?
DNA containing 2,6-diamino-4-hydroxy-5-formamidopyrimidine residues + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + DNA
FapyGua
-
-
?
DNA containing 4,6-diamino-5-formamidopyrimidine residues + H2O
4,6-diamino-5-formamidopyrimidine + DNA
FapyAde
-
-
?
DNA containing 5-hydroxy-2'-deoxyuridine + H2O
?
dublex oligodeoxynucleotide containing 5-hydroxyuracil when paired with G
-
-
?
DNA containing 7-deaza-2'-deoxyguanosine + H2O
7-deaza-2'-deoxyguanosine + DNA
-
-
-
-
?
DNA containing 7-hydro-8-oxoguanine residues + H2O
DNA + 7-hydro-8-oxoguanine
excises 8-oxoguanine from 31mer oligodeoxynucleotide, most active with G, followed by T, opposite the lesion, weak activity with C or A opposite
-
-
?
DNA containing 7-methyl-8-oxo-2'-deoxyguanosine + H2O
7-methyl-8-oxo-2'-deoxyguanosine + DNA
-
-
-
-
?
DNA containing 8-oxo-2'-deoxyguanosine + H2O
8-oxo-2'-deoxyguanosine + DNA
-
-
-
-
?
DNA containing 8-oxo-2'-deoxyguanosine residues + H2O
DNA + 8-oxo-2'-deoxyguanosine
-
-
-
-
?
DNA containing 8-thio-2'-deoxyguanosine + H2O
8-thio-2'-deoxyguanosine + DNA
-
-
-
-
?
DNA containing dihydrouracil residues + H2O
?
active as a DNA glycosylase/AP lyase with dihydrouracil 31mer dublex oligo substrate, similar activity with A, C or G opposite the lesion, reduced with T opposite
-
-
?
ds oligodeoxynucleotides containing N5-alkyl formamidopyrimidine + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + ds oligonucleotide
-
-
-
?
5,6-dihydrouracil-DNA + H2O
5,6-dihydrouracil + DNA
-
DHU is excised from DNA by a number of DNA glycosylases including Fpg and Nei
-
-
?
5,6-dihydrouracil-DNA + H2O
5,6-dihydrouracil + DNA
-
DHU is formed in DNA from cytosine under the action of OH radicals under ionizing radiation
-
-
?
DNA + H2O
?
with apurinic/apyrimidinic lyase activity, catalyzes beta and delta elimination reactions
-
-
?
DNA + H2O
?
excises formamidopyrimidines from damaged DNA and oxidized pyrimidines and 8-oxoguanine from oligodeoxynucleotides, role of the N-terminal Pro as its active site
-
-
?
DNA + H2O
?
enzyme has N-glycosylase and apurinic/apyrimidinic lyase activity
-
-
?
DNA + H2O
?
involved in replication-associated repair of oxidized bases
-
-
?
additional information
?
-
not: DNA containing 2-hydroxyadenine, 1-N6 ethenoadenine, 3-N4 ethenocytosine, hypoxanthine, xanthine
-
-
?
additional information
?
-
not: DNA containing 2-hydroxyadenine, 1-N6 ethenoadenine, 3-N4 ethenocytosine, hypoxanthine, xanthine
-
-
?
additional information
?
-
-
cross-linking of active center with a series of reactive oligonucleotide duplexes containing both a single 8-oxoguanine residue and an O-ethyl-substituted diphosphate internucleotide group results in identification of eight phosphate groups on both strands of the DNA duplex specifically interacting with nucleophilic amino acids of the enzyme. L249 of enzyme cross-links to the phosphate located 3' to the 8-oxoguanine residue
-
-
?
additional information
?
-
-
treatment of cells with 4-(acetoxymethylnitrosamino)-1-(3-pyridyl)-1-butanone generates formamidopyrimidine glycosylase sensitive DNA sites with cell-type dependent differences in adduct frequency and time
-
-
?
additional information
?
-
8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1
-
-
?
additional information
?
-
-
8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1
-
-
?
additional information
?
-
-
NEIL1 is active on DNA lesions in ssDNA, particularly in the context of a single-stranded bubble in a duplex sequence
-
-
?
additional information
?
-
8-oxoguanine-DNA glycosylase, OGG1, efficiently removes mutagenic 8-oxo-7,8-dihydroguanine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine when paired with cytosine in oxidatively damaged DNA. Excision of 8-oxoGua mispaired with adenine may lead to G to T transversions. Substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
8-oxoguanine-DNA glycosylase, OGG1, efficiently removes mutagenic 8-oxo-7,8-dihydroguanine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine when paired with cytosine in oxidatively damaged DNA. Excision of 8-oxoGua mispaired with adenine may lead to G to T transversions. Substrate specificity of wild-type and mutant enzymes, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,6-diamino-4-hydroxy-5-formamidopyrimidine:Cyt-DNA + H2O
2,6-diamino-4-hydroxy-5-formamidopyrimidine + Cyt-DNA
-
-
-
?
5,6-dihydrouracil-DNA + H2O
5,6-dihydrouracil + DNA
-
DHU is excised from DNA by a number of DNA glycosylases including Fpg and Nei
-
-
?
8-oxo-7,8-dihydroguanine:Cyt-DNA + H2O
8-oxo-7,8-dihydroguanine + Cyt-DNA
-
-
-
?
DNA containing 8-oxo-2'-deoxyguanosine residues + H2O
DNA + 8-oxo-2'-deoxyguanosine
-
-
-
-
?
DNA + H2O
?
involved in replication-associated repair of oxidized bases
-
-
?
additional information
?
-
8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1
-
-
?
additional information
?
-
-
8-oxo-7,8-dihydroguanine, i.e. 8-oxoGua, and 2,6-diamino-4-hydroxy-5-formamidopyrimidine, i.e. FapyGua, are premutagenic DNA lesions that appear in DNA damaged by reactive oxygen species of endogenous and environmental origin, and are excised from DNA by the enzyme. The fidelity of the 8-oxoGua repair system depends on discrimination between 8-oxoGua:Cyt and 8-oxoGua:Ade pairs by OGG1
-
-
?
additional information
?
-
-
NEIL1 is active on DNA lesions in ssDNA, particularly in the context of a single-stranded bubble in a duplex sequence
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cd2+
-
preferentially binds to DNA bases rather than phosphates, the presence of the metal ions causes the enzyme to lose the ability for preferential binding to damaged DNA
Cu2+
-
preferentially binds to DNA bases rather than phosphates, the presence of the metal ions causes the enzyme to lose the ability for preferential binding to damaged DNA
additional information
-
differing inhibitory effects of metal ions in potassiumphosphate buffer and Tris-HCl buffer, mechanism of NEIL1 inhibition by heavy metal salts, e.g. involving sequential elimination of phosphate groups from the 3'- and 5'-side of the formed AP site, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
complementation groups B genes
-
CSB stimulates incision activity of NEIL1, and CSB stimulates the NEIL1-mediated AP lyase activity 3fold
-
additional information
the human AP endonuclease APEX1 can stimulate wild-type OGG1 activity by increasing its turnover rate, but very little stimulation of 8-oxoGua removal in the presence of APEX1 occurs with phosphomimetic mutants, overview
-
additional information
-
the human AP endonuclease APEX1 can stimulate wild-type OGG1 activity by increasing its turnover rate, but very little stimulation of 8-oxoGua removal in the presence of APEX1 occurs with phosphomimetic mutants, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000034
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S326C
-
0.0000034
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, wild-type enzyme
-
0.0000057
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S231E
-
0.0000061
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant D322N
-
0.0000074
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S280E
-
0.0000075
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S326E
-
0.0000086
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant A288V
-
0.0000092
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S232E
-
0.00001
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S231E/S232E
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00037
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S326C
-
0.00047
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant D322N
-
0.00048
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S280E
-
0.0005
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, wild-type enzyme
-
0.00053
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S326E
-
0.00065
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S232E
-
0.00068
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S231E/S232E
-
0.0007
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant S231E
-
0.00092
8-oxo-7,8-dihydroguanine:Cyt oligodeoxynucleotide
pH 7.4-7.5, mutant A288V
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
substrate specificity of wild-type and mutant enzymes, overview
additional information
-
substrate specificity of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
primary human diploid fibroblasts, S phase-specific expression of NEH1
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
OGG1 polymorphisms might be associated with succeptibility of humans to cancer and other diseases
malfunction
-
patients with Cockayne syndrome, a segmental premature aging syndrome with progressive neurological degeneration caused by mutations in CS complementation groups A, CSA, or B, CSB, genes, show increased 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine concentrations in in genomic DNA and mtDNA, and reduced repair function due to mutation of the endonuclease VIII-like DNA glycosylase NEIL1, overview
physiological function
OGG1 is part of an enzymatic system responsible for prevention of mutations generated by 8-oxo-7,8-dihydroguanine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine
physiological function
-
the enzyme initiates the process of repair of oxidized DNA bases
physiological function
-
Fpg-expressing cells show increased susceptibility to methylmercury-initiated cytotoxicity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43582
x * 43582, recombinant NEH1, calculated from the amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 43582, recombinant NEH1, calculated from the amino acid sequence
additional information
-
cross-linking of active center with a series of reactive oligonucleotide duplexes containing both a single 8-oxoguanine residue and an O-ethyl-substituted diphosphate internucleotide group results in identification of eight phosphate groups on both strands of the DNA duplex specifically interacting with nucleophilic amino acids of the enzyme. L249 of enzyme cross-links to the phosphate located 3' to the 8-oxoguanine residue
additional information
three-dimensional structure of OGG1, PDB ID 1EBM, overview
additional information
-
three-dimensional structure of OGG1, PDB ID 1EBM, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphorylation of OGG1 can affect its biological functions at several levels, including the intrinsic activity and intracellular localization
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A288V
naturally occuring polymorphism, the mutant displays opposite-base specificity similar to that of wild-type OGG1, activity, substrate specificity and kinetics compared to the wild-type enzyme, overview
D322N
naturally occuring polymorphism, the mutant is 2.3fold more specific for the correct opposite base than the wild-type enzyme, activity, substrate specificity and kinetics compared to the wild-type enzyme
S1245C
-
naturally occuring polymorphism. No correlation between mutation and gastric cancer
S231E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S231E/S232E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S232E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S280E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
S326C
naturally occuring polymorphism, the mutant displays opposite-base specificity similar to that of wild-type OGG1. The mutant efficiently excises 8-oxoGua from oligodeoxynucleotides and 2,6-diamino-4-hydroxy-5-formamidopyrimidine from gamma-irradiated DNA, but excises 8-oxoG rather inefficiently from gamma-irradiated DNA
S326E
naturally occuring polymorphism, kinetics compared to the wild-type enzyme, overview
additional information
additional information
-
study on the polymorphism 23A to G in the DNA repair gene XPA. Presence of the A allele is associated with higher levels of DNA damage as well as with higher activity of the OGG1 8-oxoguanidine DNA glycosylase. In individuals with the A allele, OGG1 repair activity also increases with age
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genotyping, overview. Expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
NEH1 is cloned, sequenced and expressed in Escherichia coli BL21(DE3), chromosomal location: 15q25
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
analysis
-
comparison of human Ogg1, Escherichia coli Fpg and endonuclease III for the ability to modify the sensitivity of the comet assay. Use of human Ogg1 in the modified comet assay offers a useful alternative to Fpg and is more specific for 8-oxoguanine and methyl-fapy-guanine
analysis
-
DNA repair kinetics can be investigated with the comet assay and differences between cell types can be observed
analysis
-
simple and sensitive FPG activity assay using target-induced self-primed rolling circle amplification and magnetic nanoprobes. A 8-oxoguanine is positioned in duplex DNA containing a P-circle and P1, which together serve as a FPG substrate, rolling circle amplification template, and rolling circle amplification primer probe. The presence of FPG specifically binds and cleaves 8-oxoG containing duplex DNA, resulting in 5'-phosphoryl termini. The rolling circle amplification reaction produces an amount of long tandem-repeat DNA tiles with multiple recognizing regions for the modified DNA probes and biotin-modified DNA probes: A detection limit of 1.033 U/ml for FPG is obtained. FPG assays in human blood serum are also obtained using fluorescence and confocal laser scanning microscopy
medicine
-
cells from children with Down's syndrome do not display an effective DNA repair after treatment with 10 mM hydrogen peroxide. No difference in the sensitivity to DNA-damaging agents and the efficacy of DNA repair due to age and gender in children with Down's syndrome is observed
medicine
-
melatonin can have a protective effect against oxidative DNA damage by chemical inactivation of a DNA-damaging agent as well as by stimulating DNA repair, but key factors such as DNA-formaidopyrimidine glycosylase, endonuclease III are not affected by melatonin
medicine
-
no correlation between the S1245C polymorphism of the OGG! Gene and gastric cancer. In contrast, there is a strong correlation between gastric cancer occurrence, impaired DNA repair in human lymphocytes, and the G135C polymorphism of the RAD51 gene
medicine
-
significant amounts of 85% of enzyme-sensitive DNA sites are found in smokers, and considerably high but not significant amounts in passive non- and ex-smokers, 51 and 37%, respectively
medicine
-
study on the polymorphism 23A to G in the DNA repair gene XPA. Presence of the A allele is associated with higher levels of DNA damage as well as with higher activity of the OGG1 8-oxoguanidine DNA glycosylase. In individuals with the A allele, OGG1 repair activity also increases with age
medicine
-
treatment of cells with 4-(acetoxymethylnitrosamino)-1-(3-pyridyl)-1-butanone generates formamidopyrimidine glycosylase sensitive DNA sites with cell-type dependent differences in adduct frequency and time
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hazra, T.K.; Izumi, T.; Boldogh, I.; Imhoff, B.; Kow, Y.W.; Jaruga, P.; Dizdaroglu, M.; Mitra, S.
Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA
Proc. Natl. Acad. Sci. USA
99
3523-3528
2002
Homo sapiens (Q969S2), Homo sapiens (Q96FI4)
Wozniak, K.; Blasiak, J.
Nickel impairs the repair of UV- and MNNG-damaged DNA
Cell. Mol. Biol. Lett.
9
83-94
2004
Homo sapiens
Hamm, M.L.; Gill, T.J.; Nicolson, S.C.; Summers, M.R.
Substrate specificity of Fpg (MutM) and hOGG1, two repair glycosylases
J. Am. Chem. Soc.
129
7724-7725
2007
Escherichia coli, Homo sapiens
Rogacheva, M.; Ishchenko, A.; Saparbaev, M.; Kuznetsova, S.; Ogryzko, V.
High resolution characterization of formamidopyrimidine-DNA glycosylase interaction with its substrate by chemical cross-linking and mass spectrometry using substrate analogs
J. Biol. Chem.
281
32353-32365
2006
Escherichia coli, Homo sapiens
Smith, C.C.; ODonovan, M.R.; Martin, E.A.
hOGG1 recognizes oxidative damage using the comet assay with greater specificity than FPG or ENDOIII
Mutagenesis
21
185-190
2006
Escherichia coli, Homo sapiens
Dusinska, M.; Dzupinkova, Z.; Wsolova, L.; Harrington, V.; Collins, A.R.
Possible involvement of XPA in repair of oxidative DNA damage deduced from analysis of damage, repair and genotype in a human population study
Mutagenesis
21
205-211
2006
Homo sapiens
Poplawski, T.; Arabski, M.; Kozirowska, D.; Blasinska-Morawiec, M.; Morawiec, Z.; Morawiec-Bajda, A.; Klupinska, G.; Jeziorski, A.; Chojnacki, J.; Blasiak, J.
DNA damage and repair in gastric cancer - A correlation with the hOGG1 and RAD51 genes polymorphisms
Mutat. Res.
601
83-91
2006
Homo sapiens
Lacoste, S.; Castonguay, A.; Drouin, R.
Repair kinetics of specific types of nitroso-induced DNA damage using the comet assay in human cells
Mutat. Res.
624
18-30
2007
Homo sapiens
Sliwinski, T.; Rozej, W.; Morawiec-Bajda, A.; Morawiec, Z.; Reiter, R.; Blasiak, J.
Protective action of melatonin against oxidative DNA damage-Chemical inactivation versus base-excision repair
Mutat. Res.
634
220-227
2007
Homo sapiens
Morawiec, Z.; Janik, K.; Kowalski, M.; Stetkiewicz, T.; Szaflik, J.; Morawiec-Bajda, A.; Sobczuk, A.; Blasiak, J.
DNA damage and repair in children with Downs syndrome
Mutat. Res.
637
118-123
2008
Homo sapiens
Fracasso, M.E.; Doria, D.; Franceschetti, P.; Perbellini, L.; Romeo, L.
DNA damage and repair capacity by comet assay in lymphocytes of white-collar active smokers and passive smokers (non- and ex-smokers) at workplace
Toxicol. Lett.
167
131-141
2006
Homo sapiens
Grin, I.R.; Konorovsky, P.G.; Nevinsky, G.A.; Zharkov, D.O.
Heavy metal ions affect the activity of DNA glycosylases of the fpg family
Biochemistry (Moscow)
74
1253-1259
2009
Homo sapiens
Sidorenko, V.S.; Grollman, A.P.; Jaruga, P.; Dizdaroglu, M.; Zharkov, D.O.
Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase
FEBS J.
276
5149-5162
2009
Homo sapiens (O15527), Homo sapiens
Muftuoglu, M.; de Souza-Pinto, N.C.; Dogan, A.; Aamann, M.; Stevnsner, T.; Rybanska, I.; Kirkali, G.; Dizdaroglu, M.; Bohr, V.A.
Cockayne syndrome group B protein stimulates repair of formamidopyrimidines by NEIL1 DNA glycosylase
J. Biol. Chem.
284
9270-9279
2009
Homo sapiens, Mus musculus
Ondovcik, S.L.; Preston, T.J.; McCallum, G.P.; Wells, P.G.
Expression of human oxoguanine glycosylase 1 or formamidopyrimidine glycosylase in human embryonic kidney 293 cells exacerbates methylmercury toxicity in vitro
Toxicol. Appl. Pharmacol.
271
41-48
2013
Homo sapiens
Song, J.; Yin, F.; Li, X.; Dong, N.; Zhu, Y.; Shao, Y.; Chen, B.; Jiang, W.; Li, C.Z.
Sensitive detection of formamidopyrimidine-DNA glycosylase activity based on target-induced self-primed rolling circle amplification and magnetic nanoprobes
Analyst
143
1593-1598
2018
Homo sapiens
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