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Information on EC 4.2.99.18 - DNA-(apurinic or apyrimidinic site) lyase and Organism(s) Mus musculus and UniProt Accession O35980
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4.2.99.18 DNA-(apurinic or apyrimidinic site) lyaseIUBMB Comments
'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.
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Word Map
- 4.2.99.18
- strand
-
exonuclease
- glycosylases
-
single-stranded
- pyrimidine
- endonucleases
- 8-oxoguanine
- nick
- thymine
- uracil
- duplex
-
genotoxic
- xrcc1
-
phosphodiester
- comet
- deoxyribose
- methanesulfonate
- mispairs
-
uracil-dna
-
depurinated
-
beta-elimination
-
excise
- formamidopyrimidine
-
3'-phosphatase
- 7,8-dihydro-8-oxoguanine
- tetrahydrofuran
-
site-containing
-
mutyh
-
endonucleolytic
-
xeroderma
- pigmentosum
-
base-excision
- 3'-phosphodiesterase
-
cross-complementing
- 8-oxo-7,8-dihydroguanine
- fen1
-
unrepaired
-
formamidopyrimidine-dna
-
incises
-
long-patch
-
dna-repair
-
uracil-containing
-
ser326cys
- dihydrouracil
-
arg399gln
- 3'-exonuclease
-
reduction-oxidation
-
enzyme-dna
- medicine
-
gap-filling
-
damage-specific
- analysis
- diagnostics
- biotechnology
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Synonyms
ap endonuclease, ref-1, ape1/ref-1, apex1, ape/ref-1, apurinic/apyrimidinic endonuclease 1, ap lyase, ape-1, alkbh1, endo iii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AP 1
-
-
-
-
AP Dnase
-
-
-
-
AP endo
-
-
-
-
AP endonuclease
-
-
-
-
AP endonuclease 1
AP endonuclease Class I
-
-
-
-
AP lyase
-
-
-
-
AP-endonuclease
-
-
-
-
Ape
-
-
-
-
APE1
APEN
-
-
-
-
APEX nuclease
-
-
-
-
APN1
-
-
-
-
apurinic DNA endonuclease
-
-
-
-
apurinic endodeoxyribonuclease
-
-
-
-
apurinic endonuclease
-
-
-
-
apurinic-apyrimidinic DNA endonuclease
-
-
-
-
apurinic-apyrimidinic endodeoxyribonuclease
-
-
-
-
apurinic-apyrimidinic endonuclease
-
-
-
-
apurinic/apyrimidinic endonuclease 1
apurinic/apyrimidinic endonuclease-1/Redox factor-1
-
multifunctional DNA base excision repair and redox regulation enzyme
apurinic/apyrimidinic lyase
-
-
-
-
apurinic/apyrimidinic specific endonuclease
-
-
-
-
apyrimidinic endonuclease
-
-
-
-
class II apurinic/apyrimidinic(AP)-endonuclease
-
-
-
-
deoxyribonuclease (apurinic or apyrimidinic)
-
-
-
-
E. coli endonuclease III
-
-
-
-
endodeoxyribonuclease
-
-
-
-
endodeoxyribonuclease III
-
-
-
-
endonuclease III
-
-
-
-
endonuclease VI
-
-
-
-
Escherichia coli endonuclease III
-
-
-
-
HAP1
-
-
-
-
HAP1h
-
-
-
-
Micrococcus luteus UV endonuclease
-
-
-
-
MMH
-
-
-
-
Nfo
-
-
-
-
Ntg1p
-
-
-
-
Ntg2p
-
-
-
-
NTH1
-
-
-
-
nuclease, apurinic endodeoxyribo-
-
-
-
-
nuclease, apurinic-apyrimidinic endodeoxyribo-
-
-
-
-
nuclease, endodeoxyribo-, III
-
-
-
-
phage-T4 UV endonuclease
-
-
-
-
REF-1 protein
-
-
-
-
Ref1
-
-
-
-
UV endo V
-
-
-
-
UV endonuclease
-
-
-
-
UV endonuclease V
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
endonuclease reaction
endonuclease reaction
-
APE1 has dual activities, a strong endonuclease activity, and a weak exonuclease-phosphodiesterase activity
SYSTEMATIC NAME
IUBMB Comments
DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase
'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.
CAS REGISTRY NUMBER
COMMENTARY
60184-90-9
-
61811-29-8
-
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
5'-TCGAGGATCCTGAGCTCGAGTCGACGXTCGCGAATTCTGCGGATCCAAGC-3'
?
a synthetic stable AP-site analog where X represents tetrahydrofuran
-
-
?
DNA
fragments of DNA
thymine glycol DNA glycosylase, urea DNA glycosylase and AP lyase activity
-
?
DNA
fragments of DNA
-
enzyme recognizes apurinic and apyrimidinic sites induced by acid and gamma-rays, as well as lesions which are introduced into DNA by UV irradiation and OsO4
-
?
DNA
fragments of DNA
-
no activity with methylated or OsO4-treated DNA
-
?
DNA
fragments of DNA
-
enzyme plays an important role in oxidative signalling, transcription factor regulation, and cell cycle control
-
-
ir
additional information
?
-
-
role in eliminating damaged mitochondrial genomes from the gene pool
-
-
?
additional information
?
-
-
poly(ADP-ribose) polymerase-1 and apurinic/apyrimidinic endonuclease can interact with the same base excision repair intermediate. Competition between theses two proteins may influence their respective base excision repair related functions
-
-
?
additional information
?
-
-
the enzyme has two distinct roles in the repair of oxidative DNA damage and in gene regulation. Absolute requirement of the enzyme for cell survival, presumably to protect against spontaneous oxidative DNA damage
-
-
?
additional information
?
-
-
APE/Ref-1 act as tuning molecule in activated B-cells
-
-
?
additional information
?
-
-
APE/Ref-1 affect the cell cycle by inducing nucleus-cytoplasm translocation of the cyclin-dependent kinase inhibitor p21
-
-
?
additional information
?
-
-
APE1 binds with the highest efficiency to DNA substrate containing 5'-sugar phosphate group in the nick/gap
-
-
?
additional information
?
-
-
APE1 exhibits 3'-phosphodiesterase, 3'-phosphatase, and 3'-5'-exonuclease activities
-
-
?
additional information
?
-
-
APE1 is one of the candidates for the role of base excision repair (BER) pathway coordinator, which controls the whole process. APE1 participates in stimulation of activity of BER enzymes
-
-
?
additional information
?
-
-
APE1 stimulates DNA synthesis catalyzed by DNA polymerase beta, and a human Xray repair cross-complementing group 1 protein stimulates APE1 3'-5'-exonuclease activity on 3'-recessed DNA duplex
-
-
?
additional information
?
-
-
APEX1 is a protein involved both in the base excision repair pathways of DNA lesions and in the regulation of gene expression as a redox coactivator of different transcription factors, such as early growth response protein-1
-
-
?
additional information
?
-
-
apurinic/apyrimidinic endonuclease 1 participates in the base excision repair of premutagenic apurinic/apyrimidinic (AP) sites
-
-
?
additional information
?
-
-
DNA with the recessed 3'-end (DNArec) is one of the preferential substrates for APE1 3'-5'-exonuclease activity
-
-
?
additional information
?
-
-
enzyme cleaves the DNA sugar phosphate backbone at the 5'-position in relation to the AP site, forming a nick with the hydroxyl group at the 3'-end and deoxyribose phosphate at the 5'-end
-
-
?
additional information
?
-
-
enzyme plays a role in controlling CD40-mediated B-cell proliferation, increase in proliferation and decrease in apoptosis of primary mouse B-cells activated by CD40 cross-linking and transfected with functional APE/Ref-1 antisense oligonucleotide.
-
-
?
additional information
?
-
-
regulation of APEX1 expression by S-adenosylmethionine, which may be one of the mechanisms of hepatocellular carconom formation
-
-
?
additional information
?
-
-
When APE1 and DNA polymerase beta are both present, a ternary complex APE1-DNA polymerase beta-DNA is formed with the highest efficiency with DNA product of APE1 endonuclease activity and with DNA containing 5'-flap or mononucleotide-gapped DNA with 5'-p group
-
-
?
additional information
?
-
-
APE1 most efficiently binds to DNA substrate bearing tetrahydrofuran in the middle of one of the strands (AP-dsDNA)
-
-
?
additional information
?
-
-
for APE1 in MEF extract, efficiency of formation of protein-DNA crosslinking changes depending on the nature of 5'-group flanking the nick in DNA structure: DNAFAP-pF (100%), DNAFAP-OH (68.2%), DNAFAP-flap (54.6%), DNAFAP-gap (44.2%), DNAFAP-rec (41.3%), DNAFAP-p (41.1%)
-
-
?
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
DNA
fragments of DNA
-
enzyme plays an important role in oxidative signalling, transcription factor regulation, and cell cycle control
-
-
ir
additional information
?
-
-
role in eliminating damaged mitochondrial genomes from the gene pool
-
-
?
additional information
?
-
-
poly(ADP-ribose) polymerase-1 and apurinic/apyrimidinic endonuclease can interact with the same base excision repair intermediate. Competition between theses two proteins may influence their respective base excision repair related functions
-
-
?
additional information
?
-
-
the enzyme has two distinct roles in the repair of oxidative DNA damage and in gene regulation. Absolute requirement of the enzyme for cell survival, presumably to protect against spontaneous oxidative DNA damage
-
-
?
additional information
?
-
-
APE/Ref-1 act as tuning molecule in activated B-cells
-
-
?
additional information
?
-
-
APE/Ref-1 affect the cell cycle by inducing nucleus-cytoplasm translocation of the cyclin-dependent kinase inhibitor p21
-
-
?
additional information
?
-
-
APE1 binds with the highest efficiency to DNA substrate containing 5'-sugar phosphate group in the nick/gap
-
-
?
additional information
?
-
-
APE1 exhibits 3'-phosphodiesterase, 3'-phosphatase, and 3'-5'-exonuclease activities
-
-
?
additional information
?
-
-
APE1 is one of the candidates for the role of base excision repair (BER) pathway coordinator, which controls the whole process. APE1 participates in stimulation of activity of BER enzymes
-
-
?
additional information
?
-
-
APE1 stimulates DNA synthesis catalyzed by DNA polymerase beta, and a human Xray repair cross-complementing group 1 protein stimulates APE1 3'-5'-exonuclease activity on 3'-recessed DNA duplex
-
-
?
additional information
?
-
-
APEX1 is a protein involved both in the base excision repair pathways of DNA lesions and in the regulation of gene expression as a redox coactivator of different transcription factors, such as early growth response protein-1
-
-
?
additional information
?
-
-
apurinic/apyrimidinic endonuclease 1 participates in the base excision repair of premutagenic apurinic/apyrimidinic (AP) sites
-
-
?
additional information
?
-
-
DNA with the recessed 3'-end (DNArec) is one of the preferential substrates for APE1 3'-5'-exonuclease activity
-
-
?
additional information
?
-
-
enzyme cleaves the DNA sugar phosphate backbone at the 5'-position in relation to the AP site, forming a nick with the hydroxyl group at the 3'-end and deoxyribose phosphate at the 5'-end
-
-
?
additional information
?
-
-
enzyme plays a role in controlling CD40-mediated B-cell proliferation, increase in proliferation and decrease in apoptosis of primary mouse B-cells activated by CD40 cross-linking and transfected with functional APE/Ref-1 antisense oligonucleotide.
-
-
?
additional information
?
-
-
regulation of APEX1 expression by S-adenosylmethionine, which may be one of the mechanisms of hepatocellular carconom formation
-
-
?
additional information
?
-
-
When APE1 and DNA polymerase beta are both present, a ternary complex APE1-DNA polymerase beta-DNA is formed with the highest efficiency with DNA product of APE1 endonuclease activity and with DNA containing 5'-flap or mononucleotide-gapped DNA with 5'-p group
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
25 mM included in assay medium. DNA structures with a nick and DNArec used for photoaffinity modification are substrates for APE1 3'-5'-exonuclease activity, that is more efficient at decreased salt concentrations.
KCl
Mg2+
Mn2+
NaCl
-
enzyme form A: optimal activity in 20 mM NaCl or KCl, enzyme form B: more active without salt
additional information
-
presence of divalent cations does not stimulate the activity
KCl
-
enzyme form A: optimal activity in 20 mM NaCl or KCl, enzyme form B: more active without salt
Mg2+
required. Increasing the Mg2+ concentration alters the ratio of turns to beta-strands, and this change may be associated with the conformational changes required to achieve an active state
Mn2+
-
In order to cleave phosphodiester bonds in the course of endonuclease and exonuclease reactions catalyzed by APE1, Mg2+ or Mn2+ is needed
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cycloheximide
-
treatment decreases APEX1 protein levels as compared with untreated mouse hepatocytes
E3330
-
APE1 redox-specific inhibitor. E3330 suppresses secretion of inflammatory cytokines including tumor necrosis factor-alpha, interleukin IL-6 and IL-12 and inflammatory mediators nitric oxide as well as prostaglandin E2 from lipopolysaccharide-stimulated RAW264.7 cells and leads to down-regulation of the lipopolysaccharide-dependent expression of inducible nitric oxide synthase and cyclooxygenase-2 genes in the RAW264.7 cells. The effects of E3330 are mediated by the inhibition of transcription factors nuclear factor-kappaB and activator protein 1 in lipopolysaccharide-stimulated macrophages
human X-ray repair cross-complementing group 1 protein (XRCC1)
-
at high XRCC1 concentrations, inhibition of APE1 exonuclease activity is observed
-
isoflavones
-
soy isoflavones decrease apurinic/apyrimidinic endonuclease 1/redox factor-1 expression
Kainic acid
-
APE/Ref-1 is decreased by kainic acid injury in a time-dependent manner at the level of proteins, not transcripts
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
human X-ray repair cross-complementing group 1 protein
-
stimulates APendonuclease and 3'-phosphodiesterase activities of APE1 and increases efficiency of 3'-5'-exonuclease excision of the match as well as noncanonical pairs by APE1
-
S-adenosylmethionine
-
S-adenosylmethionine co-treatment is able to increase APEX1 protein levels
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00091
5'-TCGAGGATCCTGAGCTCGAGTCGACGXTCGCGAATTCTGCGGATCCAAGC-3'
pH 7.5, 37°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.2
5'-TCGAGGATCCTGAGCTCGAGTCGACGXTCGCGAATTCTGCGGATCCAAGC-3'
pH 7.5, 37°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000015
-
age-dependent modulation of APE activity in mouse liver organelles, 4-months, mitochondria
0.0000096
0.0000196
-
age-dependent modulation of APE activity in mouse liver organelles, 10-months, total extract
0.0000232
-
age-dependent modulation of APE activity in mouse liver organelles, 20-months, total extract
0.0000236
-
age-dependent modulation of APE activity in mouse liver organelles, 4-months, total extract
0.000038
-
age-dependent modulation of APE activity in mouse liver organelles, 4-months, nuclear
0.0000485
-
age-dependent modulation of APE activity in mouse liver organelles, 10-months, nuclear
0.000072
-
age-dependent modulation of APE activity in mouse liver organelles, 20-months, nuclear
additional information
0.0000096
-
age-dependent modulation of APE activity in mouse liver organelles, 10-months, mitochondria
0.0000096
-
age-dependent modulation of APE activity in mouse liver organelles, 20-months, mitochondria
additional information
-
APE1 is most efficiently (5% yield) modified by DNA substrate bearing the 5'-pF group (DNAFAP-pF), which flanks a nick. This DNA structure is a model of a short-patch BER intermediate or a long-patch BER product and is an analog of the product of endonuclease or substrate of the exonuclease APE1 activity
additional information
-
genomic instability increased in the livers of 1-month-old methionine adenosyltransferase 1a knock-out mice, compared with wild-type mice, whereas Apex1 mRNA and protein levels are reduced by 20% and 50%, in knock-out mice of all ages
additional information
-
in mouse cultured hepatocytes, APEX1 protein levels decrease by 40% despite the increase in mRNA levels, and treatment with 2 mmol/L S-adenosylmethionine is able to completely prevent it
additional information
-
the redox activity of APE/Ref-1 is regulated by chemical reduction and oxidation in vitro
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10.5
-
pH 6.5: about 25% of activity maximum, pH 10.5: about 20% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
primary cell line, murine B-cells are isolated from spleen by a negative depletion
-
from 2- to 3-month-old male C57/B6 mice isolated by collagenase perfusion
-
1-month-old, from male methionine adenosyltransferase 1a knock-out and wild-type mice
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
APE/Ref-1 is equally distributed between the nucleus and the cytoplasm, whereas at 24 hours, the CD40-induced-B cell activation relocalized APE/Ref-1 in the nucleus
-
additional information
depending on the type of cells, APE1 is localized primarily in the nucleus, cytoplasm, or mitochondria
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
inactivation of the APE1 gene causes early embryonic lethality in mice
physiological function
physiological function
-
mice deficient for the base excision repair enzyme, apurinic/apyrimidinic endonuclease APE2 protein develop relatively normally, but they display defects in lymphopoiesis. Mice nullizygous for APE2 show an inhibition of the pro-B to pre-B cell transition. APE2 is not required for V(D)J recombination and the turnover rate of APE2-deficient progenitor B cells is nearly normal. The production rate of pro- and pre-B cells is reduced due to a p53-dependent DNA damage response. Progenitors from APE2-deficient mice differentiate normally in response to IL-7 in in vitro stromal cell cocultures, but pro-B cells show defective expansion. APE2-deficient mice show a delay in recovery of B lymphocyte progenitors following bone marrow depletion by 5-fluorouracil, with the pro-B and pre-B cell pools still markedly decreased 2 weeks after a single treatment
physiological function
-
overexpression of APE/Ref-1 using adenovirus and restoration of APE small peptides significantly reduces kainic acid-induced hippocampal cell death. Both silencing of APE/Ref-1 by siRNA and inhibition of endonuclease by an antibody significantly increase caspase-3 activity and apoptotic cell death triggered from the early time after exposure to kainic acid. Findings suggest that cell death is initiated by reducing APE/Ref-1 protein and inhibiting its repair function in spite of enough protein amounts
physiological function
apurinic/apyrimidinic sites (AP sites) are among the most abundant DNA damages. They can emerge because of spontaneous hydrolysis of the N-glycoside bond and during removal of the damaged DNA bases by DNA glycosylases. In mammalian cells up to 10000 AP sites emerge daily primarily due to apurinization of DNA. The number of such damages increases dramatically during intensive oxidative stress, X-ray and UV irradiation, and other actions. The deoxyribose residues in the AP sites exist in different forms that are in equilibrium. The acyclic aldehyde form of an AP site can form a Schiff base with amino groups in proteins, most often with the epsilon-NH2 group of lysine residues. AP endonucleases are the most important enzymes involved in the DNA repair that initiates the repair of AP sites. APE1 exhibits 3'-phosphodiesterase, 3'-5'-exonuclease, and 3'-phosphatase activities. Role of APE1 in the DNA repair process and in other metabolic processes, overview. APE1 stimulates the activity of the mouse adeninex02DNA glycosylase (Myh) and enhances affinity of this enzyme to adenine/8-oxoguanine pairs in comparison with adenine/guanine pairs
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). NTH_MOUSE
300
0
33637
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme has a DNA repair domain at the C-terminus and a redox regulation domain at the N-terminus
additional information
the N-terminal domain (about 6 kDa, 60 amino acids) is responsible for the redox function of APE1, which is independent of the repair functions of this enzyme, and it contains the nuclear export signal
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
APE1 is subjected to different types of posttranslational modifications: acetylation at several residues in the N-domain, nitrosylation on residues of the C-domain, ubiquitination, proteolysis, and sumoylation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, pH 8.0, 1 mM EDTA, 0.05% Triton X-100, 0.5 mM dithiothreitol, 10 mM KCl, 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
repression of APE/Ref-1 by an antisense overexpression, transfection of mouse B-cells with phosphorothioate oligonucleotide, which is complementary to the APE/Ref-1 mRNA sequence and overlaps the translation initiation site (antisense oligonucleotide)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
selective targeting of APE1/Ref-1 could enhance conventional cancer treatment such as radiotherapy
medicine
-
pharmacological inhibition of APE1 by E3330 suppresses inflammatory response in activated macrophages
medicine
comparison of mouse and human enzyme. Overall results suggest that human and mouse APE1s have mostly similar biochemical and biophysical properties. The conclusions of mouse studies to elucidate APE1 biology and its role in carcinogenesis may be extrapolated to apply to human biology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tomkinson, A.E.; Bonk, R.T.; Linn, S.
Mitochondrial endonuclease activities specific for apurinic/apyrimidinic sites in DNA from mouse cells
J. Biol. Chem.
263
12532-12537
1988
Mus musculus
Nes, I.F.
Purification and properties of a mouse-cell DNA-repair endonuclease which recognizes lesions in DNA induced byy ultraviolet light, depurination, gamma-rays and OsO4 treatment
Eur. J. Biochem.
112
161-168
1980
Mus musculus
Nes, I.F.
Purification and characterization of an endonuclease specific for sites in DNA from a permanently established mouse palsmocytoma cell line
Nucleic Acids Res.
8
1575-1589
1980
Mus musculus
Sarker, A.H.; Ikeda, S.; Nakano, H.; Terato, H.; Ide, H.; Imai, K.; Akiyama, K.; Tsutsui, K.; Bo, Z.; Kubo, K.; Yamamoto, K.; Yasui, A.; Yoshida, M.C.; Seki, S.
Cloning and characterization of a mouse homologue (mNthl1) of Escherichia coli endonuclease III
J. Mol. Biol.
282
761-774
1998
Mus musculus (O35980), Mus musculus
Cistulli, C.; Lavrik, O.I.; Prasad, R.; Hou, E.; Wilson, S.H.
AP endonuclease and poly(ADP-ribose) polymerase-1 interact with the same base excision repair intermediate
DNA Repair
3
581-591
2004
Mus musculus
Izumi, T.; Brown, D.B.; Naidu, C.V.; Bhakat, K.K.; Macinnes, M.A.; Saito, H.; Chen, D.J.; Mitra, S.
Two essential but distinct functions of the mammalian abasic endonuclease
Proc. Natl. Acad. Sci. USA
102
5739-5743
2005
Mus musculus
Raffoul, J.J.; Banerjee, S.; Singh-Gupta, V.; Knoll, Z.E.; Fite, A.; Zhang, H.; Abrams, J.; Sarkar, F.H.; Hillman, G.G.
Down-regulation of apurinic/apyrimidinic endonuclease 1/redox factor-1 expression by soy isoflavones enhances prostate cancer radiotherapy in vitro and in vivo
Cancer Res.
67
2141-2149
2007
Homo sapiens, Mus musculus
Mitra, S.; Izumi, T.; Boldogh, I.; Bhakat, K.K.; Chattopadhyay, R.; Szczesny, B.
Intracellular trafficking and regulation of mammalian AP-endonuclease 1 (APE1), an essential DNA repair protein
DNA Repair
6
461-469
2007
Mus musculus
Dyrkheeva, N.S.; Khodyreva, S.N.; Lavrik, O.I.
Interaction of APE1 and other repair proteins with DNA duplexes imitating intermediates of DNA repair and replication
Biochemistry (Moscow)
73
261-272
2008
Mus musculus
Tomasi, M.L.; Iglesias-Ara, A.; Yang, H.; Ramani, K.; Feo, F.; Pascale, M.R.; Luz Martinez-Chantar, M.; Mato, J.M.; Lu, S.C.
S-adenosylmethionine regulates apurinic/apyrimidinic endonuclease 1 stability: implication in hepatocarcinogenesis
Gastroenterology
136
1025-1036
2009
Mus musculus
Merluzzi, S.; Gri, G.; Gattei, V.; Pagano, M.; Pucillo, C.
APE/Ref-1 makes fine-tuning of CD40-induced B cell proliferation
Mol. Immunol.
45
3731-3739
2008
Mus musculus
Jedinak, A.; Dudhgaonkar, S.; Kelley, M.R.; Sliva, D.
Apurinic/Apyrimidinic endonuclease 1 regulates inflammatory response in macrophages
Anticancer Res.
31
379-385
2011
Mus musculus
Guikema, J.E.; Gerstein, R.M.; Linehan, E.K.; Cloherty, E.K.; Evan-Browning, E.; Tsuchimoto, D.; Nakabeppu, Y.; Schrader, C.E.
Apurinic/apyrimidinic endonuclease 2 is necessary for normal B cell development and recovery of lymphoid progenitors after chemotherapeutic challenge
J. Immunol.
186
1943-1950
2011
Mus musculus
Cho, K.J.; Kim, H.J.; Park, S.C.; Kim, H.W.; Kim, G.W.
Decisive role of apurinic/apyrimidinic endonuclease/Ref-1 in initiation of cell death
Mol. Cell. Neurosci.
45
267-276
2010
Mus musculus
Adhikari, S.; Manthena, P.V.; Kota, K.K.; Karmahapatra, S.K.; Roy, G.; Saxena, R.; Uren, A.; Roy, R.
A comparative study of recombinant mouse and human apurinic/apyrimidinic endonuclease
Mol. Cell. Biochem.
362
195-201
2012
Homo sapiens (P27695), Homo sapiens, Mus musculus (P28352), Mus musculus
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