Biology Reference
In-Depth Information
125. Almeida KH, Sobol RW. A unified view of base excision repair:
lesion-dependent protein complexes regulated by post-trans-
lational modification.
DNA Repair (Amst)
2007;
146. Walker LJ, et al. A role for the human DNA repair enzyme HAP1
in cellular protection against DNA damaging agents and hypoxic
stress.
Nucleic Acids Res
1994;
711.
126. Parrilla-Castellar ER, Arlander SJ, Karnitz L. Dial 9-1-1 for DNA
damage: the Rad9-Hus1-Rad1 (9-1-1) clamp complex.
DNA Repair
(Amst)
2004;
6
(6):695
9.
147. Georgiadis MM, et al. Evolution of the redox function in
mammalian apurinic/apyrimidinic endonuclease.
Mutat Res
2008;
22
(23):4884
e
e
63.
148. Jayaraman L, et al. Identification of redox/repair protein Ref-1 as
a potent activator of p53.
Genes Dev
1997;
643
(1-2):54
14.
127. Shi Z, et al. S-Phase arrest by nucleoside analogues and abroga-
tion of survival without cell cycle progression by 7-hydrox-
ystaurosporine.
Cancer Res
2001;
3
(8-9):1009
e
e
70.
149. Ordway JM, Eberhart D, Curran T. Cysteine 64 of Ref-1 is not
essential for redox regulation of AP-1 DNA binding.
Mol Cell Biol
2003;
11
(5):558
e
72.
128. Guan X, et al. The human checkpoint sensor Rad9-Rad1-Hus1
interacts with and stimulates NEIL1 glycosylase.
Nucleic Acids
Res
2007;
61
(3):1065
e
66.
150. Ando K, et al. A new APE1/Ref-1-dependent pathway leading to
reduction of NF-kappaB and AP-1, and activation of their DNA-
binding activity.
Nucleic Acids Res
2008;
23
(12):4257
e
72.
129. Guan X, et al. The human checkpoint sensor Rad9-Rad1-Hus1
interacts with and stimulates DNA repair enzyme TDG glyco-
sylase.
Nucleic Acids Res
2007;
35
(8):2463
e
36.
151. Tell G, Fantini D, Quadrifoglio F. Understanding different func-
tions of mammalian AP endonuclease (APE1) as a promising tool
for cancer treatment.
Cell Mol Life Sci
2010;
36
(13):4327
e
18.
130. Gembka A, et al. The checkpoint clamp, Rad9-Rad1-Hus1
complex, preferentially stimulates the activity of apurinic/apyr-
imidinic endonuclease 1 and DNA polymerase beta in long patch
base excision repair.
Nucleic Acids Res
2007;
35
(18):6207
e
608.
152. Okazaki T, et al. A redox factor protein, ref1, is involved in
negative gene regulation by extracellular calcium.
J Biol Chem
1994;
67
(21):3589
e
608.
131. Toueille M, et al. The human Rad9/Rad1/Hus1 damage sensor
clamp interacts with DNA polymerase beta and increases its
DNA substrate utilisation efficiency:
35
(8):2596
e
62.
153. Mallette LE. Regulation of blood calcium in humans.
Endocrinol
Metab Clin North Am
1989;
269
(45):27855
e
10.
154. Izumi T, Henner WD, Mitra S. Negative regulation of the major
human AP-endonuclease, a multifunctional protein.
Biochemistry
1996;
18
(3):601
e
implications for DNA
24.
132. Wang W, et al. The human Rad9-Rad1-Hus1 checkpoint complex
stimulates flap endonuclease 1.
Proc Natl Acad Sci, USA
2004;
repair.
Nucleic Acids Res
2004;
32
(11):3316
e
83.
155. Bhakat KK, et al. Role of acetylated human AP-endonuclease
(APE1/Ref-1) in regulation of the parathyroid hormone gene.
EMBO J
2003;
35
(47):14679
e
7.
133. Smirnova E, et al. The human checkpoint sensor and alternative
DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA
ligase I, a component of the long-patch base excision repair
machinery.
Biochem J
2005;
101
(48):16762
e
309.
156. Barzilay G, et al. Site-directed mutagenesis of the human DNA
repair enzyme HAP1: identification of residues important for AP
endonuclease
22
(23):6299
e
7.
134. Xanthoudakis S, Curran T. Identification and characterization of
Ref-1, a nuclear protein that
389
(Pt 1):13
e
and RNase H activity.
Nucleic Acids Res
50.
157. Chattopadhyay R, et al. Regulatory role of human AP-endonu-
clease (APE1/Ref-1) in YB-1-mediated activation of the multi-
drug resistance gene MDR1.
Mol Cell Biol
2008;
1995;
23
(9):1544
e
facilitates AP-1 DNA-binding
65.
135. Harrison L, et al. Human apurinic endonuclease gene (APE):
structure and genomic mapping (chromosome 14q11.2-12).
Hum
Mol Genet
1992;
activity.
EMBO J
1992;
11
(2):653
e
80.
158. Marenstein DR, Wilson 3rd DM, Teebor GW. Human AP endo-
nuclease (APE1) demonstrates endonucleolytic activity against
AP sites in single-stranded DNA.
DNA Repair (Amst)
2004;
28
(23):7066
e
80.
136. Akiyama K, et al. Structure, promoter analysis and chromosomal
assignment of the human APEX gene.
Biochim Biophys Acta
1994;
1
(9):677
e
3
(5):
33.
159. Berquist BR, McNeill DR, Wilson 3rd DM. Characterization of
abasic endonuclease activity of human Ape1 on alternative
substrates, as well as effects of ATP and sequence context on AP
site incision.
J Mol Biol
2008;
527
e
25.
137. Yu E, Gaucher S, Hadi MZ. Probing conformational changes in
Ape1 during the progression of base excision repair.
Biochemistry
2010;
1219
(1):15
e
96.
138. Tell G, et al. The intracellular localization of APE1/Ref-1: more
than a passive phenomenon?
Antioxid Redox Signal
2005;
49
(18):3786
e
27.
160. Tanaka M, Chock B, Stadtman ER. Oxidized messenger
RNA induces translation errors.
Proc Natl Acad Sci, USA
2007;
104
379
(1):17
e
7
(3-4):
84.
139. Moran LK, Gutteridge JM, Quinlan GJ. Thiols in cellular redox
signalling and control.
Curr Med Chem
2001;
367
e
71.
161. Moreira I, et al. Nucleic acid oxidation in Alzheimer disease.
Free
Radic Biol Med
2008;
(1):66
e
72.
140. Gaiddon C, Moorthy NC, Prives C. Ref-1 regulates the trans-
activation and pro-apoptotic functions of p53 in vivo.
EMBO J
1999;
8
(7):763
e
505.
162. Asai T, et al. Increase in Ref-1 mRNA and protein by thyrotropin
in rat
44
(8):1493
e
thyroid FRTL-5 cells.
Biochem Biophys Res Commun
21.
141. Xanthoudakis S, et al. Redox activation of Fos-Jun DNA binding
activity is mediated by a DNA repair enzyme.
EMBO J
1992;
18
(20):5609
e
4.
163. Tell G, et al. TSH controls Ref-1 nuclear translocation in thyroid
cells.
J Mol Endocrinol
2000;
1997;
236
(1):71
e
90.
164. Ramana CV, et al. Activation of apurinic/apyrimidinic endonu-
clease in human cells by reactive oxygen species and its corre-
lation with their adaptive response to genotoxicity of
24
(3):383
e
35.
142. Nishi T, et al. Spatial redox regulation of a critical cysteine
residue of NF-kappa B in vivo.
J Biol Chem
2002;
11
(9):3323
e
56.
143. Huang R, Adamson ED. Characterization of the DNA-binding
properties of the early growth response-1 (Egr-1) transcription
factor: evidence for modulation by a redox mechanism.
DNA Cell
Biol
1993;
277
(46):44548
e
free
6.
165. Tell G, et al. The many functions of APE1/Ref-1: not only a DNA
repair enzyme.
Antioxid Redox Signal
2009;
radicals.
Proc Natl Acad Sci, USA
1998;
95
(9):5061
e
20.
166. Busso CS, Lake MW, Izumi T. Posttranslational modification of
mammalian AP endonuclease
11
(3):601
e
73.
144. Tell G, et al. Ref-1 controls pax-8 DNA-binding activity.
Biochem
Biophys Res Commun
1998;
12
(3):265
e
(APE1).
Cell Mol Life Sci
83.
145. Walker LJ, et al. Identification of residues in the human DNA
repair enzyme HAP1 (Ref-1) that are essential for redox regula-
tion of Jun DNA binding.
Mol Cell Biol
1993;
252
(1):178
20.
167. Fantini D, et al. Critical lysine residues within the overlooked N-
terminal domain of human APE1 regulate its biological functions.
Nucleic Acids Res
2010;
2010;
67
(21):3609
e
e
13
(9):5370
e
6.
38
(22):8239
e
56.
