The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The Many Functions of APE1/Ref-1: Not Only a DNA Repair Enzyme
Open accessAbstract
APE1/Ref-1 (APE1), the mammalian ortholog of Escherichia coli Xth, and a multifunctional protein possessing both DNA repair and transcriptional regulatory activities, has a pleiotropic role in controlling cellular response to oxidative stress. APE1 is the main apurinic/apyrimidinic endonuclease in eukaryotic cells, playing a central role in the DNA base excision repair pathway of all DNA lesions (uracil, alkylated and oxidized, and abasic sites), including single-strand breaks, and has also cotranscriptional activity by modulating genes expression directly regulated by either ubiquitous (i.e., AP-1, Egr-1, NFkappa-B, p53, and HIF) and tissue specific (i.e., PEBP-2, Pax-5 and -8, and TTF-1) transcription factors. In addition, it controls the intracellular redox state by inhibiting the reactive oxygen species (ROS) production. At present, information is still inadequate regarding the molecular mechanisms responsible for the coordinated control of its several activities. Both expression and/or subcellular localization are altered in several metabolic and proliferative disorders such as in tumors and aging. Here, we have attempted to coalesce the most relevant information concerning APE1's different functions in order to shed new light and to focus current and future studies to fully understand this unique molecule that is acquiring more and more interest and translational relevance in the field of molecular medicine.
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Cites
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
Radiation-induced cell cycle arrest compromised by p21 deficiency
Brugarolas, J., Chandrasekaran, C., Gordon, J. I., Beach, D., Jacks, T., & Hannon, G. J. (1995) · Nature · doi:10.1038/377552a0 · Cited by 1,242 · cited 1×
“126, and 35, 67, 88), other data underlined its potential role in controlling proapoptotic functions through p53-mediated activation of p21 (38, 54, 117), leading to the arrest of cell cycle by inhibiting cyclin-dependent kinase function (11), and cyclin G, having pro-apoptotic activity (97).”
Spitz, D. R., Azzam, E. I., Jian Li, J., & Gius, D. (2004) · Cancer and Metastasis Reviews · doi:10.1023/b:canc.0000031769.14728.bc · Cited by 710 · cited 1×
“…demonstrated that altering APE1 levels leads to blockage of cell growth and increased cancer cell sensitivity (8, 9, 16, 26, 31, 32, 55, 59, 65, 78, 80–83, 87, 98, 120, 124, 131, 138, 140, 149), these studies have either used overexpression of APE1, APE1 antisense oligonucleotides, or APE1 siRNA.”
Bernstein, C. (2002) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(02)00009-1 · Cited by 527
Zaky, A., Busso, C., Izumi, T., Chattopadhyay, R., Bassiouny, A., Mitra, S., & Bhakat, K. K. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkm1173 · Cited by 111
Cited by
Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373
Krokan, H. E., & Bjoras, M. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012583 · Cited by 1,322
Physical exercise, reactive oxygen species and neuroprotection
Radak, Z., Suzuki, K., Higuchi, M., Balogh, L., Boldogh, I., & Koltai, E. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.01.024 · Cited by 167
Gào, X., & Schöttker, B. (2017) · Oncotarget · doi:10.18632/oncotarget.17128 · Cited by 147
Fleming, A. M., Zhu, J., Ding, Y., & Burrows, C. J. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00636 · Cited by 108
Metadata
- Authors
- Tell, G., Quadrifoglio, F., Tiribelli, C., & Kelley, M. R.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2009-03
- Volume
- 11
- Issue
- 3
- Pages
- 601-619
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2012033459
- Cited by
- 516
- References
- 5
- FWCI
- 9.80
- Type
- journal article
- Language
- en
- Open access
- green
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