Nicotinamide treatment reduces the levels of oxidative stress, apoptosis, and PARP-1 activity in Aβ(1–42)-induced rat model of Alzheimer's disease
Abstract
The underlying mechanisms of Alzheimer's Disease (AD) are still unclear. It is suggested that poly(ADP-ribose) polymerase-1 (PARP-1) overactivation can cause neuroinflammation and cell death. In this study we searched the effects of nicotinamide (NA), endogenous PARP-1 inhibitor, on oxidative stress, apoptosis, and the regulation of PARP-1 and nuclear factor kappa B (NF-κB) in amyloid beta peptide (1-42) (Aβ(1-42))-induced neurodegeneration. Sprague-Dawley rats were divided into four groups as control, Aβ(1-42), Aβ(1-42) + NA(100 and 500 mg/kg). All groups were stereotaxically injected bilaterally into the hippocampus with Aβ(1-42) or saline. After surgery NA administrations were made intraperitoneally (ip) for 7 days. In order to investigate the effects of Aβ(1-42) and NA, protein carbonyls, lipid peroxidation, reactive oxygen species (ROS) production, glutathione (GSH) levels, activities of antioxidant enzymes (catalase, superoxide dismutase, glutathione peroxidase), mitochondrial function, mRNA and protein levels of PARP-1, NF-κB, p53, Bax, and Bcl-2 were measured in specific brain regions such as cortex and hippocampus. Aβ(1-42) treatment only increased the oxidative stress parameters and caused decline in antioxidant enzyme activities, mitochondrial function, and GSH levels. Also, overexpression of PARP-1, NF-κB, p53, Bax, and the decreased levels of Bcl-2 were observed in Aβ(1-42)-treated group. NA treatments against Aβ(1-42)-upregulated Bcl-2 and downregulated PARP-1, NF-κB, p53, and Bax levels. NA treatments also decreased the oxidative stress parameters and elevated antioxidant enzyme activities, GSH levels, and mitochondrial function against Aβ(1-42) treatment. These data suggest that NA may have a therapeutic potential in neurodegenerative processes due to the decreased levels of oxidative stress, apoptosis, and PARP-1 activity.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In vivo studies using various Alzheimer disease and Parkinson disease models have shown that loss of PARP1 protects from brain dysfunctions and cognitive decline.
“In vivo studies using various Alzheimer disease and Parkinson disease models have shown that loss of PARP1 protects from brain dysfunctions and cognitive decline170–174.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [171]
PARP1 activation is associated with Alzheimer disease and Parkinson disease pathogenesis.
“PARP1 activation is also associated with Alzheimer disease170,171 and Parkinson disease172,173 pathogenesis.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [171]
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860 · see citing works
The rat brain in stereotaxic coordinates
Palkovits, M. (1983) · Neuropeptides · doi:10.1016/0143-4179(83)90049-5 · Cited by 28,959 · see citing works
The Rat Brain in Stereotaxic Coordinates
Paxinos, G., & Watson, C. (1983) · Elsevier eBooks · doi:10.1016/c2009-0-63235-9 · Cited by 28,585 · see citing works
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,824 · see citing works
Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.
Paglia, D. E., & Valentine, W. N. (1967) · PubMed · Cited by 10,776 · see citing works
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · see citing works
[43] Malondialdehyde determination as index of lipid Peroxidation
Draper, H. H., & Hadley, M. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86135-i · Cited by 4,291 · see citing works
Bustin, S. A. (2000) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0250169 · Cited by 3,844 · see citing works
Oxidative DNA damage: mechanisms, mutation, and disease
Cooke, M. S., Evans, M. D., Dizdaroglu, M., & Lunec, J. (2003) · The FASEB Journal · doi:10.1096/fj.02-0752rev · Cited by 3,245 · see citing works
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052 · see citing works
Chomczyński, P. (1993) · PubMed · Cited by 2,788 · see citing works
[38] Oxidative damage to proteins: Spectrophotometric method for carbonyl assay
Reznick, A. Z., & Packer, L. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33041-7 · Cited by 2,455 · see citing works
A simple method for determination of serum catalase activity and revision of reference range
Góth, L. (1991) · Clinica Chimica Acta · doi:10.1016/0009-8981(91)90067-m · Cited by 2,391 · see citing works
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383 · see citing works
Wang, H., & Joseph, J. A. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00107-0 · Cited by 2,355 · see citing works
Metabolism and functions of glutathione in brain
Dringen, R. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00060-x · Cited by 1,702 · see citing works
Apoptosis in neurodegenerative disorders
Mattson, M. P. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35040009 · Cited by 1,605 · see citing works
Microglia and inflammation-mediated neurodegeneration: Multiple triggers with a common mechanism
Block, M. L., & Hong, J.-S. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.06.004 · Cited by 1,557 · see citing works
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works
The Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors
Virág, L., & Szabó, C. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.375 · Cited by 1,373 · see citing works
Pain: Moving from Symptom Control toward Mechanism-Specific Pharmacologic Management
Woolf, C. (2004) · Annals of Internal Medicine · doi:10.7326/0003-4819-140-8-200404200-00010 · Cited by 1,134 · see citing works
Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid β-peptide
Butterfield, D. A., Drake, J., Pocernich, C., & Castegna, A. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02173-6 · Cited by 1,114 · see citing works
Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD + into a nuclear signalPreprint
Kim, M. Y., Zhang, T., & Kraus, W. L. (2005) · Genes & Development · doi:10.1101/gad.1331805 · Cited by 803 · see citing works
Kruman, I. I., Culmsee, C., Chan, S. L., Kruman, Y., Guo, Z., Penix, L., & Mattson, M. P. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-18-06920.2000 · Cited by 784 · see citing works
Kaltschmidt, B., Uherek, M., Volk, B., Baeuerle, P. A., & Kaltschmidt, C. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2642 · Cited by 611 · see citing works
Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?
Shall, S., & de MURCIA, G. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00016-1 · Cited by 534 · see citing works
Increased peroxidation and reduced antioxidant enzyme activity in Alzheimer's disease
Marcus, D. L., Thomas, C., Rodriguez, C., Simberkoff, K., Tsai, J. S., Strafaci, J. A., & Freedman, M. L. (1998) · Experimental Neurology · doi:10.1006/exnr.1997.6750 · Cited by 513 · see citing works
Protection against reactive oxygen species by selenoproteins
Steinbrenner, H., & Sies, H. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.02.014 · Cited by 513 · see citing works
Poly (ADP-ribose) polymerase, nitric oxide and cell death
Pieper, A. A. (1999) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(99)01292-4 · Cited by 512 · see citing works
The importance of neuritic plaques and tangles to the development and evolution of AD
Tiraboschi, P., Hansen, L. A., Thal, L. J., & Corey-Bloom, J. (2004) · Neurology · doi:10.1212/01.wnl.0000129697.01779.0a · Cited by 477 · see citing works
Parthanatos, a messenger of death
David, K. K. (2009) · Frontiers in Bioscience · doi:10.2741/3297 · Cited by 450 · see citing works
Acrolein is increased in Alzheimer’s disease brain and is toxic to primary hippocampal cultures
Lovell, M. A., Xie, C., & Markesbery, W. R. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00235-9 · Cited by 449 · see citing works
Keller, J. N., Pang, Z., Geddes, J. W., Begley, J. G., Germeyer, A., Waeg, G., & Mattson, M. P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69010273.x · Cited by 439 · cited 2× · see citing works
“or cerebrospinal fl uids of patients with AD [57,68,69].”
BackgroundMethodSafety of high-dose nicotinamide: a review
Knip, M., Douek, I. F., Moore, W. P. T., Gillmor, H. A., McLean, A. E. M., Bingley, P. J., & Gale, E. A. M. (2000) · Diabetologia · doi:10.1007/s001250051536 · Cited by 423 · see citing works
Zhang, Y., McLaughlin, R., Goodyer, C., & LeBlanc, A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110119 · Cited by 418 · see citing works
Green, K. N., Steffan, J. S., Martinez-Coria, H., Sun, X., Schreiber, S. S., Thompson, L. M., & LaFerla, F. M. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3203-08.2008 · Cited by 404 · cited 1× · see citing works
“with microtubule depolymerization [65].”
Mandir, A. S., Przedborski, S., Jackson-Lewis, V., Wang, Z.-Q., Simbulan-Rosenthal, C. M., Smulson, M. E., Hoffman, B. E., Guastella, D. B., Dawson, V. L., & Dawson, T. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5774 · Cited by 382 · see citing works
Alzheimer Disease: Mechanistic Understanding Predicts Novel Therapies
Selkoe, D. J. (2004) · Annals of Internal Medicine · doi:10.7326/0003-4819-140-8-200404200-00047 · Cited by 381 · see citing works
Evolution of Poly(ADP-ribose) Polymerase-1 (PARP-1) Inhibitors. From Concept to Clinic
Ferraris, D. V. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100012m · Cited by 375 · see citing works
Elevation of Glutathione as a Therapeutic Strategy in Alzheimer Disease
Pocernich, C., & Butterfield, D. (2011) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2011.10.003 · Cited by 333 · see citing works
Role of Oxidative Stress in the Progression of Alzheimer's Disease
Rukhsana Sultana, A., & Butterfield, D. A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1222 · Cited by 327 · see citing works
Paradis, E., Douillard, H., Koutroumanis, M., Goodyer, C. G., & LeBlanc, A. C. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-23-07533.1996 · Cited by 325 · see citing works
Correlates of p53- and Fas (CD95)-mediated apoptosis in Alzheimer's disease
de la Monte, S. M., Sohn, Y. K., & Wands, J. R. (1997) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(97)00131-7 · Cited by 307 · see citing works
Bürkle, A. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04864.x · Cited by 294 · see citing works
Rukhsana Sultana, A., Marzia Perluigi, A., & Butterfield, D. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2021 · Cited by 259 · see citing works
Increased poly(ADP-ribosyl)ation of nuclear proteins in Alzheimer's disease
Love, S., Barber, R., & Wilcock, G. K. (1999) · Brain · doi:10.1093/brain/122.2.247 · Cited by 254 · see citing works
Liu, D., Pitta, M., Jiang, H., Lee, J.-H., Zhang, G., Chen, X., Kawamoto, E. M., & Mattson, M. P. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.020 · Cited by 238 · see citing works
Nicotinamide is a potent inhibitor of proinflammatory cytokines
Ungerstedt, J. S., Blombäck, M., & Söderström, T. (2003) · Clinical & Experimental Immunology · doi:10.1046/j.1365-2249.2003.02031.x · Cited by 222 · see citing works
Chiarugi, A., & Moskowitz, M. A. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01684.x · Cited by 216 · see citing works
NMDA But Not Non-NMDA Excitotoxicity is Mediated by Poly(ADP-Ribose) Polymerase
Mandir, A. S., Poitras, M. F., Berliner, A. R., Herring, W. J., Guastella, D. B., Feldman, A. B., Poirier, G. G., Wang, Z., Dawson, T. M., & Dawson, V. L. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-21-08005.2000 · Cited by 213 · see citing works
Poly(ADP-ribose) Polymerase-1 in the Nervous System
Ha, H. C., & Snyder, S. H. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0324 · Cited by 196 · see citing works
Nicotinamide: necessary nutrient emerges as a novel cytoprotectant for the brain
Maiese, K., & Chong, Z. Z. (2003) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(03)00078-6 · Cited by 187 · see citing works
Decreased base excision repair and increased helicase activity in Alzheimer's disease brain
Lovell, M. A., Xie, C., & Markesbery, W. R. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02335-5 · Cited by 174 · see citing works
β-amyloid activates PARP causing astrocytic metabolic failure and neuronal death
Abeti, R., Abramov, A. Y., & Duchen, M. R. (2011) · Brain · doi:10.1093/brain/awr104 · Cited by 172 · see citing works
Debra Boyd-kimball, A., Rukhsana Sultana, A., Poon, H. F., Lynn, B. C., Casamenti, F., Pepeu, G., Klein, J. B., & Butterfield, D. A. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.12.022 · Cited by 166 · see citing works
Flood, J. F., Morley, J. E., & Roberts, E. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3363 · Cited by 164 · see citing works
Cecchi, C., Fiorillo, C., Sorbi, S., Latorraca, S., Nacmias, B., Bagnoli, S., Nassi, P., & Liguri, G. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01049-3 · Cited by 159 · see citing works
Neurovascular function in Alzheimer's disease patients and experimental models
Nicolakakis, N., & Hamel, E. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2011.43 · Cited by 156 · see citing works
Role of p53 in Neurodegenerative Diseases
Chang, J. R., Ghafouri, M., Mukerjee, R., Bagashev, A., Chabrashvili, T., & Sawaya, B. E. (2011) · Neurodegenerative Diseases · doi:10.1159/000329999 · Cited by 145 · see citing works
Diagnosis and biomarkers of predementia in Alzheimer's disease
Forlenza, O. V., Diniz, B. S., & Gattaz, W. F. (2010) · BMC Medicine · doi:10.1186/1741-7015-8-89 · Cited by 145 · see citing works
Bax expression in mammalian neurons undergoing apoptosis, and in Alzheimer's disease hippocampus
MacGibbon, G. A., Lawlor, P. A., Sirimanne, E. S., Walton, M. R., Connor, B. J., Young, D., Williams, C. E., Gluckman, P. D., Faull, R. L. M., Hughes, P. E., et al. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01351-0 · Cited by 140 · see citing works
Chong, Z. Z., Lin, S., Li, F., & Maiese, K. (2005) · Current Neurovascular Research · doi:10.2174/156720205774322584 · Cited by 126 · see citing works
Nguewa, P., Fuertes, M. A., Valladares, B., Alonso‐Moreno, C., & Pérez, J. M. (2004) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2004.01.001 · Cited by 119 · see citing works
Free radical-mediated damage to brain in Alzheimer's disease and its transgenic mouse models
Sonnen, J. A., Breitner, J. C. S., Lovell, M. A., Markesbery, W. R., Quinn, J. F., & Montine, T. J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.04.022 · Cited by 103 · see citing works
Beauvieux, M.-C., Peuchant, E., Dumon, M. F., Receveur, M. C., Bras, M. L., & Clerc, M. (1995) · Clinical Biochemistry · doi:10.1016/0009-9120(94)00071-3 · Cited by 96 · see citing works
Proteomics in animal models of Alzheimer's and Parkinson's diseases
Robinson, R. A. S., Owen, J. B., & Butterfield, D. A. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2008.07.003 · Cited by 81 · see citing works
Cenini, G., Sultana, R., Memo, M., & Butterfield, D. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.015 · Cited by 79 · see citing works
Oxidants and antioxidants revisited. New concepts of oxidative stress
Packer, L., & Cadenas, E. (2007) · Free Radical Research · doi:10.1080/10715760701490975 · Cited by 78 · see citing works
Activation of PARP by Oxidative Stress Induced by β-Amyloid: Implications for Alzheimer’s Disease
Abeti, R., & Duchen, M. R. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0895-x · Cited by 78 · see citing works
Sakakibara, Y., Mitha, A. P., Ogilvy, C. S., & Maynard, K. I. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)00854-5 · Cited by 76 · see citing works
Induction of oxidative stress by L‐2‐hydroxyglutaric acid in rat brain
Latini, A., Scussiato, K., Rosa, R. B., Leipnitz, G., Llesuy, S., Belló‐Klein, A., Dutra‐Filho, C. S., & Wajner, M. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10735 · Cited by 69 · see citing works
Li, S., Cui, N., Zhang, C., Zhao, X., Yu, S.-F., & Xie, K. (2005) · Toxicology · doi:10.1016/j.tox.2005.08.018 · Cited by 69 · see citing works
Extracellular chaperones prevent Aβ42-induced toxicity in rat brains
Cascella, R., Conti, S., Tatini, F., Evangelisti, E., Scartabelli, T., Casamenti, F., Wilson, M. R., Chiti, F., & Cecchi, C. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.012 · Cited by 68 · see citing works
Behavioural and cellular effects of exogenous amyloid-β peptides in rodents.
Chambon, C., Wegener, N., Gravius, A., & Danysz, W. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.08.024 · Cited by 64 · see citing works
Alzheimer’s disease and Alzheimer’s dementia: distinct but overlapping entities
Blass, J. P. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00036-2 · Cited by 62 · see citing works
Navigating novel mechanisms of cellular plasticity with the NAD+ precursor and nutrient nicotinamide
Li, F. (2004) · Frontiers in bioscience · doi:10.2741/1412 · Cited by 61 · see citing works
Evaluation of the poly(ADP‐ribose) polymerase‐1 gene variants in Alzheimer's disease
Liu, H., Lin, W., Wu, B., Liu, S. R., Wang, W., Tsai, C., Lee, C., & Tsai, F. (2010) · Journal of Clinical Laboratory Analysis · doi:10.1002/jcla.20379 · Cited by 54 · see citing works
Zampagni, M., Wright, D., Cascella, R., D’Adamio, G., Casamenti, F., Evangelisti, E., Cardona, F., Goti, A., Nacmias, B., Sorbi, S., et al. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.012 · Cited by 54 · see citing works
Wu, G., Nan, C., Rollo, J. C., Huang, X., & Tian, J. (2010) · Journal of Biomedical Science · doi:10.1186/1423-0127-17-16 · Cited by 52 · see citing works
Propentofylline protects β-amyloid protein-induced apoptosis in cultured rat hippocampal neurons
Koriyama, Y., Chiba, K., & Mohri, T. (2002) · European Journal of Pharmacology · doi:10.1016/s0014-2999(02)02789-9 · Cited by 48 · see citing works
GPI 6150 Prevents H2O2 Cytotoxicity by Inhibiting Poly(ADP-ribose) Polymerase
Zhang, J., Lautar, S. L., Huang, S. H., Ramsey, C., Cheung, A., & Li, J.-H. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3816 · Cited by 44 · see citing works
Pandya, K. G., Patel, M. R., & Lau‐Cam, C. A. (2010) · Journal of Biomedical Science · doi:10.1186/1423-0127-17-s1-s16 · Cited by 42 · see citing works
Poly ADP-ribose polymerase-1 and health
Kirkland, J. B. (2010) · Experimental Biology and Medicine · doi:10.1258/ebm.2010.009280 · Cited by 40 · see citing works
Mechanism of amyloid β protein induced neuronal cell death: current concepts and future perspectives
Behl, C., & Sagara, Y. (1997) · Springer eBooks · doi:10.1007/978-3-7091-6844-8_14 · Cited by 35 · see citing works
Morel, P., Fauconneau, B., Page, G., Mirbeau, T., & Huguet, F. (1998) · Neuroscience Research · doi:10.1016/s0168-0102(98)00080-7 · Cited by 33 · see citing works
Bonnet, J.-J., & Costentin, J. (1989) · Life Sciences · doi:10.1016/0024-3205(89)90563-8 · Cited by 33 · see citing works
Intrinsic Mechanisms of Poly(ADP-Ribose) Neurotoxicity: Three Hypotheses
Chiarugi, A. (2005) · NeuroToxicology · doi:10.1016/j.neuro.2005.01.012 · Cited by 32 · see citing works
Pepeu, G., Giovannelli, L., Casamenti, F., Cali, C., & Bartolini, L. (1996) · Progress in brain research · doi:10.1016/s0079-6123(08)62111-1 · Cited by 26 · see citing works
Neurodegenerative Disorders and Cholesterol
Michikawa, M. (2004) · Current Alzheimer Research · doi:10.2174/1567205043331983 · Cited by 23 · see citing works
Yalçın, A., Armağan, G., Turunç, E., Konyalıoğlu, S., & Kanıt, L. (2010) · Free Radical Research · doi:10.3109/10715761003645964 · Cited by 16 · see citing works
Turunç, E., Kanıt, L., & Yalçın, A. (2010) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.2010.01122.x · Cited by 11 · see citing works
Uyanıkgil, Y., Turgut, M., Ateş, U., Baka, M., & Yurtseven, M. (2005) · Developmental Brain Research · doi:10.1016/j.devbrainres.2005.07.004 · Cited by 11 · see citing works
Baka, M., Uyanıkgil, Y., Yurtseven, M., & Turgut, M. (2004) · Child s Nervous System · doi:10.1007/s00381-004-1010-7 · Cited by 10 · see citing works
Flagged first, then by citations
1 of the 95 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648 · see citing works
NAD+ metabolism and its roles in cellular processes during ageing
Covarrubias, A. J., Perrone, R., Grozio, A., & Verdin, E. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00313-x · Cited by 1,617 · see citing works
Mitophagy and Alzheimer’s Disease: Cellular and Molecular Mechanisms
Kerr, J. S., Adriaanse, B. A., Greig, N. H., Mattson, M. P., Cader, M. Z., Bohr, V. A., & Fang, E. F. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.01.002 · Cited by 870 · see citing works
NAD+ homeostasis in health and disease
Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627 · see citing works
Lou, G., Palikaras, K., Lautrup, S., Scheibye‐Knudsen, M., Tavernarakis, N., & Fang, E. F. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.07.002 · Cited by 450 · see citing works
Oxidative and nitrative stress in neurodegeneration
Cobb, C. A., & Cole, M. P. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.04.020 · Cited by 300 · see citing works
Braidy, N., Berg, J., Clement, J., Khorshidi, F., Poljak, A., Jayasena, T., Grant, R., & Sachdev, P. S. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7269 · Cited by 286 · see citing works
Mitophagy in Alzheimer’s Disease and Other Age-Related Neurodegenerative Diseases
Cai, Q., & Jeong, Y. Y. (2020) · Cells · doi:10.3390/cells9010150 · Cited by 263 · see citing works
PARP-1 involvement in neurodegeneration: A focus on Alzheimer’s and Parkinson’s diseases
Martire, S., Mosca, L., & D’Erme, M. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.04.001 · Cited by 228 · see citing works
Neuronal cell death mechanisms in Alzheimer’s disease: An insight
Goel, P., Chakrabarti, S., Goel, K., Bhutani, K., Chopra, T., & Bali, S. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.937133 · Cited by 235 · see citing works
Modulating NAD+ metabolism, from bench to bedside
Katsyuba, E., & Auwerx, J. H. (2017) · The EMBO Journal · doi:10.15252/embj.201797135 · Cited by 224 · see citing works
Mitochondrial Dysfunction: a Potential Therapeutic Target to Treat Alzheimer’s Disease
Nand, S., Singh, C., Singh, A., Singh, M. P., & Singh, S. P. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01945-y · Cited by 213 · see citing works
The Influence of Nicotinamide on Health and Disease in the Central Nervous System
Fricker, R. A., Green, E. L., Jenkins, S. I., & Griffin, S. M. (2018) · International Journal of Tryptophan Research · doi:10.1177/1178646918776658 · Cited by 200 · see citing works
Apoptotic Pathways and Alzheimer’s Disease: Probing Therapeutic Potential
Sharma, V., Singh, T. G., Singh, S., Garg, N., & Dhiman, S. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03418-7 · Cited by 197 · see citing works
Emerging therapeutic roles for NAD+ metabolism in mitochondrial and age‐related disorders
Srivastava, S. (2016) · Clinical and Translational Medicine · doi:10.1186/s40169-016-0104-7 · Cited by 193 · see citing works
Apoptosis and its therapeutic implications in neurodegenerative diseases
Erekat, N. S. (2021) · Clinical Anatomy · doi:10.1002/ca.23792 · Cited by 163 · see citing works
Gorji, N., Moeini, R., & Memariani, Z. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.12.003 · Cited by 154 · see citing works
The Safety and Antiaging Effects of Nicotinamide Mononucleotide in Human Clinical Trials: an Update
Song, Q., Zhou, X., Xu, K., Liu, S., Zhu, X., & Yang, J. J. (2023) · Advances in Nutrition · doi:10.1016/j.advnut.2023.08.008 · Cited by 122 · see citing works
Prakash, A. K., & Kumar, A. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.07.036 · Cited by 116 · see citing works
Nuclear poly(ADP-ribose) activity is a therapeutic target in amyotrophic lateral sclerosis
McGurk, L., Mojsilovic‐Petrovic, J., Deerlin, V. M. V., Shorter, J., Kalb, R. G., Lee, V. M., Trojanowski, J. Q., Lee, E. B., & Bonini, N. M. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0586-1 · Cited by 112 · see citing works
Cell Death Mechanisms of Neurodegeneration
Fan, J., Dawson, T. M., & Dawson, V. L. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-57193-5_16 · Cited by 112 · see citing works
Poly (ADP-ribose) (PAR)-dependent cell death in neurodegenerative diseases
Park, H., Kam, T., Dawson, T. M., & Dawson, V. L. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2019.12.009 · Cited by 105 · see citing works
WISP1: Clinical Insights for a Proliferative and Restorative Member of the CCN Family
Maiese, K. (2014) · Current Neurovascular Research · doi:10.2174/1567202611666140912115107 · Cited by 103 · see citing works
Mitochondria-Targeted Protective Compounds in Parkinson’s and Alzheimer’s Diseases
Fernández‐Moriano, C., González‐Burgos, E., & Gómez-Serranillos, M. P. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/408927 · Cited by 94 · see citing works
Poly (ADP-ribose) polymerase-1 as a promising drug target for neurodegenerative diseases
Thapa, K., Khan, H., Sharma, U., Grewal, A. K., & Singh, T. G. (2021) · Life Sciences · doi:10.1016/j.lfs.2020.118975 · Cited by 92 · see citing works
Nicotinamide reduces renal interstitial fibrosis by suppressing tubular injury and inflammation
Zheng, M., Cai, J., Liu, Z., Shu, S., Wang, Y., Tang, C., & Dong, Z. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14285 · Cited by 91 · see citing works
Zhang, Y., & Zhao, J. (2015) · DNA and Cell Biology · doi:10.1089/dna.2014.2738 · Cited by 88 · see citing works
Salech, F., Ponce, D. P., Paula-Lima, A. C., SanMartín, C. D., & Behrens, M. I. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00255 · Cited by 89 · see citing works
Zarei, I., Brown, D. G., Nealon, N. J., & Ryan, E. P. (2017) · Rice · doi:10.1186/s12284-017-0157-2 · Cited by 87 · see citing works
Coffee intake and decreased amyloid pathology in human brain
Kim, J. W., Byun, M. S., Yi, D., Lee, J. H., Jeon, S. Y., Jung, G., Lee, H. N., Sohn, B. K., Lee, J.-Y., Kim, Y. K., et al. (2019) · Translational Psychiatry · doi:10.1038/s41398-019-0604-5 · Cited by 86 · see citing works
Taking aim at Alzheimer’s disease through the mammalian target of rapamycin
Maiese, K. (2014) · Annals medicus · doi:10.3109/07853890.2014.941921 · Cited by 76 · see citing works
Parthanatos in the pathogenesis of nervous system diseases
Wang, X., & Ge, P. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.09.049 · Cited by 75 · see citing works
Resveratrol Inhibits Trophoblast Apoptosis through Oxidative Stress in Preeclampsia-Model Rats
Zou, Y., Zuo, Q., Huang, S., Yu, X., Jiang, Z., Zou, S., Fan, M., & Sun, L. (2014) · Molecules · doi:10.3390/molecules191220570 · Cited by 75 · see citing works
Sarkar, B., Dhiman, M., Mittal, S., & Mantha, A. K. (2017) · Metabolic Brain Disease · doi:10.1007/s11011-017-0093-2 · Cited by 73 · see citing works
Free-radical scavenging by tryptophan and its metabolites through electron transfer based processes
Pérez‐González, A., Alvarez-Idaboy, J. R., & Galano, A. (2015) · Journal of Molecular Modeling · doi:10.1007/s00894-015-2758-2 · Cited by 72 · see citing works
More, J., Galusso, N., Veloso, P., Montecinos, L., Finkelstein, J. P., Sánchez, G., Bull, R., Valdés, J. L., Hidalgo, C., & Paula-Lima, A. C. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00399 · Cited by 71 · see citing works
Xu, X., Sun, B., & Zhao, C. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106314 · Cited by 70 · see citing works
Forsythiaside Protects Against Hydrogen Peroxide-Induced Oxidative Stress and Apoptosis in PC12 Cell
Huang, C., Lin, Y., Su, H., & Ye, D. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1461-5 · Cited by 68 · see citing works
Hosseini, L., Farokhi-Sisakht, F., Badalzadeh, R., Khabbaz, A., Mahmoudi, J., & Sadigh‐Eteghad, S. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.09.037 · Cited by 66 · see citing works
Supplementation with NAD+ and Its Precursors to Prevent Cognitive Decline across Disease Contexts
Campbell, J. M. (2022) · Nutrients · doi:10.3390/nu14153231 · Cited by 62 · see citing works
Li, J., Wen, P., Li, W., & Zhou, J. (2015) · Neuroreport · doi:10.1097/wnr.0000000000000419 · Cited by 61 · see citing works
B Vitamins and Fatty Acids: What Do They Share with Small Vessel Disease-Related Dementia?
Moretti, R., & Peinkhofer, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225797 · Cited by 57 · see citing works
Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity
Brady, P. N., Goel, A., & Johnson, M. A. (2019) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00038-18 · Cited by 58 · see citing works
Regeneration in the nervous system with erythropoietin
Maiese, K. (2015) · Frontiers in bioscience · doi:10.2741/4408 · Cited by 54 · see citing works
Wang, X., He, H., Xiong, X., Zhou, S., Wang, W., Feng, L., Han, R., & Xie, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.668491 · Cited by 54 · see citing works
The Carbamate Aldicarb Altered the Gut Microbiome, Metabolome, and Lipidome of C57BL/6J Mice
Gao, B., Chi, L., Tu, P., Gao, N., & Lü, K. (2018) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.8b00179 · Cited by 52 · see citing works
Wang, Y., Dong, J., Nie, J., Zhu, J., Wang, H., Chen, Q., Chen, J., Xia, J.-M., & Shuai, W. (2017) · APOPTOSIS · doi:10.1007/s10495-017-1393-z · Cited by 51 · see citing works
New Insights for nicotinamide Metabolic disease autophagy and mTOR
Maiese, K. (2020) · Frontiers in bioscience · doi:10.2741/4886 · Cited by 53 · see citing works
Dailah, H. G. (2022) · Molecules · doi:10.3390/molecules27217207 · Cited by 50 · see citing works
Perinatal asphyxia: CNS development and deficits with delayed onset
Herrera‐Marschitz, M., Neira-Peña, T., Rojas-Mancilla, E., Espina-Marchant, P., Esmar, D., Perez, R. S., Muñoz, V., Gutierrez-Hernandez, M., Rivera, B., Simola, N., et al. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00047 · Cited by 50 · see citing works
Liu, C., & Fang, Y. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.04.028 · Cited by 50 · see citing works
Troxerutin protects hippocampal neurons against amyloid beta-induced oxidative stress and apoptosis
Farajdokht, F., Amani, M., Mirzaei, F., Alihemmati, A., Mohaddes, G., & Babri, S. (2017) · EXCLI journal · doi:10.17179/excli2017-526 · Cited by 48 · see citing works
Cioancă, O., Hăncianu, M., Mihăşan, M., & Hriţcu, L. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1550-0 · Cited by 47 · see citing works
Xiao, Y. M., Dai, Y., Li, L., Geng, F., Xu, Y., Wang, J., Wang, S., & Zhao, J. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111651 · Cited by 45 · see citing works
Koh, E.-J., Kim, K.-J., Choi, J., Kang, D.-H., & Lee, B.-Y. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.02.057 · Cited by 43 · see citing works
Programming Apoptosis and Autophagy with Novel Approaches for Diabetes Mellitus
Maiese, K. (2015) · Current Neurovascular Research · doi:10.2174/1567202612666150305110929 · Cited by 43 · see citing works
Poly (ADP-ribose) polymerase 1 and neurodegenerative diseases: past, present, and future
Hu, M.-L., Pan, Y.-R., Yong, Y.-Y., Liu, Y., Yu, L., Qin, D.-L., Qiao, G., Law, B. Y.-K., Wu, J.-M., Zhou, X.-G., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102078 · Cited by 44 · see citing works
PARP-1-Associated Pathological Processes: Inhibition by Natural Polyphenols
Maluchenko, N. V., Feofanov, A. V., & Studitsky, V. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111441 · Cited by 42 · see citing works
Yalcin, A., Soddu, E., Turunc Bayrakdar, E., Uyanikgil, Y., Kanit, L., Armagan, G., Rassu, G., Gavini, E., & Giunchedi, P. (2016) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2016.05.017 · Cited by 37 · see citing works
Evaluation of safety and effectiveness of NAD in different clinical conditions: a systematic review
Gindri, I. M., Ferrari, G. A., Pinto, L. P. S., Bicca, J. M., dos Santos, Í. K., Dallacosta, D., & Roesler, C. R. D. M. (2023) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00242.2023 · Cited by 37 · see citing works
Pyridine Dinucleotides from Molecules to Man
Fessel, J. P., & Oldham, W. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7120 · Cited by 35 · see citing works
Poly(ADP-Ribosylation) in Age-Related Neurological Disease
McGurk, L., Rifai, O. M., & Bonini, N. M. (2019) · Trends in Genetics · doi:10.1016/j.tig.2019.05.004 · Cited by 36 · see citing works
Defective Autophagy and Mitophagy in Alzheimer’s Disease: Mechanisms and Translational Implications
Chen, J., He, H., Ye, Q., Feng, F., Wang, W., Gu, Y., Han, R., & Xie, C. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02487-7 · Cited by 36 · see citing works
Chen, G., Liu, C., Meng, G., Zhang, C., Chen, F., Tang, S., Hong, H., & Zhang, C. (2018) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.13056 · Cited by 34 · see citing works
Protective Effects of Phillyrin on H2O2-induced Oxidative Stress and Apoptosis in PC12 Cells
Wei, T., Tian, W., Yan, H., Shao, G., & Xie, G. (2014) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0091-4 · Cited by 34 · see citing works
Cho, C. H., Kim, E.-A. L., Kim, J., Choi, S. Y., Yang, S.-J., & Cho, S. (2016) · Free Radical Research · doi:10.3109/10715762.2016.1167277 · Cited by 34 · see citing works
Role of nicotinamide (vitamin B3) in acetaminophen-induced changes in rat liver
Mahmoud, Y. I., & Mahmoud, A. A. (2016) · Experimental and Toxicologic Pathology · doi:10.1016/j.etp.2016.05.003 · Cited by 33 · see citing works
Sidhu, A., Diwan, V., Kaur, H., Bhateja, D., Singh, C. K., Sharma, S., & Padi, S. S. V. (2018) · Metabolic Brain Disease · doi:10.1007/s11011-018-0297-0 · Cited by 32 · see citing works
Synaptosome as a tool in Alzheimer’s disease research
Ahmad, F., & Liu, P. (2020) · Brain Research · doi:10.1016/j.brainres.2020.147009 · Cited by 33 · see citing works
Som, S., Antony, J., Dhanabal, S. P., & Ponnusankar, S. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-021-00880-8 · Cited by 32 · see citing works
Boosting mitochondrial health to counteract neurodegeneration
Burtscher, J., Romani, M., Bernardo, G., Popa, T., Ziviani, E., Hummel, F. C., Sorrentino, V., & Millet, G. P. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102289 · Cited by 34 · see citing works
Turunç, E., Armağan, G., Uyanıkgil, Y., Kanıt, L., Koylu, E. O., & Yalçın, A. (2014) · Cell Biochemistry and Function · doi:10.1002/cbf.3049 · Cited by 31 · see citing works
Self-citationHan, G., Zhen, W., Dai, Y., Yu, H., Li, D., & Ma, T. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.873929 · Cited by 30 · see citing works
Acute sources of mitochondrial NAD+ during respiratory chain dysfunction
Chinopoulos, C. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113218 · Cited by 29 · see citing works
Wang, X., Wang, C., Geng, C.-H., & Zhao, K. (2018) · Europe PMC (PubMed Central) · Cited by 30 · see citing works
Rawat, D., Shrivastava, S., Naik, R. A., Chhonker, S. K., & Koiri, R. K. (2020) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22576 · Cited by 29 · see citing works
Cysewski, P., Przybyłek, M., Kowalska, A., & Tymorek, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147365 · Cited by 28 · see citing works
Mitochondrial mechanisms in Alzheimer’s disease: Quest for therapeutics
Kalani, K., Chaturvedi, P., Chaturvedi, P., Verma, V. K., Lal, N., Awasthi, S. K., & Kalani, A. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103547 · Cited by 28 · see citing works
Wu, Z., & Nakanishi, H. (2015) · Journal of Immunology Research · doi:10.1155/2015/471342 · Cited by 27 · see citing works
Advances in the Synthesis and Physiological Metabolic Regulation of Nicotinamide Mononucleotide
Zheng, C., Li, Y., Wu, X., Gao, L., & Chen, X. (2024) · Nutrients · doi:10.3390/nu16142354 · Cited by 26 · see citing works
Sirtuins, a key regulator of ageing and age-related neurodegenerative diseases
Bhatt, V., & Tiwari, A. K. (2022) · International Journal of Neuroscience · doi:10.1080/00207454.2022.2057849 · Cited by 27 · see citing works
Francisco‐Márquez, M., Aguilar-Fernández, M., & Galano, A. (2015) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2015.09.025 · Cited by 25 · see citing works
Converged avenues: depression and Alzheimer’s disease– shared pathophysiology and novel therapeutics
Bajaj, S., & Mahesh, R. (2024) · Molecular Biology Reports · doi:10.1007/s11033-023-09170-1 · Cited by 23 · see citing works
Hosseini, L., Mahmoudi, J., Pashazadeh, F., Salehi‐Pourmehr, H., & Sadigh‐Eteghad, S. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-021-01842-6 · Cited by 22 · see citing works
Recent advances in preventing neurodegenerative diseases
Chou, S.-C., Aggarwal, A., Dawson, V. L., Dawson, T. M., & Kam, T. (2021) · Faculty Reviews · doi:10.12703/r/10-81 · Cited by 24 · see citing works
Alam, S., Réhman, S. U., & Kim, M. O. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8020271 · Cited by 22 · see citing works
Simvastatin inhibits the apoptosis of hippocampal cells in a mouse model of Alzheimer's disease
Hu, X., Song, C., Fang, M., & Li, C. (2017) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2017.5620 · Cited by 20 · see citing works
Yang, S.-J., Han, A. R., Kim, E.-A., Yang, J. W., Ahn, J., Na, J.-M., & Cho, S. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172412 · Cited by 20 · see citing works
Genome-wide network-based pathway analysis of CSF t-tau/Aβ1-42 ratio in the ADNI cohort
Initiative, A. D. N., Wang, C., Meng, X., Li, J., Zhang, Q., Chen, F., Liu, W., Wang, Y., Cheng, S., Yao, X., et al. (2017) · BMC Genomics · doi:10.1186/s12864-017-3798-z · Cited by 20 · see citing works
Kim, E. J., & Yang, S. J. (2017) · Clinical Nutrition Research · doi:10.7762/cnr.2017.6.2.130 · Cited by 19 · see citing works
Nicotinamide as a Foundation for Treating Neurodegenerative Disease and Metabolic Disorders
Maiese, K. (2021) · Current Neurovascular Research · doi:10.2174/1567202617999210104220334 · Cited by 19 · see citing works
Poly(ADP-ribosylation) and neurodegenerative disorders
Basello, D. A., & Scovassi, A. I. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.07.005 · Cited by 19 · see citing works
Sriram, C. S., Jangra, A., Kasala, E. R., Bodduluru, L. N., & Bezbaruah, B. K. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.07.001 · Cited by 19 · see citing works
Kim, Y., Lee, H., Woo, J. J., Wang, Y., Kim, K., Choi, S., Jang, J., Kim, Y., Park, I. A., Han, D., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-03322-7 · Cited by 19 · see citing works
Dong, R., Denier‐Fields, D. N., Lu, Q., Suridjan, I., Kollmorgen, G., Wild, N., Betthauser, T. J., Carlsson, C. M., Asthana, S., Johnson, S. C., et al. (2022) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2022.04.009 · Cited by 18 · see citing works
Bioinorganic Chemistry of Micronutrients Related to Alzheimer’s and Parkinson’s Diseases
Kola, A., Nencioni, F., & Valensin, D. (2023) · Molecules · doi:10.3390/molecules28145467 · Cited by 18 · see citing works
Chaubey, K., Vázquez-Rosa, E., Tripathi, S., Shin, M.-K., Yu, Y. J., Dhar, M., Chakraborty, S., Yamakawa, M., Wang, X.-M., Sridharan, P. S., et al. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102535 · Cited by 24 · see citing works
Mitochondrial One-Carbon Metabolism and Alzheimer’s Disease
Yu, Y., & Martins, L. M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126302 · Cited by 17 · see citing works
Sobriety and Satiety: Is NAD+ the Answer?
Braidy, N., Villalva, M. D., & van Eeden, S. (2020) · Antioxidants · doi:10.3390/antiox9050425 · Cited by 17 · see citing works
Cai, W.-B., Zhao, Y., Liu, L., Cheng, Q., Wang, J., Shi, X., Liu, Y. Z., Qiao, X., Zhu, Y., Chen, C., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.06.033 · Cited by 16 · see citing works
- Authors
- Turunc Bayrakdar, E., Uyanikgil, Y., Kanit, L., Koylu, E., & Yalcin, A.
- Affiliations
- Ege University (TR)
- ORCID
- Koylu, E.
- Venue
- Free Radical Research
- Publisher
- Informa UK Limited
- Published
- 2013-11-11
- Volume
- 48
- Issue
- 2
- Pages
- 146-158
- ISSN
- 1029-2470 (ISSN-L)
- 1071-5762
- OpenAlex
- W1980204153
- Cited by
- 169
- References
- 95
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 16 · 2023: 13 · 2022: 13 · 2021: 17 · 2020: 17 · 2019: 17 · 2018: 13 · 2017: 15 · 2016: 8 · 2015: 17 · 2014: 11
- FWCI
- 8.33
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Neurology › Neurological Disease Mechanisms and Treatments
- Keywords
- nicotinamide, Alzheimer's disease, amyloid-beta 42, oxidative stress, apoptosis, PARP1, NF-κB, p53, Bax, Bcl-2, neuroinflammation, neurodegeneration, hippocampus, antioxidant enzymes, glutathione, mitochondrial function, reactive oxygen species, lipid peroxidation
- MeSH terms
- Poly(ADP-ribose) Polymerase Inhibitors, Poly (ADP-Ribose) Polymerase-1, Alzheimer Disease, Animals, Antioxidants, Catalase, Drug Evaluation, Preclinical, Glutathione, Glutathione Peroxidase, Hippocampus, Humans, Male, Malondialdehyde, Niacinamide, Peptide Fragments, Poly(ADP-ribose) Polymerases, Superoxide Dismutase, Synaptosomes, Lipid Peroxidation, Gene Expression, Amyloid beta-Peptides, NF-kappa B, Rats, Sprague-Dawley, Apoptosis, Reactive Oxygen Species, Oxidative Stress, Neuroprotective Agents, Apoptosis Regulatory Proteins, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review