Trientine Reduces BACE1 Activity and Mitigates Amyloidosis via the AGE/RAGE/NF-κB Pathway in a Transgenic Mouse Model of Alzheimer's Disease
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Aims: There is mounting evidence that the transition metal copper may play an important role in the pathophysiology of Alzheimer's disease (AD). Triethylene tetramine dihydrochloride (trientine), a CuII-selective chelator, is a commonly used treatment for Wilson's disease to decrease accumulated copper, and thereby decreases oxidative stress. In the present study, we evaluated the effects of a 3-month treatment course of trientine (Trien) on amyloidosis in 7-month-old β-amyloid (Aβ) precursor protein and presenilin-1 (APP/PS1) double transgenic (Tg) AD model mice. Results: We observed that Trien reduced the level of advanced glycation end products (AGEs), and decreased Aβ deposition and synapse loss in brain of APP/PS1 mice. Importantly, we found that Trien blocked the receptor for AGEs (RAGE), downregulated β-site APP cleaving enzyme 1 (BACE1), inhibited amyloidogenic APP cleavage, and subsequently reduced Aβ levels. In vitro , in SH-SY5Y cells overexpressing Swedish mutant APP, Trien-mediated downregulation of BACE1 occurred via inhibition of the NF-κB signaling pathway. Innovation: In this study, we demonstrated for the first time that Trien inhibited amyloidogenic pathway including targeting the downregulation of RAGE and NF-κB. Conclusion: Trien might mitigate amyloidosis in AD by inhibiting the RAGE/NF-κB/BACE1 pathway. Our study demonstrates that Trien may be a viable therapeutic strategy for the intervention and treatment of AD and other AD-like pathologies. Antioxid. Redox Signal . 19, 2024–2039.
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RAGEs are significantly or markedly expressed in many areas of the brain, such as the cortex, hippocampus, cerebellum, and substantia nigra, during the development of neurodegenerative diseases.
“Similar to AGEs, RAGEs are significantly or markedly expressed in many areas of the brain, such as the cortex, hippocampus, cerebellum, and substantia nigra105–107 during the development of neurodegenerative diseases.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [105]
Accumulation of AGEs and the AGE-RAGE interaction greatly induce reactive gliosis and the NF-κB proinflammatory pathway, leading to cellular stress, activated gliosis, and eventually neuronal degeneration.
“Additionally, the accumulation of AGEs and the AGE-RAGE interaction greatly induce reactive gliosis and the NF-κB proinflammatory pathway, leading to cellular stress, activated gliosis, and eventually neuronal degeneration105.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [105]
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The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063 · see citing works
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Hayden, M. S., & Ghosh, S. (2004) · Genes & Development · doi:10.1101/gad.1228704 · Cited by 3,842 · see citing works
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · 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
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120 · see citing works
RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012 · see citing works
Nitric oxide in the central nervous system: neuroprotection versus neurotoxicity
Calabrese, V., Mancuso, C., Calvani, M., Rizzarelli, E., Butterfield, D. A., & Giuffrida Stella, A. M. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2214 · Cited by 1,543 · cited 10× · see citing works
“The mRNA level of BACE1 was analyzed by real-time polymerase chain reaction (PCR), and Trien treatment did not alter the level of BACE1 mRNA [F(2,15) = 0.”
InfluentialProduction of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447 · see citing works
Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447 · see citing works
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426 · see citing works
Yan, S. D., Schmidt, A. M., Anderson, G. M., Zhang, J., Brett, J., Zou, Y., Pinsky, D. J., & Stern, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36966-1 · Cited by 1,305 · see citing works
The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
Schmidt, A. M., Yan, S. D., Yan, S. F., & Stern, D. M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci14002 · Cited by 1,256 · see citing works
The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
Schmidt, A. M., Yan, S. D., Yan, S. F., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200114002 · Cited by 1,039 · see citing works
Butterfield, D. A., & Lauderback, C. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00794-3 · Cited by 999 · see citing works
Increased Risk of Type 2 Diabetes in Alzheimer Disease
Janson, J., Laedtke, T., Parisi, J. E., O’Brien, P., Petersen, R. C., & Butler, P. C. (2004) · Diabetes · doi:10.2337/diabetes.53.2.474 · Cited by 950 · see citing works
Lander, H. M., Tauras, J. M., Ogiste, J. S., Hori, O., Moss, R. A., & Schmidt, A. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17810 · Cited by 813 · see citing works
Calabrese, V., Cornelius, C., Dinkova‐Kostova, A. T., Calabrese, E. J., & Mattson, M. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3074 · Cited by 803 · see citing works
The biology of the receptor for advanced glycation end products and its ligands
Schmidt, A. M., Yan, S. D., Yan, S. F., & Stern, D. M. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00087-2 · Cited by 687 · see citing works
Diabetes Mellitus and Risk of Alzheimer's Disease and Dementia with Stroke in a Multiethnic Cohort
Luchsinger, J. A. (2001) · American Journal of Epidemiology · doi:10.1093/aje/154.7.635 · Cited by 682 · 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
Schosinsky, K. H., Lehmann, H. P., & Beeler, M. F. (1974) · Clinical Chemistry · doi:10.1093/clinchem/20.12.1556 · Cited by 596 · see citing works
Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid
Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 580 · see citing works
Vassar, R., Kovacs, D. M., Yan, R., & Wong, P. C. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3657-09.2009 · Cited by 577 · see citing works
Dong, J., Atwood, C., Anderson, V. E., Siedlak, S. L., Smith, M. A., Perry, G. L., & CAREY, P. R. (2003) · Biochemistry · doi:10.1021/bi0272151 · Cited by 560 · see citing works
Frederickson, C. J., Kasarskis, E. J., Ringo, D., & Frederickson, R. E. (1987) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(87)90042-2 · Cited by 527 · see citing works
Lue, L.-F., Walker, D. G., Brachova, L., Beach, T. G., Rogers, J., Schmidt, A. M., Stern, D. M., & Yan, S. D. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7732 · Cited by 439 · see citing works
Cellular stress responses, hormetic phytochemicals and vitagenes in aging and longevity
Calabrese, V., Cornelius, C., Dinkova‐Kostova, A. T., Iavicoli, I., Paola, R. D., Koverech, A., Cuzzocrea, S., Rizzarelli, E., & Calabrese, E. J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.002 · Cited by 420 · see citing works
Deane, R., Wu, Z., & Zlokovic, B. V. (2004) · Stroke · doi:10.1161/01.str.0000143452.85382.d1 · Cited by 392 · see citing works
TREATMENT OF WILSON'S DISEASE WITH TRIENTINE (TRIETHYLENE TETRAMINE) DIHYDROCHLORIDE
Walshe, J. M. (1982) · The Lancet · doi:10.1016/s0140-6736(82)92201-2 · Cited by 381 · see citing works
Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β
Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371 · see citing works
Reddy, P. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03530.x · Cited by 356 · see citing works
Metals and amyloid‐β in Alzheimer's disease
Maynard, C. J., Bush, A. I., Masters, C. L., Cappai, R., & Li, Q. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00434.x · Cited by 353 · see citing works
Modulation of A beta adhesiveness and secretase site cleavage by zinc.
Bush, A. I., Pettingell, W. H., Paradis, M. D., & Tanzi, R. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32694-7 · Cited by 331 · see citing works
RAGE potentiates Aβ‐induced perturbation of neuronal function in transgenic mice
Arancio, O., Zhang, H. P., Chen, X., Lin, C., Trinchese, F., Puzzo, D., Liu, S., Hegde, A. N., Yan, S. F., Stern, A., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600415 · Cited by 328 · see citing works
Bucciarelli, L. G., Wendt, T., Rong, L., Lalla, E., Hofmann, M. A., Goova, M. T., Taguchi, A., Yan, S. F., Yan, S. D., Stern, D. M., et al. (2002) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-002-8491-x · Cited by 304 · see citing works
Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease
Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 288 · see citing works
Elevated cortical zinc in Alzheimer disease
Religa, D., Strozyk, D., Cherny, R. A., Volitakis, I., Haroutunian, V., Winblad, B. G., Näslund, J., & Bush, A. I. (2006) · Neurology · doi:10.1212/01.wnl.0000223644.08653.b5 · Cited by 272 · see citing works
Salkovic-Petrisic, M., & Hoyer, S. (2007) · Springer eBooks · doi:10.1007/978-3-211-73574-9_28 · Cited by 249 · see citing works
Hormesis, cellular stress response and vitagenes as critical determinants in aging and longevity
Calabrese, V., Cornelius, C., Cuzzocrea, S., Iavicoli, I., Rizzarelli, E., & Calabrese, E. J. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.007 · Cited by 225 · see citing works
Trojanowski, J. Q., & Lee, V. M. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.15.8529836 · Cited by 216 · see citing works
Terai, K., Matsuo, A., & McGeer, P. L. (1996) · Brain Research · doi:10.1016/0006-8993(96)00310-1 · Cited by 215 · see citing works
Cui, Z., Lockman, P. R., Atwood, C., Hsu, C. C., Gupte, A., ALLEN, D., & Mumper, R. J. (2004) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2004.07.009 · Cited by 203 · see citing works
Hippocampal RAGE immunoreactivity in early and advanced Alzheimer’s disease
Miller, M. C., Tavares, R., Johanson, C. E., Hovanesian, V., Donahue, J. E., Gonzalez, L., Silverberg, G. D., & Stopa, E. G. (2008) · Brain Research · doi:10.1016/j.brainres.2008.06.124 · Cited by 194 · see citing works
Danscher, G. (1984) · Histochemistry and Cell Biology · doi:10.1007/bf00514327 · Cited by 191 · see citing works
Bourne, K. Z., Ferrari, D. C., Lange‐Dohna, C., Roßner, S., Wood, T. G., & Perez-Polo, J. R. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21252 · Cited by 188 · see citing works
Inflammation and NF-κB in Alzheimer's Disease and Diabetes
Granic, I., Dolga, A. M., Nijholt, I. M., van Dijk, G., & Eisel, U. L. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0976 · Cited by 174 · see citing works
Münch, G. W., Mayer, S., Michaelis, J., Hipkiss, A. R., Riederer, P. F., Müller, R., Neumann, A., Schinzel, R., & Cunningham, A. M. (1997) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(96)00062-2 · Cited by 174 · see citing works
Chiurchiù, V., & Maccarrone, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3547 · Cited by 171 · see citing works
AGEs/RAGE complex upregulates BACE1 via NF-κB pathway activation
Guglielmotto, M., Aragno, M., Tamagno, E., Vercellinatto, I., Visentin, S., Medana, C., Catalano, M. G., Smith, M. A., Perry, G. L., Danni, O., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.05.026 · Cited by 162 · see citing works
Amyloid β protein precursor and the pathogenesis of Alzheimer's disease
Selkoe, D. J. (1989) · Cell · doi:10.1016/0092-8674(89)90093-7 · Cited by 154 · see citing works
Biochemical basis of regulation of human copper-transporting ATPases
Lutsenko, S., LeShane, E. S., & Shinde, U. P. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.04.013 · Cited by 151 · see citing works
Regeneration of the Heart in Diabetes by Selective Copper Chelation
Cooper, G. J. S., Phillips, A. R. J., Choong, S. Y., Leonard, B. L., Crossman, D. J., Brunton, D. H., Saafi, E. L., Dissanayake, A. M., Cowan, B. R., Young, A. A., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.9.2501 · Cited by 151 · see citing works
Cameron, N. E., & Cotter, M. A. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118104 · Cited by 147 · see citing works
Lee, J., Mook‐Jung, I., & Koh, J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-11-j0002.1999 · Cited by 136 · see citing works
Engineering metal ion coordination to regulate amyloid fibril assembly and toxicity
Dong, J., Canfield, J. M., Mehta, A. K., Shokes, J. E., Tian, B., Childers, W. S., Simmons, J. A., Mao, Z., Scott, R. A., Warncke, K., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702669104 · Cited by 133 · see citing works
Defective biliary excretion of copper in Wilson's disease
Frommer, D. (1974) · Gut · doi:10.1136/gut.15.2.125 · Cited by 127 · see citing works
NFκB-dependent Control of BACE1 Promoter Transactivation by Aβ42
Buggia-Prévot, V., Sévalle, J., Roßner, S., & Checler, F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706579200 · Cited by 125 · see citing works
Angeletti, B., Waldron, K. J., Freeman, K. B., Bawagan, H., Hussain, I., Miller, C. C. J., Lau, K., Tennant, M. E., Dennison, C., Robinson, N. J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412034200 · Cited by 125 · see citing works
RAGE regulates BACE1 and Aβ generation via NFAT1 activation in Alzheimer's disease animal model
Cho, H. J., Son, S. M., Jin, S. M., Hong, H. S., Shin, D. H., Kim, S. J., Huh, K. H., & Mook‐Jung, I. (2009) · The FASEB Journal · doi:10.1096/fj.08-126383 · Cited by 124 · see citing works
Copper, Zinc, and the Metallobiology of Alzheimer Disease
Bush, A. I. (2003) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-200307000-00005 · Cited by 117 · see citing works
Cooper, G. J. S. (2011) · Drugs · doi:10.2165/11591370-000000000-00000 · Cited by 113 · see citing works
Transition metal‐mediated glycoxidation accelerates cross‐linking of β‐amyloid peptide
Loske, C., Gerdemann, A., Schepl, W., Wycislo, M., Schinzel, R., Palm, D., Riederer, P. F., & Münch, G. W. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01452.x · Cited by 108 · see citing works
Wang, C., Zheng, W. H., Wang, T., Xie, J., Wang, S., Zhao, B., Teng, W., & Wang, Z. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2010.245 · Cited by 107 · see citing works
Self-citationMaynard, C. J., Cappai, R., Volitakis, I., Cherny, R. A., Masters, C. L., Li, Q., & Bush, A. I. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.02.010 · Cited by 96 · see citing works
Moriguchi, M., Nakajima, T., Kimura, H., Watanabe, T., Takashima, H., Mitsumoto, Y., Katagishi, T., Okanoue, T., & Kagawa, K. (2002) · International Journal of Cancer · doi:10.1002/ijc.10740 · Cited by 93 · see citing works
The Generation of Superoxide Anions in Glycation Reactions with Sugars, Osones, and 3-Deoxyosones
ORTWERTH, B. J., James, H. L., Simpson, G., & Linetsky, M. D. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8401 · Cited by 89 · see citing works
Cherny, R. A., Barnham, K. J., Lynch, T., Volitakis, I., Li, Q.-X., McLean, C., Multhaup, G., Beyreuther, K. T., Tanzi, R. E., Masters, C. L., et al. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4285 · Cited by 85 · see citing works
Cooper, G. J. S., Young, A. A., Gamble, G. D., Occleshaw, C., Dissanayake, A. M., Cowan, B. R., Brunton, D. H., Baker, J. R., Phillips, A. R. J., Frampton, C. M. A., et al. (2009) · Diabetologia · doi:10.1007/s00125-009-1265-3 · Cited by 83 · see citing works
Abnormalities of the Physiology of Copper in Wilson's Disease
OʼReilly, S. (1971) · Archives of Neurology · doi:10.1001/archneur.1971.00490010038005 · Cited by 48 · see citing works
Quinn, J. F., Harris, C., Cobb, K. E., Domes, C. M., Ralle, M., Brewer, G. J., & Wadsworth, T. L. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100408 · Cited by 44 · see citing works
Electrophoretic, biosensor, and bioactivity analyses of perlecans of different cellular origins
Knox, S. M., Melrose, J., & Whitelock, J. M. (2001) · PROTEOMICS · doi:10.1002/1615-9861(200111)1:12 · Cited by 44 · see citing works
Dysregulated NF-κB Pathway in Peripheral Mononuclear Cells of Alzheimers Disease Patients
Ascolani, A., Balestrieri, E., Minutolo, A., et al. (2012) · Current Alzheimer Research · doi:10.2174/156720512799015091 · Cited by 40 · see citing works
Cytotoxic effects of autoxidative glycation
Carubelli, R., Schneider, J. E., Pye, Q. N., & Floyd, R. A. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)e0134-5 · Cited by 35 · see citing works
Baynes, J., & Murray, D. B. (2009) · Experimental Diabetes Research · doi:10.1155/2009/696378 · Cited by 32 · see citing works
Characterization and antitumor activity of triethylene tetramine, a novel telomerase inhibitor
Liu, J., Guo, L., Yin, F., Zheng, X., Chen, G., & Yun, W. (2007) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2007.11.003 · Cited by 25 · see citing works
Transition metals and polyol pathway in the development of diabetic neuropathy in rats
Nakamura, J., Hamada, Y., Chaya, S., Nakashima, E., Naruse, K., Kato, K., Yasuda, Y., Kamiya, H., Sakakibara, F., Koh, N., et al. (2002) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.319 · Cited by 24 · see citing works
Flagged first, then by citations
Research works printed but not linked: 3
- [8]Buggia-Prevot V, Sevalle J, Rossner S, and Checler F. NFkappaB-dependent control of BACE1 promoter transactivation by Abeta42. J Biol Chem 283: 10037–10047, 2008 [DOI] [PubMed] [Google Scholar]
- [38]Hayden MS. and Ghosh S. Signaling to NF-kappaB. Genes Dev 18: 2195–2224, 2004 [DOI] [PubMed] [Google Scholar]
- [65]Schonberger SJ, Edgar PF, Kydd R, Faull RL, and Cooper GJ. Proteomic analysis of the brain in Alzheimer's disease: molecular phenotype of a complex disease process. Proteomics 1: 1519–1528, 2001 [DOI] [PubMed] [Google Scholar]
Cited by
Sorted by citations
Advanced glycation endproducts in food and their effects on health
Poulsen, M. W., Hedegaard, R. V., Andersen, J. M., de Courten, B., Bügel, S., Nielsen, J., Skibsted, L. H., & Dragsted, L. O. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.06.052 · Cited by 751 · see citing works
Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411 · see citing works
Self-citationByun, K., Yoo, Y., Son, M., Lee, J., Jeong, G.-B., Park, Y. M., Salekdeh, G. H., & Lee, B. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.030 · Cited by 357 · see citing works
- Authors
- Wang, C.-Y., Xie, J.-W., Xu, Y., Wang, T., Cai, J.-H., Wang, X., Zhao, B.-L., An, L., & Wang, Z.-Y.
- Affiliations
- China Medical University
- Jilin Medical University (CN)
- China Medical University (TW)
- Jilin Medical College
- Liaoning University of Traditional Chinese Medicine (CN)
- Institute of Biophysics
- Corresponding author
- Wang, Zhan-You
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2013-12
- Volume
- 19
- Issue
- 17
- Pages
- 2024-2039
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC3869419
- OpenAlex
- W1847017938
- Cited by
- 66
- References
- 80
- Citations by year
- 2026: 2 · 2025: 9 · 2024: 12 · 2023: 6 · 2022: 1 · 2021: 6 · 2020: 4 · 2019: 3 · 2018: 2 · 2017: 4 · 2016: 5 · 2015: 5 · 2014: 5 · 2013: 2
- FWCI
- 3.95
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81100810, 81200972, 81071004, 81100808)
- China Postdoctoral Science Foundation (2012M510849)
- Specialized Research Fund for the Doctoral Program of Higher Education of China (20112104120010)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Keywords
- triethylenetetramine, Alzheimer's disease, amyloidosis, BACE1, advanced glycation end products, RAGE, NF-κB signaling, copper chelation, APP/PS1 mice, amyloid-beta, synaptic loss, APP cleavage, oxidative stress
- MeSH terms
- Receptor for Advanced Glycation End Products, Superoxide Dismutase-1, Alzheimer Disease, Amyloidosis, Animals, Cerebral Cortex, Ceruloplasmin, Chelating Agents, Copper, Female, Humans, Malondialdehyde, Mice, Inbred C57BL, Mice, Transgenic, Receptors, Immunologic, Superoxide Dismutase, Trientine, Signal Transduction, Down-Regulation, Aspartic Acid Endopeptidases, NF-kappa B, Glycation End Products, Advanced, Cell Line, Tumor, Mice, Amyloid Precursor Protein Secretases
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 ›
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