메뉴 건너뛰기




Volumn 5 JUN, Issue , 2014, Pages

Osteoporosis and Alzheimer pathology: Role of cellular stress response and hormetic redox signaling in aging and bone remodeling

Author keywords

Alzheimer's disease; Cellular stress response; Hormesis; Oxidative stress; Redox status; Vitagenes

Indexed keywords

AMYLOID BETA PROTEIN; ANTICONVULSIVE AGENT; ANTIOXIDANT; ANXIOLYTIC AGENT; CURCUMIN; HEAT SHOCK PROTEIN 70; HEME OXYGENASE 1; HEME OXYGENASE 2; KELCH LIKE ECH ASSOCIATED PROTEIN 1; NOOTROPIC AGENT; OSTEOCLAST DIFFERENTIATION FACTOR; REACTIVE OXYGEN METABOLITE; SIRTUIN; THIOREDOXIN; TRANSCRIPTION FACTOR NRF2;

EID: 84904768694     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2014.00120     Document Type: Review
Times cited : (53)

References (136)
  • 1
    • 33746468121 scopus 로고    scopus 로고
    • Acetyl-L-carnitine-induced up-regulation of heat shock proteins protects cortical neurons against amyloid-beta peptide 1-42-mediated oxidative stress and neurotoxicity: implications for Alzheimer's disease
    • doi: 10.1002/jnr.20877
    • Abdul, H. M., Calabrese, V., Calvani, M., and Butterfield, D. A. (2006). Acetyl-L-carnitine-induced up-regulation of heat shock proteins protects cortical neurons against amyloid-beta peptide 1-42-mediated oxidative stress and neurotoxicity: implications for Alzheimer's disease. J. Neurosci. Res. 84, 398-408. doi: 10.1002/jnr.20877
    • (2006) J. Neurosci. Res , vol.84 , pp. 398-408
    • Abdul, H.M.1    Calabrese, V.2    Calvani, M.3    Butterfield, D.A.4
  • 2
    • 70549106846 scopus 로고    scopus 로고
    • Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses
    • doi: 10.1038/nn.2433
    • Abramov, E., Dolev, I., Fogel, H., Ciccotosto, G. D., Ruff, E., and Slutsky, I. (2009). Amyloid-beta as a positive endogenous regulator of release probability at hippocampal synapses. Nat. Neurosci. 12, 1567-1576. doi: 10.1038/nn.2433
    • (2009) Nat. Neurosci , vol.12 , pp. 1567-1576
    • Abramov, E.1    Dolev, I.2    Fogel, H.3    Ciccotosto, G.D.4    Ruff, E.5    Slutsky, I.6
  • 3
    • 78049368373 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 localizes to sex chromatin during meiotic repression
    • doi: 10.1074/jbc.M110.157552
    • Akerfelt, M., Vihervaara, A. A., Laiho, A., Conter, A., Christians, E. S., Sistonen, L., et al. (2012). Heat shock transcription factor 1 localizes to sex chromatin during meiotic repression. J. Biol. Chem. 285, 34469-34476. doi: 10.1074/jbc.M110.157552
    • (2012) J. Biol. Chem , vol.285 , pp. 34469-34476
    • Akerfelt, M.1    Vihervaara, A.A.2    Laiho, A.3    Conter, A.4    Christians, E.S.5    Sistonen, L.6
  • 4
    • 33846924300 scopus 로고    scopus 로고
    • How many transcription factors does it take to turn on the heme oxygenase-1 gene? Am
    • doi: 10.1165/rcmb.2006-0340TR
    • Alam, J., and Cook, J. L. (2007). How many transcription factors does it take to turn on the heme oxygenase-1 gene? Am. J. Respir. Cell Mol. Biol. 36, 166-174. doi: 10.1165/rcmb.2006-0340TR
    • (2007) J. Respir. Cell Mol. Biol , vol.36 , pp. 166-174
    • Alam, J.1    Cook, J.L.2
  • 5
    • 84890016169 scopus 로고    scopus 로고
    • Parathyroid hormone and parathyroid hormone-related protein analogs as therapies for osteoporosis
    • doi: 10.1007/s11914-013-0171-2
    • Augustine, M., and Horwitz, M. J. (2013). Parathyroid hormone and parathyroid hormone-related protein analogs as therapies for osteoporosis. Curr. Osteoporos. Rep. 11, 400-406. doi: 10.1007/s11914-013-0171-2
    • (2013) Curr. Osteoporos. Rep , vol.11 , pp. 400-406
    • Augustine, M.1    Horwitz, M.J.2
  • 6
    • 45749089694 scopus 로고    scopus 로고
    • Curcumin structure-function, bioavailability, and efficacy in models of neuroinflammation and Alzheimer's disease
    • doi: 10.1124/jpet.108.137455
    • Begum, A. N., Jones, M. R., Lim, G. P., Morihara, T., Kim, P., Heath, D. D., et al. (2008). Curcumin structure-function, bioavailability, and efficacy in models of neuroinflammation and Alzheimer's disease. J. Pharmacol. Exp. Ther. 326, 196-208. doi: 10.1124/jpet.108.137455
    • (2008) J. Pharmacol. Exp. Ther , vol.326 , pp. 196-208
    • Begum, A.N.1    Jones, M.R.2    Lim, G.P.3    Morihara, T.4    Kim, P.5    Heath, D.D.6
  • 7
    • 73449088037 scopus 로고    scopus 로고
    • Carnosinase levels in aging brain: redox state induction and cellular stress response
    • doi: 10.1089/ars.2009.2738
    • Bellia, F., Calabrese, V., Guarino, F., Cavallaro, M., Cornelius, C., De Pinto, V., et al. (2009). Carnosinase levels in aging brain: redox state induction and cellular stress response. Antioxid. Redox Signal. 11, 2759-2775. doi: 10.1089/ars.2009.2738
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 2759-2775
    • Bellia, F.1    Calabrese, V.2    Guarino, F.3    Cavallaro, M.4    Cornelius, C.5    De Pinto, V.6
  • 8
    • 81855196984 scopus 로고    scopus 로고
    • Neuroprotective features of carnosine in oxidative driven diseases
    • doi: 10.1016/j.mam.2011.10.009
    • Bellia, F., Vecchio, G., Cuzzocrea, S., Calabrese, V., and Rizzarelli, E. (2011). Neuroprotective features of carnosine in oxidative driven diseases. Mol. Aspects Med. 32, 258-266 doi: 10.1016/j.mam.2011.10.009
    • (2011) Mol. Aspects Med , vol.32 , pp. 258-266
    • Bellia, F.1    Vecchio, G.2    Cuzzocrea, S.3    Calabrese, V.4    Rizzarelli, E.5
  • 9
    • 84882445921 scopus 로고    scopus 로고
    • Is amyloid binding alcohol dehydrogenase a drug target for treating Alzheimer's disease?
    • Borger, E., Aitken, L., Du, H., Zhang, W., Gunn-Moore, F. J., and Yan, S. S. (2013). Is amyloid binding alcohol dehydrogenase a drug target for treating Alzheimer's disease? Curr. Alzheimer Res. 10, 21-29.
    • (2013) Curr. Alzheimer Res. , vol.10 , pp. 21-29
    • Borger, E.1    Aitken, L.2    Du, H.3    Zhang, W.4    Gunn-Moore, F.J.5    Yan, S.S.6
  • 10
    • 84897141031 scopus 로고    scopus 로고
    • Amyloid ß peptide (25-35) in picomolar concentrations modulates the function of glycine receptors in rat hippocampal pyramidal neurons through interaction with extracellular site(s)
    • doi: 10.1016/j.brainres.2014.02.031
    • Bukanova, J. V., Sharonova, I. N., and Skrebitsky, V. G. (2014). Amyloid ß peptide (25-35) in picomolar concentrations modulates the function of glycine receptors in rat hippocampal pyramidal neurons through interaction with extracellular site(s). Brain Res. 1558, 1-10. doi: 10.1016/j.brainres.2014.02.031
    • (2014) Brain Res , vol.1558 , pp. 1-10
    • Bukanova, J.V.1    Sharonova, I.N.2    Skrebitsky, V.G.3
  • 11
    • 29144459937 scopus 로고    scopus 로고
    • Historical blunders: how toxicology got the dose-response relationship half right
    • Calabrese, E. J. (2005). Historical blunders: how toxicology got the dose-response relationship half right. Cell. Mol. Biol. 51, 643-654.
    • (2005) Cell. Mol. Biol. , vol.51 , pp. 643-654
    • Calabrese, E.J.1
  • 12
    • 45849139711 scopus 로고    scopus 로고
    • Alzheimer's disease drugs: an application of the hormetic dose-response model
    • doi: 10.1080/10408440802003991
    • Calabrese, E. J. (2008a). Alzheimer's disease drugs: an application of the hormetic dose-response model. Crit. Rev. Toxicol. 38, 419-451. doi: 10.1080/10408440802003991
    • (2008) Crit. Rev. Toxicol , vol.38 , pp. 419-451
    • Calabrese, E.J.1
  • 13
    • 46949108881 scopus 로고    scopus 로고
    • An assessment of anxiolytic drug screening tests: hormetic dose responses predominate
    • doi: 10.1080/10408440802014238
    • Calabrese, E. J. (2008b). An assessment of anxiolytic drug screening tests: hormetic dose responses predominate. Crit. Rev. Toxicol. 38, 489-542. doi: 10.1080/10408440802014238
    • (2008) Crit. Rev. Toxicol , vol.38 , pp. 489-542
    • Calabrese, E.J.1
  • 14
    • 55149119710 scopus 로고    scopus 로고
    • Hormesis and medicine
    • doi: 10.1111/j.1365-2125.2008.03243.x
    • Calabrese, E. J. (2008c). Hormesis and medicine. Br. J. Clin. Pharmacol. 66, 594-617. doi: 10.1111/j.1365-2125.2008.03243.x
    • (2008) Br. J. Clin. Pharmacol , vol.66 , pp. 594-617
    • Calabrese, E.J.1
  • 15
    • 46949094048 scopus 로고    scopus 로고
    • Hormesis: why it is important to toxicology and toxicologists
    • doi: 10.1897/07-541.1
    • Calabrese, E. J. (2008d). Hormesis: why it is important to toxicology and toxicologists. Environ. Toxicol. Chem. 27, 1451-1474. doi: 10.1897/07-541.1
    • (2008) Environ. Toxicol. Chem , vol.27 , pp. 1451-1474
    • Calabrese, E.J.1
  • 16
    • 46949083071 scopus 로고    scopus 로고
    • Modulation of the epileptic seizure threshold: implications of biphasic dose responses
    • doi: 10.1080/10408440802014261
    • Calabrese, E. J. (2008e). Modulation of the epileptic seizure threshold: implications of biphasic dose responses. Crit. Rev. Toxicol. 38, 543-556. doi: 10.1080/10408440802014261
    • (2008) Crit. Rev. Toxicol , vol.38 , pp. 543-556
    • Calabrese, E.J.1
  • 17
    • 77949908145 scopus 로고    scopus 로고
    • Hormesis is central to toxicology, pharmacology and risk assessment
    • doi: 10.1177/0960327109363973
    • Calabrese, E. J. (2010). Hormesis is central to toxicology, pharmacology and risk assessment. Hum. Exp. Toxicol. 29, 249-261. doi: 10.1177/0960327109363973
    • (2010) Hum. Exp. Toxicol , vol.29 , pp. 249-261
    • Calabrese, E.J.1
  • 18
    • 81155144590 scopus 로고    scopus 로고
    • Toxicology rewrites its history and rethinks its future: giving equal focus to both harmful and beneficial effects
    • doi: 10.1002/etc.687
    • Calabrese, E. J. (2011). Toxicology rewrites its history and rethinks its future: giving equal focus to both harmful and beneficial effects. Environ. Toxicol. Chem. 30, 2658-2673. doi: 10.1002/etc.687
    • (2011) Environ. Toxicol. Chem , vol.30 , pp. 2658-2673
    • Calabrese, E.J.1
  • 19
    • 84891611966 scopus 로고    scopus 로고
    • Biphasic dose responses in biology, toxicology and medicine: accounting for their generalizability and quantitative features
    • doi: 10.1016/j.envpol.2013.07.046
    • Calabrese, E. J. (2013a). Biphasic dose responses in biology, toxicology and medicine: accounting for their generalizability and quantitative features. Environ. Pollut. 182, 452-460. doi: 10.1016/j.envpol.2013.07.046
    • (2013) Environ. Pollut , vol.182 , pp. 452-460
    • Calabrese, E.J.1
  • 20
    • 84874846693 scopus 로고    scopus 로고
    • Historical foundations of wound healing and its potential for acceleration: dose-response considerations
    • doi: 10.1111/j.1524-475X.2012.00842.x
    • Calabrese, E. J. (2013b). Historical foundations of wound healing and its potential for acceleration: dose-response considerations. Wound Repair Regen. 21, 180-193. doi: 10.1111/j.1524-475X.2012.00842.x
    • (2013) Wound Repair Regen , vol.21 , pp. 180-193
    • Calabrese, E.J.1
  • 21
    • 84872036965 scopus 로고    scopus 로고
    • Hormesis: toxicological foundations and role in aging research
    • doi: 10.1016/j.exger.2012.02.004
    • Calabrese, E. J. (2013c). Hormesis: toxicological foundations and role in aging research. Exp. Gerontol. 48, 99-102. doi: 10.1016/j.exger.2012.02.004
    • (2013) Exp. Gerontol , vol.48 , pp. 99-102
    • Calabrese, E.J.1
  • 22
    • 84880785593 scopus 로고    scopus 로고
    • Hormetic mechanisms
    • doi: 10.3109/10408444.2013.808172
    • Calabrese, E. J. (2013d). Hormetic mechanisms. Crit. Rev. Toxicol. 43, 580-606. doi: 10.3109/10408444.2013.808172
    • (2013) Crit. Rev. Toxicol , vol.43 , pp. 580-606
    • Calabrese, E.J.1
  • 23
    • 0033657377 scopus 로고    scopus 로고
    • Chemical hormesis: its historical foundations as a biological hypothesis
    • doi: 10.1191/096032700678815585
    • Calabrese, E. J., and Baldwin, L. A. (2000a). Chemical hormesis: its historical foundations as a biological hypothesis. Hum. Exp. Toxicol. 19, 2-31. doi: 10.1191/096032700678815585
    • (2000) Hum. Exp. Toxicol , vol.19 , pp. 2-31
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 24
    • 0034076363 scopus 로고    scopus 로고
    • Radiation hormesis: its historical foundations as a biological hypothesis
    • doi: 10.1191/096032700678815602
    • Calabrese, E. J., and Baldwin, L. A. (2000b). Radiation hormesis: its historical foundations as a biological hypothesis. Hum. Exp. Toxicol. 19, 41-75. doi: 10.1191/096032700678815602
    • (2000) Hum. Exp. Toxicol , vol.19 , pp. 41-75
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 25
    • 0034076364 scopus 로고    scopus 로고
    • Radiation hormesis: the demise of a legitimate hypothesis
    • doi: 10.1191/096032700678815611
    • Calabrese, E. J., and Baldwin, L. A. (2000c). Radiation hormesis: the demise of a legitimate hypothesis. Hum. Exp. Toxicol. 19, 76-84. doi: 10.1191/096032700678815611
    • (2000) Hum. Exp. Toxicol , vol.19 , pp. 76-84
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 26
    • 0034115903 scopus 로고    scopus 로고
    • Tale of two similar hypotheses: the rise and fall of chemical and radiation hormesis
    • doi: 10.1191/096032700678815620
    • Calabrese, E. J., and Baldwin, L. A. (2000d). Tale of two similar hypotheses: the rise and fall of chemical and radiation hormesis. Hum. Exp. Toxicol. 19, 85-97. doi: 10.1191/096032700678815620
    • (2000) Hum. Exp. Toxicol , vol.19 , pp. 85-97
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 27
    • 0033643737 scopus 로고    scopus 로고
    • The marginalization of hormesis
    • doi: 10.1191/096032700678815594
    • Calabrese, E. J., and Baldwin, L. A. (2000e). The marginalization of hormesis. Hum. Exp. Toxicol. 19, 32-40. doi: 10.1191/096032700678815594
    • (2000) Hum. Exp. Toxicol , vol.19 , pp. 32-40
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 28
    • 0034904233 scopus 로고    scopus 로고
    • The frequency of U-shaped dose responses in the toxicological literature
    • doi: 10.1093/toxsci/62.2.330
    • Calabrese, E. J., and Baldwin, L. A. (2001). The frequency of U-shaped dose responses in the toxicological literature. Toxicol. Sci. 62, 330-338. doi: 10.1093/toxsci/62.2.330
    • (2001) Toxicol. Sci , vol.62 , pp. 330-338
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 29
    • 0037291219 scopus 로고    scopus 로고
    • The hormetic dose-response model is more common than the threshold model in toxicology
    • doi: 10.1093/toxsci/71.2.246
    • Calabrese, E. J., and Baldwin, L. A. (2003). The hormetic dose-response model is more common than the threshold model in toxicology. Toxicol. Sci. 71, 246-250. doi: 10.1093/toxsci/71.2.246
    • (2003) Toxicol. Sci , vol.71 , pp. 246-250
    • Calabrese, E.J.1    Baldwin, L.A.2
  • 30
    • 12844251475 scopus 로고    scopus 로고
    • The occurrence of hormetic dose responses in the toxicological literature, the hormesis database: an overview
    • doi: 10.1016/j.taap.2004.06.023
    • Calabrese, E. J., and Blain, R. B. (2005). The occurrence of hormetic dose responses in the toxicological literature, the hormesis database: an overview. Toxicol. Appl. Pharmacol. 202, 289-301. doi: 10.1016/j.taap.2004.06.023
    • (2005) Toxicol. Appl. Pharmacol , vol.202 , pp. 289-301
    • Calabrese, E.J.1    Blain, R.B.2
  • 31
    • 56749158033 scopus 로고    scopus 로고
    • Hormesis and plant biology
    • doi: 10.1016/j.envpol.2008.07.028
    • Calabrese, E. J., and Blain, R. B. (2009). Hormesis and plant biology. Environ. Pollut. 157, 42-48. doi: 10.1016/j.envpol.2008.07.028
    • (2009) Environ. Pollut , vol.157 , pp. 42-48
    • Calabrese, E.J.1    Blain, R.B.2
  • 32
    • 80052403916 scopus 로고    scopus 로고
    • The hormesis database: the occurrence of hormetic dose responses in the toxicological literature
    • doi: 10.1016/j.yrtph.2011.06.003
    • Calabrese, E. J., and Blain, R. B. (2011). The hormesis database: the occurrence of hormetic dose responses in the toxicological literature. Regul. Toxicol. Pharmacol. 61, 73-81. doi: 10.1016/j.yrtph.2011.06.003
    • (2011) Regul. Toxicol. Pharmacol , vol.61 , pp. 73-81
    • Calabrese, E.J.1    Blain, R.B.2
  • 33
    • 84875826346 scopus 로고    scopus 로고
    • Low dose radiation therapy (LD-RT) is effective in the treatment of arthritis: animal model findings
    • doi: 10.3109/09553002.2013.752595
    • Calabrese, E. J., and Calabrese, V. (2013a). Low dose radiation therapy (LD-RT) is effective in the treatment of arthritis: animal model findings. Int. J. Radiat. Biol. 89, 287-294. doi: 10.3109/09553002.2013.752595
    • (2013) Int. J. Radiat. Biol , vol.89 , pp. 287-294
    • Calabrese, E.J.1    Calabrese, V.2
  • 34
    • 84875844205 scopus 로고    scopus 로고
    • Reduction of arthritic symptoms by low dose radiation therapy (LD-RT) is associated with an anti-inflammatory phenotype
    • doi: 10.3109/09553002.2013.752594
    • Calabrese, E. J., and Calabrese, V. (2013b). Reduction of arthritic symptoms by low dose radiation therapy (LD-RT) is associated with an anti-inflammatory phenotype. Int. J. Radiat. Biol. 89, 278-286. doi: 10.3109/09553002.2013.752594
    • (2013) Int. J. Radiat. Biol , vol.89 , pp. 278-286
    • Calabrese, E.J.1    Calabrese, V.2
  • 35
    • 84891126083 scopus 로고    scopus 로고
    • How radiotherapy was historically used to treat pneumonia: could it be useful today?
    • Calabrese, E. J., and Dhawan, G. (2013). How radiotherapy was historically used to treat pneumonia: could it be useful today? Yale J. Biol. Med. 86, 555-570.
    • (2013) Yale J. Biol. Med. , vol.86 , pp. 555-570
    • Calabrese, E.J.1    Dhawan, G.2
  • 36
    • 77953848821 scopus 로고    scopus 로고
    • Hormesis in high-throughput screening of antibacterial compounds in E
    • doi: 10.1177/0960327109358917
    • Calabrese, E. J., Hoffmann, G. R., Stanek E. J. III, and Nascarella, M. A. (2010a). Hormesis in high-throughput screening of antibacterial compounds in E. coli. Hum. Exp. Toxicol. 29, 667-677. doi: 10.1177/0960327109358917
    • (2010) coli. Hum. Exp. Toxicol , vol.29 , pp. 667-677
    • Calabrese, E.J.1    Hoffmann, G.R.2    Stanek III, E.J.3    Nascarella, M.A.4
  • 37
    • 78649936101 scopus 로고    scopus 로고
    • Dose response biology: the case of resveratrol
    • doi: 10.1177/0960327110383641
    • Calabrese, E. J., Mattson, M. P., and Calabrese, V. (2010b). Dose response biology: the case of resveratrol. Hum. Exp. Toxicol. 29, 1034-1037. doi: 10.1177/0960327110383641
    • (2010) Hum. Exp. Toxicol , vol.29 , pp. 1034-1037
    • Calabrese, E.J.1    Mattson, M.P.2    Calabrese, V.3
  • 38
    • 78649979775 scopus 로고    scopus 로고
    • Resveratrol commonly displays hormesis: occurrence and biomedical significance
    • doi: 10.1177/0960327110383625
    • Calabrese, E. J., Mattson, M. P., and Calabrese, V. (2010c). Resveratrol commonly displays hormesis: occurrence and biomedical significance. Hum. Exp. Toxicol. 29, 980-1015. doi: 10.1177/0960327110383625
    • (2010) Hum. Exp. Toxicol , vol.29 , pp. 980-1015
    • Calabrese, E.J.1    Mattson, M.P.2    Calabrese, V.3
  • 39
    • 77958126450 scopus 로고    scopus 로고
    • Cellular stress responses, the hormesis paradigm and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders
    • doi: 10.1089/ars.2009.3074
    • Calabrese, V., Cornelius, C., Dinkova-Kostova, A. T., Calabrese, E. J., and Mattson, M. P. (2010d). Cellular stress responses, the hormesis paradigm and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders. Antioxid. Redox Signal. 13, 1763-1811. doi: 10.1089/ars.2009.3074
    • (2010) Antioxid. Redox Signal , vol.13 , pp. 1763-1811
    • Calabrese, V.1    Cornelius, C.2    Dinkova-Kostova, A.T.3    Calabrese, E.J.4    Mattson, M.P.5
  • 40
    • 78651324323 scopus 로고    scopus 로고
    • Cellular stress responses, mitostress and carnitine insufficiencies as critical determinants in aging and neurodegenerative disorders: role of hormesis and vitagenes
    • doi: 10.1007/s11064-010-0307-z
    • Calabrese, V., Cornelius, C., Giuffrida, A. M., and Calabrese, E. J. (2010e). Cellular stress responses, mitostress and carnitine insufficiencies as critical determinants in aging and neurodegenerative disorders: role of hormesis and vitagenes. Neurochem. Res. 35, 1880-1915. doi: 10.1007/s11064-010-0307-z
    • (2010) Neurochem. Res , vol.35 , pp. 1880-1915
    • Calabrese, V.1    Cornelius, C.2    Giuffrida, A.M.3    Calabrese, E.J.4
  • 41
    • 78651268075 scopus 로고    scopus 로고
    • Oxidative stress, redox homeostasis and cellular stress response in Ménière's disease: role of vitagenes
    • doi: 10.1007/s11064-010-0304-2
    • Calabrese, V., Cornelius, C., Maiolino, L., Luca, M., Chiaramonte, R., Toscano, M. A., et al. (2010f). Oxidative stress, redox homeostasis and cellular stress response in Ménière's disease: role of vitagenes. Neurochem. Res. 35, 2208-2217. doi: 10.1007/s11064-010-0304-2
    • (2010) Neurochem. Res , vol.35 , pp. 2208-2217
    • Calabrese, V.1    Cornelius, C.2    Maiolino, L.3    Luca, M.4    Chiaramonte, R.5    Toscano, M.A.6
  • 42
    • 77449098537 scopus 로고    scopus 로고
    • Redox homeostasis and cellular stress response in aging and neurodegeneration
    • doi: 10.1007/978-1-60327-029-8_17
    • Calabrese, V., Cornelius, C., Mancuso, C., Lentile, R., Stella, A. M., and Butterfield, D. A. (2010g). Redox homeostasis and cellular stress response in aging and neurodegeneration. Methods Mol. Biol. 610, 285-308. doi: 10.1007/978-1-60327-029-8_17
    • (2010) Methods Mol. Biol , vol.610 , pp. 285-308
    • Calabrese, V.1    Cornelius, C.2    Mancuso, C.3    Lentile, R.4    Stella, A.M.5    Butterfield, D.A.6
  • 43
    • 77950268110 scopus 로고    scopus 로고
    • The hormetic role of dietary antioxidants in free radical-related diseases
    • doi: 10.2174/138161210790883615
    • Calabrese, V., Cornelius, C., Trovato, A., Cambria, M. T., Lo Cascio, M. S., Di Rienzo, L., et al. (2010h). The hormetic role of dietary antioxidants in free radical-related diseases. Curr. Pharm. Des. 16, 8778-8783. doi: 10.2174/138161210790883615
    • (2010) Curr. Pharm. Des , vol.16 , pp. 8778-8783
    • Calabrese, V.1    Cornelius, C.2    Trovato, A.3    Cambria, M.T.4    Lo Cascio, M.S.5    Di Rienzo, L.6
  • 44
    • 84865088842 scopus 로고    scopus 로고
    • Hormesis: why it is important to biogerontologists
    • doi: 10.1007/s10522-012-9374-7
    • Calabrese, E. J., Iavicoli, I., and Calabrese, V. (2012). Hormesis: why it is important to biogerontologists. Biogerontology 13, 215-235. doi: 10.1007/s10522-012-9374-7
    • (2012) Biogerontology , vol.13 , pp. 215-235
    • Calabrese, E.J.1    Iavicoli, I.2    Calabrese, V.3
  • 45
    • 84858153162 scopus 로고    scopus 로고
    • Cellular stress responses, hormetic phytochemicals and vitagenes in aging and longevity
    • doi: 10.1016/j.bbadis.2011.11.002
    • Calabrese, V., Cornelius, C., Dinkova-Kostova, A. T., Iavicoli, I., Di Paola, R., Koverech, A., et al. (2012b). Cellular stress responses, hormetic phytochemicals and vitagenes in aging and longevity. Biochim. Biophys. Acta 1822, 753-783. doi: 10.1016/j.bbadis.2011.11.002
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 753-783
    • Calabrese, V.1    Cornelius, C.2    Dinkova-Kostova, A.T.3    Iavicoli, I.4    Di Paola, R.5    Koverech, A.6
  • 46
    • 84872295104 scopus 로고    scopus 로고
    • Hormesis: its impact on medicine and health
    • doi: 10.1177/0960327112455069
    • Calabrese, E. J., Iavicoli, I., and Calabrese, V. (2013). Hormesis: its impact on medicine and health. Hum. Exp. Toxicol. 32, 120-152. doi: 10.1177/0960327112455069
    • (2013) Hum. Exp. Toxicol , vol.32 , pp. 120-152
    • Calabrese, E.J.1    Iavicoli, I.2    Calabrese, V.3
  • 47
    • 79953029961 scopus 로고    scopus 로고
    • Hormesis provides a generalized quantitative estimate of biological plasticity
    • doi: 10.1007/s12079-011-0119-1
    • Calabrese, E. J., and Mattson, M. P. (2011). Hormesis provides a generalized quantitative estimate of biological plasticity. J. Cell Commun. Signal. 5, 25-38. doi: 10.1007/s12079-011-0119-1
    • (2011) J. Cell Commun. Signal , vol.5 , pp. 25-38
    • Calabrese, E.J.1    Mattson, M.P.2
  • 48
    • 57049167149 scopus 로고    scopus 로고
    • Hormesis predicts low-dose responses better than threshold model
    • doi: 10.1080/10915810802503735
    • Calabrese, E. J., Stanek, E. J. III, Nascarella, M. A., and Hoffmann, G. R. (2008a). Hormesis predicts low-dose responses better than threshold model. Int. J. Toxicol. 27, 369-378. doi: 10.1080/10915810802503735
    • (2008) Int. J. Toxicol , vol.27 , pp. 369-378
    • Calabrese, E.J.1    Stanek III, E.J.2    Nascarella, M.A.3    Hoffmann, G.R.4
  • 49
    • 54949107786 scopus 로고    scopus 로고
    • Curcumin and the cellular stress response in free radical-related diseases
    • doi: 10.1002/mnfr.200700316
    • Calabrese, V., Bates, T. E., Mancuso, C., Cornelius, C., Ventimiglia, B., Cambria, M. T., et al. (2008b). Curcumin and the cellular stress response in free radical-related diseases. Mol. Nutr. Food Res. 52, 1062-1073. doi: 10.1002/mnfr.200700316
    • (2008) Mol. Nutr. Food Res , vol.52 , pp. 1062-1073
    • Calabrese, V.1    Bates, T.E.2    Mancuso, C.3    Cornelius, C.4    Ventimiglia, B.5    Cambria, M.T.6
  • 52
    • 48449087215 scopus 로고    scopus 로고
    • Redox regulation of cellular stress response by ferulic acid ethyl ester in human dermal fibroblasts: role of vitagenes
    • doi: 10.1016/j.clindermatol.2008.01.005
    • Calabrese, V., Calafato, S., Puleo, E., Cornelius, C., Sapienza, M., Morganti, P., et al. (2008e). Redox regulation of cellular stress response by ferulic acid ethyl ester in human dermal fibroblasts: role of vitagenes. Clin. Dermatol. 26, 358-363. doi: 10.1016/j.clindermatol.2008.01.005
    • (2008) Clin. Dermatol , vol.26 , pp. 358-363
    • Calabrese, V.1    Calafato, S.2    Puleo, E.3    Cornelius, C.4    Sapienza, M.5    Morganti, P.6
  • 53
    • 84877626765 scopus 로고    scopus 로고
    • Redox homeostasis and cellular stress response in aging and neurodegeneration
    • 2nd Edn, eds R. M. Uppu, S. N. Murthy, W. A. Pryor, and N. L. Parinandi (New York: Humana Press)
    • Calabrese, V., Cornelius, C., Mancuso, C., Ientile, R., Giuffrida Stella, A. M., and Butterfield, D. A. (2008f). "Redox homeostasis and cellular stress response in aging and neurodegeneration," in Free Radical and Antioxidant Protocols, 2nd Edn, eds R. M. Uppu, S. N. Murthy, W. A. Pryor, and N. L. Parinandi (New York: Humana Press), 285-308.
    • (2008) Free Radical and Antioxidant Protocols , pp. 285-308
    • Calabrese, V.1    Cornelius, C.2    Mancuso, C.3    Ientile, R.4    Giuffrida Stella, A.M.5    Butterfield, D.A.6
  • 54
    • 56449129616 scopus 로고    scopus 로고
    • Cellular stress response: a novel target for chemoprevention and nutritional neuroprotection in aging, neurodegenerative disorders and longevity
    • doi: 10.1007/s11064-008-9775-9
    • Calabrese, V., Cornelius, C., Mancuso, C., Pennisi, G., Calafato, S., Bellia, F., et al. (2008g). Cellular stress response: a novel target for chemoprevention and nutritional neuroprotection in aging, neurodegenerative disorders and longevity. Neurochem. Res. 33, 2444-2471. doi: 10.1007/s11064-008-9775-9
    • (2008) Neurochem. Res , vol.33 , pp. 2444-2471
    • Calabrese, V.1    Cornelius, C.2    Mancuso, C.3    Pennisi, G.4    Calafato, S.5    Bellia, F.6
  • 55
    • 84877608724 scopus 로고    scopus 로고
    • Nutritional redox homeostasis and cellular stress response: differential role of homocysteine and acetylcarnitine
    • eds Y. J. Surh, Z. Dong, E. Cadenas, and L. Packer (New York, NY: CRC Press)
    • Calabrese, V., Ientile, R., Cornelius, C., Scalia, M., Cambria, M. T., Ventimiglia, B., et al. (2008h). "Nutritional redox homeostasis and cellular stress response: differential role of homocysteine and acetylcarnitine," in Dietary Modulation of Cell Signaling Pathways, eds Y. J. Surh, Z. Dong, E. Cadenas, and L. Packer (New York, NY: CRC Press), 229-250.
    • (2008) Dietary Modulation of Cell Signaling Pathways , pp. 229-250
    • Calabrese, V.1    Ientile, R.2    Cornelius, C.3    Scalia, M.4    Cambria, M.T.5    Ventimiglia, B.6
  • 56
    • 77957164066 scopus 로고    scopus 로고
    • Reactive nitrogen species and cellular stress tolerance in aging and neurodegeneration: role of vitagenes
    • eds S. Alvarez and P. Evelson (Trivandrum: Transworld Research Network)
    • Calabrese, V., Mancuso, C., Cornelius, C., Calafato, M., Ventimiglia, B., Butterfield, D. A., et al. (2008i). "Reactive nitrogen species and cellular stress tolerance in aging and neurodegeneration: role of vitagenes," in Free Radical Pathophysiology, eds S. Alvarez and P. Evelson (Trivandrum: Transworld Research Network), 345-367.
    • (2008) Free Radical Pathophysiology , pp. 345-367
    • Calabrese, V.1    Mancuso, C.2    Cornelius, C.3    Calafato, M.4    Ventimiglia, B.5    Butterfield, D.A.6
  • 57
    • 52249099052 scopus 로고    scopus 로고
    • Practical approaches to investigate redox regulation of heat shock protein expression and intracellular glutathione redox state
    • doi: 10.1016/S0076-6879(08)01206-8
    • Calabrese, V., Signorile, A., Cornelius, C., Mancuso, C., Scapagnini, G., Ventimiglia, B., et al. (2008j). Practical approaches to investigate redox regulation of heat shock protein expression and intracellular glutathione redox state. Methods Enzymol. 441, 83-110. doi: 10.1016/S0076-6879(08)01206-8
    • (2008) Methods Enzymol , vol.441 , pp. 83-110
    • Calabrese, V.1    Signorile, A.2    Cornelius, C.3    Mancuso, C.4    Scapagnini, G.5    Ventimiglia, B.6
  • 58
    • 33751399246 scopus 로고    scopus 로고
    • Hormesis outperforms threshold model in National Cancer Institute antitumor drug screening database
    • doi: 10.1093/toxsci/kfl098
    • Calabrese, E. J., Staudenmayer, J. W., Stanek, E. J. III, and Hoffmann, G. R. (2006a). Hormesis outperforms threshold model in National Cancer Institute antitumor drug screening database. Toxicol. Sci. 94, 368-378. doi: 10.1093/toxsci/kfl098
    • (2006) Toxicol. Sci , vol.94 , pp. 368-378
    • Calabrese, E.J.1    Staudenmayer, J.W.2    Stanek III, E.J.3    Hoffmann, G.R.4
  • 59
    • 33646681219 scopus 로고    scopus 로고
    • Redox regulation of heat shock protein expression by signaling involving nitric oxide and carbon monoxide: relevance to brain aging, neurodegenerative disorders, and longevity
    • doi: 10.1089/ars.2006.8.444
    • Calabrese, V., Butterfield, D. A., Scapagnini, G., Stella, A. M., and Maines, M. D. (2006b). Redox regulation of heat shock protein expression by signaling involving nitric oxide and carbon monoxide: relevance to brain aging, neurodegenerative disorders, and longevity. Antioxid. Redox Signal. 8, 444-477. doi: 10.1089/ars.2006.8.444
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 444-477
    • Calabrese, V.1    Butterfield, D.A.2    Scapagnini, G.3    Stella, A.M.4    Maines, M.D.5
  • 60
    • 33646675336 scopus 로고    scopus 로고
    • Redox modulation of heat shock protein expression by acetylcarnitine in aging brain: relationship to antioxidant status and mitochondrial function
    • doi: 10.1089/ars.2006.8.404
    • Calabrese, V., Colombrita, C., Sultana, R., Scapagnini, G., Calvani, M., Butterfield, D. A., et al. (2006c). Redox modulation of heat shock protein expression by acetylcarnitine in aging brain: relationship to antioxidant status and mitochondrial function. Antioxid. Redox Signal. 8, 404-416. doi: 10.1089/ars.2006.8.404
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 404-416
    • Calabrese, V.1    Colombrita, C.2    Sultana, R.3    Scapagnini, G.4    Calvani, M.5    Butterfield, D.A.6
  • 61
    • 33947606911 scopus 로고    scopus 로고
    • Nitrosative stress, cellular stress response, and thiol homeostasis in patients with Alzheimer's disease
    • doi: 10.1089/ars.2006.8.1975
    • Calabrese, V., Sultana, R., Scapagnini, G., Guagliano, E., Sapienza, M., Bella, R., et al. (2006d). Nitrosative stress, cellular stress response, and thiol homeostasis in patients with Alzheimer's disease. Antioxid. Redox Signal. 8, 1975-1986. doi: 10.1089/ars.2006.8.1975
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 1975-1986
    • Calabrese, V.1    Sultana, R.2    Scapagnini, G.3    Guagliano, E.4    Sapienza, M.5    Bella, R.6
  • 62
    • 81855201861 scopus 로고    scopus 로고
    • Hormesis, cellular stress response and vitagenes as critical determinants in aging and longevity
    • doi: 10.1016/j.mam.2011.10.007
    • Calabrese, V., Cornelius, C., Cuzzocrea, S., Iavicoli, I., Rizzarelli, E., and Calabrese, E. J. (2011). Hormesis, cellular stress response and vitagenes as critical determinants in aging and longevity. Mol. Aspects Med. 32, 279-304. doi: 10.1016/j.mam.2011.10.007
    • (2011) Mol. Aspects Med , vol.32 , pp. 279-304
    • Calabrese, V.1    Cornelius, C.2    Cuzzocrea, S.3    Iavicoli, I.4    Rizzarelli, E.5    Calabrese, E.J.6
  • 63
    • 67649213915 scopus 로고    scopus 로고
    • Vitagenes, cellular stress response and acetylcarnitine: relevance to hormesis
    • doi: 10.1002/biof.22
    • Calabrese, V., Cornelius, C., Dinkova-Kostova, A. T., and Calabrese, E. J. (2009a). Vitagenes, cellular stress response and acetylcarnitine: relevance to hormesis. Biofactors 35, 146-160. doi: 10.1002/biof.22
    • (2009) Biofactors , vol.35 , pp. 146-160
    • Calabrese, V.1    Cornelius, C.2    Dinkova-Kostova, A.T.3    Calabrese, E.J.4
  • 64
    • 63849154150 scopus 로고    scopus 로고
    • Vitagenes, dietary antioxidants and neuroprotection in neurodegenerative diseases
    • doi: 10.2741/3250
    • Calabrese, V., Cornelius, C., Mancuso, C., Barone, E., Calafato, S., Bates, T., et al. (2009b). Vitagenes, dietary antioxidants and neuroprotection in neurodegenerative diseases. Front. Biosci. 14:376-397. doi: 10.2741/3250
    • (2009) Front. Biosci , vol.14 , pp. 376-397
    • Calabrese, V.1    Cornelius, C.2    Mancuso, C.3    Barone, E.4    Calafato, S.5    Bates, T.6
  • 67
    • 33947601659 scopus 로고    scopus 로고
    • Redox regulation of cellular stress response in aging and neurodegenerative disorders: role of vitagenes
    • doi: 10.1007/s11064-006-9203-y
    • Calabrese, V., Guagliano, E., Sapienza, M., Panebianco, M., Calafato, S., Puleo, E., et al. (2007a). Redox regulation of cellular stress response in aging and neurodegenerative disorders: role of vitagenes. Neurochem. Res. 32, 757-773. doi: 10.1007/s11064-006-9203-y
    • (2007) Neurochem. Res , vol.32 , pp. 757-773
    • Calabrese, V.1    Guagliano, E.2    Sapienza, M.3    Panebianco, M.4    Calafato, S.5    Puleo, E.6
  • 69
    • 34247326430 scopus 로고    scopus 로고
    • In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state
    • doi: 10.1111/j.1471-4159.2006.04367.x
    • Calabrese, V., Mancuso, C., Ravagna, A., Perluigi, M., Cini, C., De Marco, C., et al. (2007c). In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state. J. Neurochem. 101, 709-717. doi: 10.1111/j.1471-4159.2006.04367.x
    • (2007) J. Neurochem , vol.101 , pp. 709-717
    • Calabrese, V.1    Mancuso, C.2    Ravagna, A.3    Perluigi, M.4    Cini, C.5    De Marco, C.6
  • 70
    • 33646698439 scopus 로고    scopus 로고
    • Antiaging medicine: antioxidants and aging
    • doi: 10.1089/ars.2006.8.362
    • Calabrese, V., and Maines, M. D. (2006). Antiaging medicine: antioxidants and aging. Antioxid. Redox Signal. 8, 362-364. doi: 10.1089/ars.2006.8.362
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 362-364
    • Calabrese, V.1    Maines, M.D.2
  • 71
    • 84893747678 scopus 로고    scopus 로고
    • Systemic oxidative stress and conversion to dementia of elderly patients with mild cognitive impairment
    • doi: 10.1155/2014/309507
    • Cervellati, C., Romani, A., Seripa, D., Cremonini, E., Bosi, C., Magon, S., et al. (2014). Systemic oxidative stress and conversion to dementia of elderly patients with mild cognitive impairment. Biomed. Res. Int. 2014, 309507. doi: 10.1155/2014/309507
    • (2014) Biomed. Res. Int , vol.2014 , pp. 309507
    • Cervellati, C.1    Romani, A.2    Seripa, D.3    Cremonini, E.4    Bosi, C.5    Magon, S.6
  • 72
    • 84880275605 scopus 로고    scopus 로고
    • Oxidative stress and APO E polymorphisms in Alzheimer's disease and in mild cognitive impairment
    • doi: 10.3109/10715762.2013.804622
    • Chico, L., Simoncini, C., Lo Gerfo, A., Rocchi, A., Petrozzi, L., Carlesi, C., et al. (2013). Oxidative stress and APO E polymorphisms in Alzheimer's disease and in mild cognitive impairment. Free Radic. Res. 47, 569-576. doi: 10.3109/10715762.2013.804622
    • (2013) Free Radic. Res , vol.47 , pp. 569-576
    • Chico, L.1    Simoncini, C.2    Lo Gerfo, A.3    Rocchi, A.4    Petrozzi, L.5    Carlesi, C.6
  • 73
    • 84876958820 scopus 로고    scopus 로고
    • Stress responses, vitagenes and hormesis as critical determinants in aging and longevity: mitochondria as a "chi"
    • doi: 10.1186/1742-4933-10-15
    • Cornelius, C., Perrotta, R., Graziano, A., Calabrese, E. J., and Calabrese, V. (2013a). Stress responses, vitagenes and hormesis as critical determinants in aging and longevity: mitochondria as a "chi". Immun. Ageing 10:15. doi: 10.1186/1742-4933-10-15
    • (2013) Immun. Ageing , vol.10 , pp. 15
    • Cornelius, C.1    Perrotta, R.2    Graziano, A.3    Calabrese, E.J.4    Calabrese, V.5
  • 74
    • 84885524005 scopus 로고    scopus 로고
    • Cellular stress response, sirtuins and UCP proteins in Alzheimer disease: role of vitagenes
    • doi: 10.1186/1742-4933-10-41
    • Cornelius, C., Trovato Salinaro, A., Scuto, M., Fronte, V., Cambria, M. T., Pennisi, M., et al. (2013b). Cellular stress response, sirtuins and UCP proteins in Alzheimer disease: role of vitagenes. Immun. Ageing 10:41. doi: 10.1186/1742-4933-10-41
    • (2013) Immun. Ageing , vol.10 , Issue.41
    • Cornelius, C.1    Trovato Salinaro, A.2    Scuto, M.3    Fronte, V.4    Cambria, M.T.5    Pennisi, M.6
  • 75
    • 79955641534 scopus 로고    scopus 로고
    • APPswe/Aß regulation of osteoclast activation and RAGE expression in an age-dependent manner
    • doi: 10.1002/jbmr.299
    • Cui, S., Xiong, F., Hong, Y., Jung, J. U., Li, X. S., Liu, J. Z., et al. (2011). APPswe/Aß regulation of osteoclast activation and RAGE expression in an age-dependent manner. J. Bone Miner. Res. 26, 1084-1098. doi: 10.1002/jbmr.299
    • (2011) J. Bone Miner. Res , vol.26 , pp. 1084-1098
    • Cui, S.1    Xiong, F.2    Hong, Y.3    Jung, J.U.4    Li, X.S.5    Liu, J.Z.6
  • 76
    • 84901188020 scopus 로고    scopus 로고
    • Insights into the physiological function of the ß-amyloid precursor protein: beyond Alzheimer's disease
    • doi: 10.1111/jnc.12675 [Epub ahead of print].
    • Dawkins, E., and Small, D. H. (2014). Insights into the physiological function of the ß-amyloid precursor protein: beyond Alzheimer's disease. J. Neurochem. doi: 10.1111/jnc.12675 [Epub ahead of print].
    • (2014) J. Neurochem
    • Dawkins, E.1    Small, D.H.2
  • 77
    • 78651283063 scopus 로고    scopus 로고
    • Oxidative damage in rat brain during aging: interplay between energy and metabolic key target proteins
    • doi: 10.1007/s11064-010-0295-z
    • Di Domenico, F., Perluigi, M., Butterfield, D. A., Cornelius, C., and Calabrese, V. (2010). Oxidative damage in rat brain during aging: interplay between energy and metabolic key target proteins. Neurochem. Res. 35, 2184-2192. doi: 10.1007/s11064-010-0295-z
    • (2010) Neurochem. Res , vol.35 , pp. 2184-2192
    • Di Domenico, F.1    Perluigi, M.2    Butterfield, D.A.3    Cornelius, C.4    Calabrese, V.5
  • 78
    • 80054715568 scopus 로고    scopus 로고
    • Administration of carnosine in the treatment of acute spinal cord injury
    • doi: 10.1016/j.bcp.2011.07.074
    • Di Paola, R., Impellizzeri, D., Trovato Salinaro, A., Mazzon, E., Bellia, F., Cavallaro, M., et al. (2011). Administration of carnosine in the treatment of acute spinal cord injury. Biochem. Pharm. 82, 1478-1489. doi: 10.1016/j.bcp.2011.07.074
    • (2011) Biochem. Pharm , vol.82 , pp. 1478-1489
    • Di Paola, R.1    Impellizzeri, D.2    Trovato Salinaro, A.3    Mazzon, E.4    Bellia, F.5    Cavallaro, M.6
  • 79
    • 84890100345 scopus 로고    scopus 로고
    • Oxidative damage and amyloid-ß metabolism in brain regions of the longest-lived rodents
    • doi: 10.1002/jnr.23320
    • Edrey, Y. H., Oddo, S., Cornelius, C., Caccamo, A., Calabrese, V., and Buffenstein, R. (2014). Oxidative damage and amyloid-ß metabolism in brain regions of the longest-lived rodents. J. Neurosci. Res. 92, 195-205. doi: 10.1002/jnr.23320
    • (2014) J. Neurosci. Res , vol.92 , pp. 195-205
    • Edrey, Y.H.1    Oddo, S.2    Cornelius, C.3    Caccamo, A.4    Calabrese, V.5    Buffenstein, R.6
  • 80
    • 77953916565 scopus 로고    scopus 로고
    • Dual functions of beta-amyloid oligomer and fibril in Cu(II)-induced H2O2 production
    • doi: 10.1016/j.regpep.2010.05.001
    • Fang, C. L., Wu, W. H., Liu, Q., Sun, X., Ma, Y., Zhao, Y. F., et al. (2010). Dual functions of beta-amyloid oligomer and fibril in Cu(II)-induced H2O2 production. Regul. Pept. 163, 1-6. doi: 10.1016/j.regpep.2010.05.001
    • (2010) Regul. Pept , vol.163 , pp. 1-6
    • Fang, C.L.1    Wu, W.H.2    Liu, Q.3    Sun, X.4    Ma, Y.5    Zhao, Y.F.6
  • 81
    • 75649144450 scopus 로고    scopus 로고
    • A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock
    • doi: 10.1091/mbc.E09-07-0639
    • Fujimoto, M., Hayashida, N., Katoh, T., Oshima, K., Shinkawa, T., Prakasam, R., et al. (2010). A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock. Mol. Biol. Cell 21, 106-116. doi: 10.1091/mbc.E09-07-0639
    • (2010) Mol. Biol. Cell , vol.21 , pp. 106-116
    • Fujimoto, M.1    Hayashida, N.2    Katoh, T.3    Oshima, K.4    Shinkawa, T.5    Prakasam, R.6
  • 82
    • 79958848355 scopus 로고    scopus 로고
    • Role of nuclear factor kappaB-mediated inflammatory pathways in cancer-related symptoms and their regulation by nutritional agents
    • (Maywood). doi: 10.1258/ebm.2011.011028
    • Gupta, S. C., Kim, J. H., Kannappan, R., Reuter, S., Dougherty, P. M., and Aggarwal, B. B. (2011). Role of nuclear factor kappaB-mediated inflammatory pathways in cancer-related symptoms and their regulation by nutritional agents. Exp. Biol. Med. (Maywood) 236, 658-671. doi: 10.1258/ebm.2011.011028
    • (2011) Exp. Biol. Med. , vol.236 , pp. 658-671
    • Gupta, S.C.1    Kim, J.H.2    Kannappan, R.3    Reuter, S.4    Dougherty, P.M.5    Aggarwal, B.B.6
  • 83
    • 84878786543 scopus 로고    scopus 로고
    • Oxidative modification of lipoic acid by HNE in Alzheimer disease brain
    • doi: 10.1016/j.redox.2013.01.002
    • Hardas, S. S., Sultana, R., Clark, A. M., Beckett, T. L., Szweda, L. I., Murphy, M. P., et al. (2013). Oxidative modification of lipoic acid by HNE in Alzheimer disease brain. Redox Biol. 1, 80-85. doi: 10.1016/j.redox.2013.01.002
    • (2013) Redox Biol , vol.1 , pp. 80-85
    • Hardas, S.S.1    Sultana, R.2    Clark, A.M.3    Beckett, T.L.4    Szweda, L.I.5    Murphy, M.P.6
  • 84
    • 84894292228 scopus 로고    scopus 로고
    • Relationship between amyloid-beta and the ubiquitin-proteasome system in Alzheimer's disease
    • doi: 10.1179/1743132813Y.0000000288
    • Hong, L., Huang, H. C., and Jiang, Z. F. (2014). Relationship between amyloid-beta and the ubiquitin-proteasome system in Alzheimer's disease. Neurol. Res. 36, 276-282. doi: 10.1179/1743132813Y.0000000288
    • (2014) Neurol. Res , vol.36 , pp. 276-282
    • Hong, L.1    Huang, H.C.2    Jiang, Z.F.3
  • 85
    • 84891373794 scopus 로고    scopus 로고
    • Markers of cholesterol transport are associated with amyloid deposition in the brain
    • doi: 10.1016/j.neurobiolaging.2013.09.040
    • Hughes, T. M., Lopez, O. L., Evans, R. W., Kamboh, M. I., Williamson, J. D., Klunk, W. E., et al. (2014). Markers of cholesterol transport are associated with amyloid deposition in the brain. Neurobiol. Aging 35, 802-807. doi: 10.1016/j.neurobiolaging.2013.09.040
    • (2014) Neurobiol. Aging , vol.35 , pp. 802-807
    • Hughes, T.M.1    Lopez, O.L.2    Evans, R.W.3    Kamboh, M.I.4    Williamson, J.D.5    Klunk, W.E.6
  • 86
    • 84891349503 scopus 로고    scopus 로고
    • Adjusting the compass: new insights into the role of angiogenesis in Alzheimer's disease
    • doi: 10.1186/alzrt230
    • Jefferies, W. A., Price, K. A., Biron, K. E., Fenninger, F., Pfeifer, C. G., and Dickstein, D. L. (2013). Adjusting the compass: new insights into the role of angiogenesis in Alzheimer's disease. Alzheimers Res. Ther. 5:64. doi: 10.1186/alzrt230
    • (2013) Alzheimers Res. Ther , vol.5 , Issue.64
    • Jefferies, W.A.1    Price, K.A.2    Biron, K.E.3    Fenninger, F.4    Pfeifer, C.G.5    Dickstein, D.L.6
  • 87
    • 84888265424 scopus 로고    scopus 로고
    • Distinct roles of sAPP-a and sAPP-ß in regulating U251 cell differentiation
    • doi: 10.2174/15672050113109990141
    • Jiang, J., Wang, Y., Hou, L., Fan, L., Wang, Q., Xu, Z., et al. (2013). Distinct roles of sAPP-a and sAPP-ß in regulating U251 cell differentiation. Curr. Alzheimer Res. 10, 706-713. doi: 10.2174/15672050113109990141
    • (2013) Curr. Alzheimer Res , vol.10 , pp. 706-713
    • Jiang, J.1    Wang, Y.2    Hou, L.3    Fan, L.4    Wang, Q.5    Xu, Z.6
  • 88
    • 84878439275 scopus 로고    scopus 로고
    • Clinical utility and analytical challenges in measurement of cerebrospinal fluid amyloid-ß(1-42) and t -proteins as Alzheimer disease biomarkers
    • doi: 10.1373/clinchem.2013.202937
    • Kang, J. H., Korecka, M., Toledo, J. B., Trojanowski, J. Q., and Shaw, L. M. (2013). Clinical utility and analytical challenges in measurement of cerebrospinal fluid amyloid-ß(1-42) and t -proteins as Alzheimer disease biomarkers. Clin. Chem. 59, 903-916. doi: 10.1373/clinchem.2013.202937
    • (2013) Clin. Chem , vol.59 , pp. 903-916
    • Kang, J.H.1    Korecka, M.2    Toledo, J.B.3    Trojanowski, J.Q.4    Shaw, L.M.5
  • 89
    • 84881399163 scopus 로고    scopus 로고
    • The Keap1/Nrf2 protein axis plays a role in osteoclast differentiation by regulating intracellular reactive oxygen species signaling
    • doi: 10.1074/jbc.M113.478545
    • Kanzaki, H., Shinohara, F., Kajiya, M., and Kodama, T. (2013). The Keap1/Nrf2 protein axis plays a role in osteoclast differentiation by regulating intracellular reactive oxygen species signaling. J. Biol. Chem. 288, 23009-230020. doi: 10.1074/jbc.M113.478545
    • (2013) J. Biol. Chem , vol.288 , pp. 23009-230020
    • Kanzaki, H.1    Shinohara, F.2    Kajiya, M.3    Kodama, T.4
  • 90
    • 54849442254 scopus 로고    scopus 로고
    • TNAP, TrAP, ecto-purinergic signaling, and bone remodeling
    • doi: 10.1002/jcb.21885
    • Kaunitz, J. D., and Yamaguchi, D. T. (2008). TNAP, TrAP, ecto-purinergic signaling, and bone remodeling. J. Cell. Biochem. 105, 655-662. doi: 10.1002/jcb.21885
    • (2008) J. Cell. Biochem , vol.105 , pp. 655-662
    • Kaunitz, J.D.1    Yamaguchi, D.T.2
  • 91
    • 84904738161 scopus 로고    scopus 로고
    • Cell survival programs and ischemia/reperfusion: hormesis, preconditioning, and cardioprotection
    • eds D. N. Granger and J. Granger (San Rafael, CA: Morgan & Claypool Life Science Digital Library)
    • Krenz, M., Baines, C., Kalogeris, T., and Korthuis, R. J. (2013). "Cell survival programs and ischemia/reperfusion: hormesis, preconditioning, and cardioprotection," in Colloquium Series on Integrated Systems Physiology: From Molecule to Function to Disease, Vol. 109, eds D. N. Granger and J. Granger (San Rafael, CA: Morgan & Claypool Life Science Digital Library), 1-32.
    • (2013) Colloquium Series on Integrated Systems Physiology: From Molecule to Function to Disease , vol.109 , pp. 1-32
    • Krenz, M.1    Baines, C.2    Kalogeris, T.3    Korthuis, R.J.4
  • 92
    • 84893590433 scopus 로고    scopus 로고
    • Amyloid beta peptide is elevated in osteoporotic bone tissues and enhances osteoclast function
    • doi: 10.1016/j.bone.2014.01.010
    • Li, S., Liu, B., Zhang, L., and Rong, L. (2014). Amyloid beta peptide is elevated in osteoporotic bone tissues and enhances osteoclast function. Bone 61C, 164-175. doi: 10.1016/j.bone.2014.01.010
    • (2014) Bone , vol.61 C , pp. 164-175
    • Li, S.1    Liu, B.2    Zhang, L.3    Rong, L.4
  • 93
    • 84896324370 scopus 로고    scopus 로고
    • The role of inflammasome in Alzheimer's disease
    • doi: 10.1016/j.arr.2013.12.007
    • Liu, L., and Chan, C. (2014). The role of inflammasome in Alzheimer's disease. Ageing Res. Rev. 15, 6-15. doi: 10.1016/j.arr.2013.12.007
    • (2014) Ageing Res. Rev , vol.15 , pp. 6-15
    • Liu, L.1    Chan, C.2
  • 94
    • 33646687948 scopus 로고    scopus 로고
    • Friedreich's ataxia: from disease mechanisms to therapeutic interventions
    • doi: 10.1089/ars.2006.8.438
    • Lodi, R., Tonon, C., Calabrese, V., and Schapira, A. H. (2006). Friedreich's ataxia: from disease mechanisms to therapeutic interventions. Antioxid. Redox Signal. 8, 438-443. doi: 10.1089/ars.2006.8.438
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 438-443
    • Lodi, R.1    Tonon, C.2    Calabrese, V.3    Schapira, A.H.4
  • 96
    • 34248187134 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, free radical generation and cellular stress response in neurodegenerative disorders
    • doi: 10.2741/2130
    • Mancuso, C., Scapagnini, G., Curro, D., Giuffrida Stella, A. M., De Marco, C., Butterfield, D. A., et al. (2007b). Mitochondrial dysfunction, free radical generation and cellular stress response in neurodegenerative disorders. Front. Biosci. 12:1107-1123. doi: 10.2741/2130
    • (2007) Front. Biosci , vol.12 , pp. 1107-1123
    • Mancuso, C.1    Scapagnini, G.2    Curro, D.3    Giuffrida Stella, A.M.4    De Marco, C.5    Butterfield, D.A.6
  • 97
    • 48249127222 scopus 로고    scopus 로고
    • Bilirubin as an endogenous modulator of neurotrophin redox signaling
    • doi: 10.1002/jnr.21665
    • Mancuso, C., Capone, C., Ranieri, S. C., Fusco, S., Calabrese, V., Eboli, M. L., et al. (2008). Bilirubin as an endogenous modulator of neurotrophin redox signaling. J. Neurosci. Res. 86, 1212-1230. doi: 10.1002/jnr.21665
    • (2008) J. Neurosci. Res , vol.86 , pp. 1212-1230
    • Mancuso, C.1    Capone, C.2    Ranieri, S.C.3    Fusco, S.4    Calabrese, V.5    Eboli, M.L.6
  • 98
    • 33750978157 scopus 로고    scopus 로고
    • Bilirubin: an endogenous scavenger of nitric oxide and reactive nitrogen species
    • doi: 10.1179/135100006X154978
    • Mancuso, C., Pani, G., and Calabrese, V. (2006). Bilirubin: an endogenous scavenger of nitric oxide and reactive nitrogen species. Redox Rep. 11, 207-213. doi: 10.1179/135100006X154978
    • (2006) Redox Rep , vol.11 , pp. 207-213
    • Mancuso, C.1    Pani, G.2    Calabrese, V.3
  • 99
    • 84896737480 scopus 로고    scopus 로고
    • Distinction between mild cognitive impairment and Alzheimer's disease by CSF amyloid ß(40) and ß(42), and protein-conjugated acrolein
    • doi: 10.1016/j.cca.2014.01.007
    • Mizoi, M., Yoshida, M., Saiki, R., Waragai, M., Uemura, K., Akatsu, H., et al. (2014). Distinction between mild cognitive impairment and Alzheimer's disease by CSF amyloid ß(40) and ß(42), and protein-conjugated acrolein. Clin. Chim. Acta. 430C, 150-155. doi: 10.1016/j.cca.2014.01.007
    • (2014) Clin. Chim. Acta , vol.430 C , pp. 150-155
    • Mizoi, M.1    Yoshida, M.2    Saiki, R.3    Waragai, M.4    Uemura, K.5    Akatsu, H.6
  • 100
    • 84881157846 scopus 로고    scopus 로고
    • Stress proteins in aging and life span
    • doi: 10.3109/02656736.2013.798873
    • Murshid, A., Eguchi, T., and Calderwood, S. K. (2013). Stress proteins in aging and life span. Int. J. Hyperthermia 29, 442-447. doi: 10.3109/02656736.2013.798873
    • (2013) Int. J. Hyperthermia , vol.29 , pp. 442-447
    • Murshid, A.1    Eguchi, T.2    Calderwood, S.K.3
  • 101
    • 84900024072 scopus 로고    scopus 로고
    • New Diagnostic Criteria and Guidelines on Osteoporosis. Anti-osteoporosis drugs based on the guidelines for the Prevention and Treatment of Osteoporosis
    • (2011 edition). doi: CliCa1403401406
    • Ono, K., Ohashi, S., and Tanaka, S. (2014). New Diagnostic Criteria and Guidelines on Osteoporosis. Anti-osteoporosis drugs based on the guidelines for the Prevention and Treatment of Osteoporosis (2011 edition). Clin. Calcium 24, 401-406. doi: CliCa1403401406
    • (2014) Clin. Calcium , vol.24 , pp. 401-406
    • Ono, K.1    Ohashi, S.2    Tanaka, S.3
  • 102
    • 84896711700 scopus 로고    scopus 로고
    • Imaging and cerebrospinal fluid biomarkers in the search for Alzheimer's disease mechanisms
    • doi: 10.1159/000355063
    • Osorio, R. S., Pirraglia, E., Gumb, T., Mantua, J., Ayappa, I., Williams, S., et al. (2014). Imaging and cerebrospinal fluid biomarkers in the search for Alzheimer's disease mechanisms. Neurodegener. Dis. 13, 163-165. doi: 10.1159/000355063
    • (2014) Neurodegener. Dis , vol.13 , pp. 163-165
    • Osorio, R.S.1    Pirraglia, E.2    Gumb, T.3    Mantua, J.4    Ayappa, I.5    Williams, S.6
  • 103
    • 84892694666 scopus 로고    scopus 로고
    • Increased OPG/RANKL ratio in the conditioned medium of soybean-treated osteoblasts suppresses RANKL-induced osteoclast differentiation
    • doi: 10.3892/ijmm.2013.1557
    • Park, K., Ju, W. C., Yeo, J. H., Kim, J. Y., Seo, H. S., Uchida, Y., et al. (2014). Increased OPG/RANKL ratio in the conditioned medium of soybean-treated osteoblasts suppresses RANKL-induced osteoclast differentiation. Int. J. Mol. Med. 33, 178-184. doi: 10.3892/ijmm.2013.1557
    • (2014) Int. J. Mol. Med , vol.33 , pp. 178-184
    • Park, K.1    Ju, W.C.2    Yeo, J.H.3    Kim, J.Y.4    Seo, H.S.5    Uchida, Y.6
  • 104
    • 79957904660 scopus 로고    scopus 로고
    • Synthesis of substituted triazolyl curcumin mimics that inhibit RANKL-induced osteoclastogenesis
    • doi: 10.1016/j.bmcl.2011.04.106
    • Park, S. K., Oh, S., Shin, H. K., Kim, S. H., Ham, J., Song, J. S., et al. (2011). Synthesis of substituted triazolyl curcumin mimics that inhibit RANKL-induced osteoclastogenesis. Bioorg. Med. Chem. Lett. 21, 3573-3577. doi: 10.1016/j.bmcl.2011.04.106
    • (2011) Bioorg. Med. Chem. Lett , vol.21 , pp. 3573-3577
    • Park, S.K.1    Oh, S.2    Shin, H.K.3    Kim, S.H.4    Ham, J.5    Song, J.S.6
  • 105
    • 80054684930 scopus 로고    scopus 로고
    • Redox regulation of cellular stress response in multiple sclerosis
    • doi: 10.1016/j.bcp.2011.07.092
    • Pennisi, G., Cornelius, C., Cavallaro, M. M., Trovato Salinaro, A., Cambria, M. T., Pennisi, M., et al. (2011). Redox regulation of cellular stress response in multiple sclerosis. Biochem. Pharm. 82, 1490-1499. doi: 10.1016/j.bcp.2011.07.092
    • (2011) Biochem. Pharm , vol.82 , pp. 1490-1499
    • Pennisi, G.1    Cornelius, C.2    Cavallaro, M.M.3    Trovato Salinaro, A.4    Cambria, M.T.5    Pennisi, M.6
  • 106
    • 78049423686 scopus 로고    scopus 로고
    • Redox proteomics in aging rat brain: involvement of mitochondrial reduced glutathione status and mitochondrial protein oxidation in the aging process
    • doi: 10.1002/jnr.22500
    • Perluigi, M., Di Domenico, F., Giorgi, A., Schininà, M. E., Coccia, R., Cini, C., et al. (2010). Redox proteomics in aging rat brain: involvement of mitochondrial reduced glutathione status and mitochondrial protein oxidation in the aging process. J. Neurosci. Res. 88, 3498-3507. doi: 10.1002/jnr.22500
    • (2010) J. Neurosci. Res , vol.88 , pp. 3498-3507
    • Perluigi, M.1    Di Domenico, F.2    Giorgi, A.3    Schininà, M.E.4    Coccia, R.5    Cini, C.6
  • 107
    • 33746415658 scopus 로고    scopus 로고
    • In vivo protective effects of ferulic acid ethyl ester against amyloid-beta peptide 1-42-induced oxidative stress
    • doi: 10.1002/jnr.20879
    • Perluigi, M., Joshi, G., Sultana, R., Calabrese, V., De Marco, C., Coccia, R., et al. (2006). In vivo protective effects of ferulic acid ethyl ester against amyloid-beta peptide 1-42-induced oxidative stress. J. Neurosci. Res. 84, 418-426. doi: 10.1002/jnr.20879
    • (2006) J. Neurosci. Res , vol.84 , pp. 418-426
    • Perluigi, M.1    Joshi, G.2    Sultana, R.3    Calabrese, V.4    De Marco, C.5    Coccia, R.6
  • 108
    • 69149105914 scopus 로고    scopus 로고
    • Apoptosis of human primary osteoclasts treated with molecules targeting nuclear factor-kappaB
    • doi: 10.1111/j.1749-6632.2009.04906.x
    • Piva, R., Penolazzi, L., Borgatti, M., Lampronti, I., Lambertini, E., Torreggiani, E., et al. (2009). Apoptosis of human primary osteoclasts treated with molecules targeting nuclear factor-kappaB. Ann. N. Y. Acad. Sci. 1171, 448-456. doi: 10.1111/j.1749-6632.2009.04906.x
    • (2009) Ann. N. Y. Acad. Sci , vol.1171 , pp. 448-456
    • Piva, R.1    Penolazzi, L.2    Borgatti, M.3    Lampronti, I.4    Lambertini, E.5    Torreggiani, E.6
  • 109
    • 84911981780 scopus 로고    scopus 로고
    • Review of the validated HPLC and LC-MS/MS methods for determination of drugs used in clinical practice for Alzheimer's disease
    • doi: 10.1002/bmc.3116. [Epub ahead of print].
    • Ponnayyan Sulochana, S., Sharma, K., Mullangi, R., and Sukumaran, S. K. (2014). Review of the validated HPLC and LC-MS/MS methods for determination of drugs used in clinical practice for Alzheimer's disease. Biomed. Chromatogr. doi: 10.1002/bmc.3116. [Epub ahead of print].
    • (2014) Biomed. Chromatogr
    • Ponnayyan Sulochana, S.1    Sharma, K.2    Mullangi, R.3    Sukumaran, S.K.4
  • 110
    • 79953751008 scopus 로고    scopus 로고
    • Osteoporosis: now and the future
    • doi: 10.1016/S0140-6736(10)62349-5
    • Rachner, T. D., Khosla, S., and Hofbauer, L. C. (2011). Osteoporosis: now and the future. Lancet 377, 1276-1287. doi: 10.1016/S0140-6736(10)62349-5
    • (2011) Lancet , vol.377 , pp. 1276-1287
    • Rachner, T.D.1    Khosla, S.2    Hofbauer, L.C.3
  • 111
    • 84895927467 scopus 로고    scopus 로고
    • Dementia: mild cognitive impairment - not always what it seems
    • doi: 10.1038/nrneurol.2014.23
    • Richard, E., and Brayne, C. (2014). Dementia: mild cognitive impairment - not always what it seems. Nat. Rev. Neurol. 10, 130-131. doi: 10.1038/nrneurol.2014.23
    • (2014) Nat. Rev. Neurol , vol.10 , pp. 130-131
    • Richard, E.1    Brayne, C.2
  • 112
    • 58049155245 scopus 로고    scopus 로고
    • Amyloid beta peptides in human plasma and tissues and their significance for Alzheimer's disease
    • doi: 10.1016/j.jalz.2008.10.004
    • Roher, A. E., Esh, C. L., Kokjohn, T. A., Castano, E. M., Van Vickle, G. D., Kalback, W. M., et al. (2009). Amyloid beta peptides in human plasma and tissues and their significance for Alzheimer's disease. Alzheimers Dement. 5, 18-29. doi: 10.1016/j.jalz.2008.10.004
    • (2009) Alzheimers Dement , vol.5 , pp. 18-29
    • Roher, A.E.1    Esh, C.L.2    Kokjohn, T.A.3    Castano, E.M.4    Van Vickle, G.D.5    Kalback, W.M.6
  • 113
    • 84886412961 scopus 로고    scopus 로고
    • Chaperone machines for protein folding, unfolding and disaggregation
    • doi: 10.1038/nrm3658
    • Saibil, H. (2013). Chaperone machines for protein folding, unfolding and disaggregation. Nat. Rev. Mol. Cell Biol. 14, 630-642. doi: 10.1038/nrm3658
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 630-642
    • Saibil, H.1
  • 114
    • 79956318842 scopus 로고    scopus 로고
    • Therapeutic potential of dietary polyphenols against brain ageing and neurodegenerative disorders
    • doi: 10.1007/978-1-4419-7347-4_3
    • Scapagnini, G., Caruso, C., and Calabrese, V. (2011). Therapeutic potential of dietary polyphenols against brain ageing and neurodegenerative disorders. Adv. Exp. Med. Biol. 698, 27-35. doi: 10.1007/978-1-4419-7347-4_3
    • (2011) Adv. Exp. Med. Biol , vol.698 , pp. 27-35
    • Scapagnini, G.1    Caruso, C.2    Calabrese, V.3
  • 115
    • 33646691510 scopus 로고    scopus 로고
    • Curcumin activates defensive genes and protects neurons against oxidative stress
    • doi: 10.1089/ars.2006.8.395
    • Scapagnini, G., Colombrita, C., Amadio, M., D'Agata, V., Arcelli, E., Sapienza, M., et al. (2006). Curcumin activates defensive genes and protects neurons against oxidative stress. Antioxid. Redox Signal. 8, 395-403. doi: 10.1089/ars.2006.8.395
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 395-403
    • Scapagnini, G.1    Colombrita, C.2    Amadio, M.3    D'Agata, V.4    Arcelli, E.5    Sapienza, M.6
  • 116
    • 0001155660 scopus 로고
    • Zur Lehre von der Arzneiwirdung
    • doi: 10.1007/BF02281473
    • Schulz, H. (1887). Zur Lehre von der Arzneiwirdung. Virchows Arch. Pathol. Anat. Physiol. Klin. Med. 108, 423-445. doi: 10.1007/BF02281473
    • (1887) Virchows Arch. Pathol. Anat. Physiol. Klin. Med , vol.108 , pp. 423-445
    • Schulz, H.1
  • 118
    • 81155126167 scopus 로고    scopus 로고
    • Experimental research on nitric oxide and the therapy of Alzheimer disease: a challenging bridge
    • doi: 10.2174/187152711798072356
    • Siciliano, R., Barone, E., Calabrese, V., Rispoli, V., Butterfield, D. A., and Mancuso, C. (2011). Experimental research on nitric oxide and the therapy of Alzheimer disease: a challenging bridge. CNS Neurol. Disord. Drug Targets 10, 766-776. doi: 10.2174/187152711798072356
    • (2011) CNS Neurol. Disord. Drug Targets , vol.10 , pp. 766-776
    • Siciliano, R.1    Barone, E.2    Calabrese, V.3    Rispoli, V.4    Butterfield, D.A.5    Mancuso, C.6
  • 119
    • 0000000661 scopus 로고
    • Effects of extract of western red-cedar heartwood on certain wood-decaying fungi in culture
    • Southam, C. M., and Ehrlich, J. (1943). Effects of extract of western red-cedar heartwood on certain wood-decaying fungi in culture. Phytopathology 33, 517-524.
    • (1943) Phytopathology , vol.33 , pp. 517-524
    • Southam, C.M.1    Ehrlich, J.2
  • 120
    • 77953365526 scopus 로고    scopus 로고
    • The pivotal role of the alternative NF-kappaB pathway in maintenance of basal bone homeostasis and osteoclastogenesis
    • doi: 10.1359/jbmr.091030
    • Soysa, N. S., Alles, N., Weih, D., Lovas, A., Mian, A. H., Shimokawa, H., et al. (2010). The pivotal role of the alternative NF-kappaB pathway in maintenance of basal bone homeostasis and osteoclastogenesis. J. Bone Miner. Res. 25, 809-818. doi: 10.1359/jbmr.091030
    • (2010) J. Bone Miner. Res , vol.25 , pp. 809-818
    • Soysa, N.S.1    Alles, N.2    Weih, D.3    Lovas, A.4    Mian, A.H.5    Shimokawa, H.6
  • 121
    • 84898000916 scopus 로고    scopus 로고
    • Senescence-accelerated OXYS rats: a model of age-related cognitive decline with relevance to abnormalities in Alzheimer disease
    • doi: 10.4161/cc.28255
    • Stefanova, N. A., Kozhevnikova, O. S., Vitovtov, A. O., Maksimova, K. Y., Logvinov, S. V., Rudnitskaya, E. A., et al. (2014). Senescence-accelerated OXYS rats: a model of age-related cognitive decline with relevance to abnormalities in Alzheimer disease. Cell Cycle 13, 898-909. doi: 10.4161/cc.28255
    • (2014) Cell Cycle , vol.13 , pp. 898-909
    • Stefanova, N.A.1    Kozhevnikova, O.S.2    Vitovtov, A.O.3    Maksimova, K.Y.4    Logvinov, S.V.5    Rudnitskaya, E.A.6
  • 122
    • 84858735072 scopus 로고    scopus 로고
    • The noncanonical NF-κB pathway
    • doi: 10.1111/j.1600-065X.2011.01088.x
    • Sun, S. C. (2012). The noncanonical NF-κB pathway. Immunol. Rev. 246, 125-140. doi: 10.1111/j.1600-065X.2011.01088.x
    • (2012) Immunol. Rev , vol.246 , pp. 125-140
    • Sun, S.C.1
  • 123
    • 84903276737 scopus 로고    scopus 로고
    • Abeta, oxidative stress in Alzheimer disease: evidence based on proteomics studies
    • doi: 10.1016/j.bbadis.2013.09.015 [Epub ahead of print].
    • Swomley, A. M., Förster, S., Keeney, J. T., Triplett, J., Zhang, Z., Sultana, R., et al. (2013). Abeta, oxidative stress in Alzheimer disease: evidence based on proteomics studies. Biochim. Biophys. Acta doi: 10.1016/j.bbadis.2013.09.015 [Epub ahead of print].
    • (2013) Biochim. Biophys. Acta
    • Swomley, A.M.1    Förster, S.2    Keeney, J.T.3    Triplett, J.4    Zhang, Z.5    Sultana, R.6
  • 124
    • 84895866256 scopus 로고    scopus 로고
    • Targeting the intrinsically disordered structural ensemble of a-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease
    • doi: 10.1371/journal.pone.0087133
    • Tóth, G., Gardai, S. J., Zago, W., Bertoncini, C. W., Cremades, N., Roy, S. L., et al. (2014). Targeting the intrinsically disordered structural ensemble of a-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease. PLoS ONE 9:e87133. doi: 10.1371/journal.pone.0087133
    • (2014) PLoS ONE , vol.9
    • Tóth, G.1    Gardai, S.J.2    Zago, W.3    Bertoncini, C.W.4    Cremades, N.5    Roy, S.L.6
  • 125
    • 84882436145 scopus 로고    scopus 로고
    • The role of homocysteine in bone remodeling
    • doi: 10.1515/cclm-2012-0605
    • Vacek, T. P., Kalani, A., Voor, M. J., Tyagi, S. C., and Tyagi, N. (2013). The role of homocysteine in bone remodeling. Clin. Chem. Lab. Med. 51, 579-590. doi: 10.1515/cclm-2012-0605
    • (2013) Clin. Chem. Lab. Med , vol.51 , pp. 579-590
    • Vacek, T.P.1    Kalani, A.2    Voor, M.J.3    Tyagi, S.C.4    Tyagi, N.5
  • 126
    • 84896938404 scopus 로고    scopus 로고
    • Identification of human ABAD inhibitors for rescuing Aß-mediated mitochondrial dysfunction
    • doi: 10.2174/1567205011666140130150108
    • Valasani, K. R., Sun, Q., Hu, G., Li, J., Du, F., Guo, Y., et al. (2014). Identification of human ABAD inhibitors for rescuing Aß-mediated mitochondrial dysfunction. Curr. Alzheimer Res. 11, 128-136. doi: 10.2174/1567205011666140130150108
    • (2014) Curr. Alzheimer Res , vol.11 , pp. 128-136
    • Valasani, K.R.1    Sun, Q.2    Hu, G.3    Li, J.4    Du, F.5    Guo, Y.6
  • 127
    • 49849088591 scopus 로고    scopus 로고
    • Mitochondria as chi
    • doi: 10.1534/genetics.104.91769
    • Wallace, D. C. (2008). Mitochondria as chi. Genetics 179, 727-735. doi: 10.1534/genetics.104.91769
    • (2008) Genetics , vol.179 , pp. 727-735
    • Wallace, D.C.1
  • 128
    • 77953507107 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in disease and aging
    • doi: 10.1002/em.20586
    • Wallace, D. C. (2010). Mitochondrial DNA mutations in disease and aging. Environ. Mol. Mutagen. 5, 440-450. doi: 10.1002/em.20586
    • (2010) Environ. Mol. Mutagen , vol.5 , pp. 440-450
    • Wallace, D.C.1
  • 129
    • 84866665390 scopus 로고    scopus 로고
    • Mitochondria and cancer
    • doi: 10.1038/nrc3365
    • Wallace, D. C. (2012). Mitochondria and cancer. Nat. Rev. Cancer 10, 685-698. doi: 10.1038/nrc3365
    • (2012) Nat. Rev. Cancer , vol.10 , pp. 685-698
    • Wallace, D.C.1
  • 130
    • 84892715273 scopus 로고    scopus 로고
    • Bioenergetics in human evolution and disease: implications for the origins of biological complexity and the missing genetic variation of common diseases
    • doi: 10.1098/rstb.2012.0267
    • Wallace, D. C. (2013). Bioenergetics in human evolution and disease: implications for the origins of biological complexity and the missing genetic variation of common diseases. Philos. Trans. R. Soc. Lond. B Biol. Sci. 368, 20120267. doi: 10.1098/rstb.2012.0267
    • (2013) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.368 , pp. 20120267
    • Wallace, D.C.1
  • 131
    • 84857131348 scopus 로고    scopus 로고
    • HSF transcription factor family, heat shock response, and protein intrinsic disorder
    • doi: 10.2174/138920312799277956
    • Westerheide, S. D., Raynes, R., Powell, C., Xue, B., and Uversky, V. N. (2012). HSF transcription factor family, heat shock response, and protein intrinsic disorder. Curr. Protein Pept. Sci. 13, 86-103. doi: 10.2174/138920312799277956
    • (2012) Curr. Protein Pept. Sci , vol.13 , pp. 86-103
    • Westerheide, S.D.1    Raynes, R.2    Powell, C.3    Xue, B.4    Uversky, V.N.5
  • 132
    • 84890928478 scopus 로고    scopus 로고
    • Caloric restriction, caloric restriction mimetics, and healthy aging in Okinawa: controversies and clinical implications
    • doi: 10.1097/MCO.0000000000000019
    • Willcox, B. J., and Willcox, D. C. (2014). Caloric restriction, caloric restriction mimetics, and healthy aging in Okinawa: controversies and clinical implications. Curr. Opin. Clin. Nutr. Metab. Care 17, 51-58. doi: 10.1097/MCO.0000000000000019
    • (2014) Curr. Opin. Clin. Nutr. Metab. Care , vol.17 , pp. 51-58
    • Willcox, B.J.1    Willcox, D.C.2
  • 133
    • 84887199518 scopus 로고    scopus 로고
    • Osteoporosis: linking osteoporosis with Alzheimer disease
    • doi: 10.1038/nrrheum.2013.152
    • Woodman, I. (2013). Osteoporosis: linking osteoporosis with Alzheimer disease. Nat. Rev. Rheumatol. 9, 638. doi: 10.1038/nrrheum.2013.152
    • (2013) Nat. Rev. Rheumatol , vol.9 , pp. 638
    • Woodman, I.1
  • 134
    • 84884506516 scopus 로고    scopus 로고
    • Swedish mutant APP suppresses osteoblast differentiation and causes osteoporotic deficit, which are ameliorated by N-acetyl-L-cysteine
    • doi: 10.1002/jbmr.1954
    • Xia, W. F., Jung, J. U., Shun, C., Xiong, S., Xiong, L., Shi, X. M., et al. (2013). Swedish mutant APP suppresses osteoblast differentiation and causes osteoporotic deficit, which are ameliorated by N-acetyl-L-cysteine. J. Bone Miner. Res. 28, 2122-2135. doi: 10.1002/jbmr.1954
    • (2013) J. Bone Miner. Res , vol.28 , pp. 2122-2135
    • Xia, W.F.1    Jung, J.U.2    Shun, C.3    Xiong, S.4    Xiong, L.5    Shi, X.M.6
  • 135
    • 82255181180 scopus 로고    scopus 로고
    • HSF1-dependent upregulation of Hsp70 by sulfhydryl-reactive inducers of the KEAP1/NRF2/ARE pathway
    • doi: 10.1016/j.chembiol.2011.09.008
    • Zhang, Y., Ahn, Y. H., Benjamin, I. J., Honda, T., Hicks, R. J., Calabrese, V., et al. (2011). HSF1-dependent upregulation of Hsp70 by sulfhydryl-reactive inducers of the KEAP1/NRF2/ARE pathway. Chem. Biol. 18, 1355-1361. doi: 10.1016/j.chembiol.2011.09.008
    • (2011) Chem. Biol , vol.18 , pp. 1355-1361
    • Zhang, Y.1    Ahn, Y.H.2    Benjamin, I.J.3    Honda, T.4    Hicks, R.J.5    Calabrese, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.