메뉴 건너뛰기




Volumn 3, Issue 4, 2006, Pages 377-391

Challenges in neuronal apoptosis

Author keywords

amyloid protein; Alzheimer disease; Apoptosis; Caspases; Cell cycle; Death effector domain; Programmed cell death; Signaling pathways; Tau phosphorylation

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; CASPASE 3; CASPASE INHIBITOR; DNA FRAGMENT; TUMOR NECROSIS FACTOR;

EID: 33748474961     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/156720506778249434     Document Type: Review
Times cited : (69)

References (202)
  • 2
    • 1542381057 scopus 로고    scopus 로고
    • Cell cycle regulation of neuronal apoptosis in development and disease
    • Becker EB and Bonni A. Cell cycle regulation of neuronal apoptosis in development and disease. Prog Neurobiol 72: 1-25 (2004).
    • (2004) Prog Neurobiol , vol.72 , pp. 1-25
    • Becker, E.B.1    Bonni, A.2
  • 3
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH and Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26: 239-257 (1972).
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 6
    • 0002710249 scopus 로고
    • Ueber die Bildung von Richtungsfiguren in Saeugethiereiern beim Untergang Graaf'scher Follikel
    • Flemming W. Ueber die Bildung von Richtungsfiguren in Saeugethiereiern beim Untergang Graaf'scher Follikel. Arch Anat Physiol: 221-224 (1885).
    • (1885) Arch Anat Physiol , pp. 221-224
    • Flemming, W.1
  • 7
    • 0002023977 scopus 로고    scopus 로고
    • Apoptosis versus necrosis
    • (Eds Koliatsosue M, Ratan RR). Humana Press, Totowa, NY
    • Clarke PGH. Apoptosis versus necrosis. In 'Cell death and disease of the nervous system' (Eds Koliatsosue M, Ratan RR). Humana Press, Totowa, NY, pp. 3-28 (1999).
    • (1999) Cell Death and Disease of the Nervous System , pp. 3-28
    • Clarke, P.G.H.1
  • 8
    • 0032765190 scopus 로고    scopus 로고
    • The nomenclature of cell death: Recommendations of an ad hoc Committee of the Society of Toxicologic Pathologists
    • Levin S, Bucci TJ, Cohen SM, Fix AS, Hardisty JF, LeGrand EK, et al. The nomenclature of cell death: recommendations of an ad hoc Committee of the Society of Toxicologic Pathologists. Toxicol Pathol 27: 484-490 (1999).
    • (1999) Toxicol Pathol , vol.27 , pp. 484-490
    • Levin, S.1    Bucci, T.J.2    Cohen, S.M.3    Fix, A.S.4    Hardisty, J.F.5    LeGrand, E.K.6
  • 9
    • 0019225636 scopus 로고
    • Cell death: The significance of apoptosis
    • Wyllie AH, Kerr JF and Currie AR. Cell death: the significance of apoptosis. Int Rev Cytol 68: 251-306 (1980).
    • (1980) Int Rev Cytol , vol.68 , pp. 251-306
    • Wyllie, A.H.1    Kerr, J.F.2    Currie, A.R.3
  • 10
    • 22544480574 scopus 로고    scopus 로고
    • Phagocytosis of apoptotic cells: A matter of balance
    • Almeida CJ and Linden R. Phagocytosis of apoptotic cells: a matter of balance. Cell Mol Life Sci: (2005).
    • (2005) Cell Mol Life Sci
    • Almeida, C.J.1    Linden, R.2
  • 11
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky DJ and Emr SD. Autophagy as a regulated pathway of cellular degradation. Science 290: 1717-1721 (2000).
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 13
    • 0033667521 scopus 로고    scopus 로고
    • Role of mitochondria in neuronal apoptosis
    • Gorman AM, Ceccatelli S and Orrenius S. Role of mitochondria in neuronal apoptosis. Dev Neurosci 22: 348-358 (2000).
    • (2000) Dev Neurosci , vol.22 , pp. 348-358
    • Gorman, A.M.1    Ceccatelli, S.2    Orrenius, S.3
  • 14
    • 0033290849 scopus 로고    scopus 로고
    • Apoptosis and necrosis: Different execution of the same death
    • Nicotera P, Leist M and Ferrando-May E. Apoptosis and necrosis: different execution of the same death. Biochem Soc Symp 66: 69-73 (1999).
    • (1999) Biochem Soc Symp , vol.66 , pp. 69-73
    • Nicotera, P.1    Leist, M.2    Ferrando-May, E.3
  • 15
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S and Martinou JC. Mitochondria as the central control point of apoptosis. Trends Cell Biol 10: 369-377 (2000).
    • (2000) Trends Cell Biol , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 16
    • 0035077448 scopus 로고    scopus 로고
    • Problems of cell death in neurodegeneration and Alzheimer's Disease
    • Jellinger KA and Stadelmann C. Problems of cell death in neurodegeneration and Alzheimer's Disease. J Alzheimers Dis 3: 31-40 (2001).
    • (2001) J Alzheimers Dis , vol.3 , pp. 31-40
    • Jellinger, K.A.1    Stadelmann, C.2
  • 17
    • 0031029859 scopus 로고    scopus 로고
    • Excitotoxic neuronal death in the immature brain is an apoptosis-necrosis morphological continuum
    • Portera-Cailliau C, Price DL and Martin LJ. Excitotoxic neuronal death in the immature brain is an apoptosis-necrosis morphological continuum. J Comp Neurol 378: 70-87 (1997).
    • (1997) J Comp Neurol , vol.378 , pp. 70-87
    • Portera-Cailliau, C.1    Price, D.L.2    Martin, L.J.3
  • 18
    • 0035348408 scopus 로고    scopus 로고
    • Neuronal cell death in nervous system development, disease, and injury
    • Martin LJ. Neuronal cell death in nervous system development, disease, and injury (Review). Int J Mol Med 7: 455-478 (2001).
    • (2001) Int J Mol Med , vol.7 , pp. 455-478
    • Martin, L.J.1
  • 19
    • 0034520112 scopus 로고    scopus 로고
    • The enigma of cell death in neurodegenerative disorders
    • Jellinger KA and Stadelmann CH. The enigma of cell death in neurodegenerative disorders. J Neural Transm Suppl: 21-36 (2000).
    • (2000) J Neural Transm Suppl , pp. 21-36
    • Jellinger, K.A.1    Stadelmann, C.H.2
  • 20
    • 0036019165 scopus 로고    scopus 로고
    • Mechanisms of cell death in neurodegenerative diseases: Fashion, fiction, and facts
    • Graeber MB and Moran LB. Mechanisms of cell death in neurodegenerative diseases: fashion, fiction, and facts. Brain Pathol 12: 385-390 (2002).
    • (2002) Brain Pathol , vol.12 , pp. 385-390
    • Graeber, M.B.1    Moran, L.B.2
  • 22
    • 2342465589 scopus 로고    scopus 로고
    • Regulation of the apoptosis-necrosis switch
    • Nicotera P and Melino G. Regulation of the apoptosis-necrosis switch. Oncogene 2757-65: 2757-2765 (2004).
    • (2004) Oncogene , vol.2757 , Issue.65 , pp. 2757-2765
    • Nicotera, P.1    Melino, G.2
  • 23
    • 0141884305 scopus 로고    scopus 로고
    • Diversity in the mechanisms of neuronal cell death
    • Yuan J, Lipinski M and Degterev A. Diversity in the mechanisms of neuronal cell death. Neuron 40: 401-413 (2003).
    • (2003) Neuron , vol.40 , pp. 401-413
    • Yuan, J.1    Lipinski, M.2    Degterev, A.3
  • 24
    • 27844595293 scopus 로고    scopus 로고
    • Caspase and calpain function in cell death: Bridging the gap between apoptosis and necrosis
    • Harwood SM, Yaqoob MM and Allen DA. Caspase and calpain function in cell death: bridging the gap between apoptosis and necrosis. Ann Clin Biochem 42: 415-431 (2005).
    • (2005) Ann Clin Biochem , vol.42 , pp. 415-431
    • Harwood, S.M.1    Yaqoob, M.M.2    Allen, D.A.3
  • 25
    • 1542747255 scopus 로고    scopus 로고
    • Apoptosis vs nonapoptotic mechanisms in neurodegeneration
    • (Ed Wood PL). Human Press, Totowa, NJ
    • Jellinger KA. Apoptosis vs nonapoptotic mechanisms in neurodegeneration. In 'Neuroinflammation. 2nd Edition' (Ed Wood PL). Human Press, Totowa, NJ, pp 29-88 (2003).
    • (2003) Neuroinflammation. 2nd Edition , pp. 29-88
    • Jellinger, K.A.1
  • 26
    • 0033786442 scopus 로고    scopus 로고
    • Apoptosis: Overview and signal transduction pathways
    • Bredesen DE. Apoptosis: overview and signal transduction pathways. J Neurotrauma 17: 801-810 (2000).
    • (2000) J Neurotrauma , vol.17 , pp. 801-810
    • Bredesen, D.E.1
  • 27
    • 0030829777 scopus 로고    scopus 로고
    • Apoptosis: An overview
    • Wyllie AH. Apoptosis: an overview. Br Med Bull 53: 451-465 (1997).
    • (1997) Br Med Bull , vol.53 , pp. 451-465
    • Wyllie, A.H.1
  • 28
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan J and Yankner BA. Apoptosis in the nervous system. Nature 407: 802-809 (2000).
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 29
    • 0036793843 scopus 로고    scopus 로고
    • Csp-cleaved amyloid precursor protein in Alzheimer's disease
    • Ayala-Grosso C, Ng G, Roy S and Robertson GS. Csp-cleaved amyloid precursor protein in Alzheimer's disease. Brain Pathol 12: 430-441 (2002).
    • (2002) Brain Pathol , vol.12 , pp. 430-441
    • Ayala-Grosso, C.1    Ng, G.2    Roy, S.3    Robertson, G.S.4
  • 30
    • 85160144618 scopus 로고    scopus 로고
    • Cell death in Parkinson's disease
    • (Eds Ebadi M, Pfeiffer RF). CRC Press, Boca Raton, London, New York, Washington
    • Faherty CJ and Smeyne RJ. Cell death in Parkinson's disease. In 'Parkinson's Disease' (Eds Ebadi M, Pfeiffer RF). CRC Press, Boca Raton, London, New York, Washington, pp 523-535 (2005).
    • (2005) Parkinson's Disease , pp. 523-535
    • Faherty, C.J.1    Smeyne, R.J.2
  • 31
    • 2342502556 scopus 로고    scopus 로고
    • Neuronal apoptosis in neurodegenerative diseases: From basic research to clinical application
    • Kermer P, Liman J, Weishaupt JH and Baehr M. Neuronal apoptosis in neurodegenerative diseases: from basic research to clinical application. Neurodeg Dis 1: 9-19 (2004).
    • (2004) Neurodeg Dis , vol.1 , pp. 9-19
    • Kermer, P.1    Liman, J.2    Weishaupt, J.H.3    Baehr, M.4
  • 32
    • 24344508845 scopus 로고    scopus 로고
    • Csp-cleaved tau accumulation in neurodegenerative diseases associated with tau and alpha-synuclein pathology
    • Berl
    • Newman J, Rissman RA, Sarsoza F, Kim RC, Dick M, Bennett DA, et al. Csp-cleaved tau accumulation in neurodegenerative diseases associated with tau and alpha-synuclein pathology. Acta Neuropathol (Berl) 110: 135-144 (2005).
    • (2005) Acta Neuropathol , vol.110 , pp. 135-144
    • Newman, J.1    Rissman, R.A.2    Sarsoza, F.3    Kim, R.C.4    Dick, M.5    Bennett, D.A.6
  • 34
    • 0034830488 scopus 로고    scopus 로고
    • Caspases, apoptosis, and Alzheimer disease: Causation, correlation, and confusion
    • Roth KA. Caspases, apoptosis, and Alzheimer disease: causation, correlation, and confusion. J Neuropathol Exp Neurol 60: 829-838 (2001).
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 829-838
    • Roth, K.A.1
  • 35
    • 0034864628 scopus 로고    scopus 로고
    • Apoptosis in amyotrophic lateral sclerosis: A review of the evidence
    • Sathasivam S, Ince PG and Shaw PJ. Apoptosis in amyotrophic lateral sclerosis: a review of the evidence. Neuropathol Appl Neurobiol 27: 257-274 (2001).
    • (2001) Neuropathol Appl Neurobiol , vol.27 , pp. 257-274
    • Sathasivam, S.1    Ince, P.G.2    Shaw, P.J.3
  • 36
    • 5444270967 scopus 로고    scopus 로고
    • Neuronal pathology in Parkinson's disease
    • Schulz JB and Falkenburger BH. Neuronal pathology in Parkinson's disease. Cell Tissue Res 318: 135-147 (2004).
    • (2004) Cell Tissue Res , vol.318 , pp. 135-147
    • Schulz, J.B.1    Falkenburger, B.H.2
  • 37
    • 0032993576 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative diseases: The role of mitochondria
    • Tatton WG and Olanow CW. Apoptosis in neurodegenerative diseases: the role of mitochondria. Biochim Biophys Acta 1410: 195-213 (1999).
    • (1999) Biochim Biophys Acta , vol.1410 , pp. 195-213
    • Tatton, W.G.1    Olanow, C.W.2
  • 39
    • 0031958152 scopus 로고    scopus 로고
    • Apoptosis decision cascades and neuronal degeneration in Alzheimer's disease
    • Cotman CW. Apoptosis decision cascades and neuronal degeneration in Alzheimer's disease. Neurobiol Aging 19: S29-32 (1998).
    • (1998) Neurobiol Aging , vol.19
    • Cotman, C.W.1
  • 41
    • 0001263665 scopus 로고    scopus 로고
    • Cellular signaling pathways in neuronal apoptosis. Role in neurodegeneration and Alzheimer's disease
    • (Ed Reith MEA). Humana Press, Totowa, NJ
    • Cotman CW, Qian HY and Anderson AJ. Cellular signaling pathways in neuronal apoptosis. Role in neurodegeneration and Alzheimer's disease. In 'Cerebral Signal Transduction. From First to Fourth Messengers' (Ed Reith MEA). Humana Press, Totowa, NJ, pp. 175-206 (2000).
    • (2000) Cerebral Signal Transduction. from First to Fourth Messengers , pp. 175-206
    • Cotman, C.W.1    Qian, H.Y.2    Anderson, A.J.3
  • 42
    • 0142010013 scopus 로고    scopus 로고
    • General aspects of neurodegeneration
    • Jellinger KA. General aspects of neurodegeneration. J Neural Transm Suppl: 101-144 (2003).
    • (2003) J Neural Transm Suppl , pp. 101-144
    • Jellinger, K.A.1
  • 44
    • 1542432296 scopus 로고    scopus 로고
    • Mechanisms of neuronal apoptosis and excitotoxicity
    • (Ed Mattson MP). Humana Press, Totowa, NJ
    • Mattson MP. Mechanisms of neuronal apoptosis and excitotoxicity. In 'Pathogenesis of Neurodegenerative Disorders' (Ed Mattson MP). Humana Press, Totowa, NJ, pp. 1-20 (2001).
    • (2001) Pathogenesis of Neurodegenerative Disorders , pp. 1-20
    • Mattson, M.P.1
  • 46
    • 0034320568 scopus 로고    scopus 로고
    • Mechanisms of apoptosis
    • Reed JC. Mechanisms of apoptosis. Am J Pathol 157: 1415-1430 (2000).
    • (2000) Am J Pathol , vol.157 , pp. 1415-1430
    • Reed, J.C.1
  • 48
    • 0033779336 scopus 로고    scopus 로고
    • Attenuation of a Csp-3 dependent cell death in NT4- and p75-deficient embryonic sensory neurons
    • Agerman K, Baudet C, Fundin B, Willson C and Ernfors P. Attenuation of a Csp-3 dependent cell death in NT4- and p75-deficient embryonic sensory neurons. Mol Cell Neurosci 16: 258-268 (2000).
    • (2000) Mol Cell Neurosci , vol.16 , pp. 258-268
    • Agerman, K.1    Baudet, C.2    Fundin, B.3    Willson, C.4    Ernfors, P.5
  • 49
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A and Dixit VM. Death receptors: signaling and modulation. Science 281: 1305-1308 (1998).
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 51
    • 0036463649 scopus 로고    scopus 로고
    • Apoptosis-based therapies
    • Reed JC. Apoptosis-based therapies. Nat Rev Drug Discov 1: 111-121 (2002).
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 111-121
    • Reed, J.C.1
  • 52
    • 0035368563 scopus 로고    scopus 로고
    • Apoptotic death sensor: An organelle's alter ego?
    • Bratton SB and Cohen GM. Apoptotic death sensor: an organelle's alter ego? Trends Pharmacol Sci 22: 306-315 (2001).
    • (2001) Trends Pharmacol Sci , vol.22 , pp. 306-315
    • Bratton, S.B.1    Cohen, G.M.2
  • 53
    • 0035003589 scopus 로고    scopus 로고
    • Cascade of Csp activation in potassium-deprived cerebellar granule neurons: Targets for treatment with peptide and protein inhibitors of apoptosis
    • Gerhardt E, Kugler S, Leist M, Beier C, Berliocchi L, Volbracht C, et al. Cascade of Csp activation in potassium-deprived cerebellar granule neurons: targets for treatment with peptide and protein inhibitors of apoptosis. Mol Cell Neurosci 17: 717-731 (2001).
    • (2001) Mol Cell Neurosci , vol.17 , pp. 717-731
    • Gerhardt, E.1    Kugler, S.2    Leist, M.3    Beier, C.4    Berliocchi, L.5    Volbracht, C.6
  • 55
    • 0033565587 scopus 로고    scopus 로고
    • Csp-8 and Csp-3 are expressed by different populations of cortical neurons undergoing delayed cell death after focal stroke in the rat
    • Velier JJ, Ellison JA, Kikly KK, Spera PA, Barone FC and Feuerstein GZ. Csp-8 and Csp-3 are expressed by different populations of cortical neurons undergoing delayed cell death after focal stroke in the rat. J Neurosci 19: 5932-5941 (1999).
    • (1999) J Neurosci , vol.19 , pp. 5932-5941
    • Velier, J.J.1    Ellison, J.A.2    Kikly, K.K.3    Spera, P.A.4    Barone, F.C.5    Feuerstein, G.Z.6
  • 56
    • 0034705057 scopus 로고    scopus 로고
    • Mitochondrial and extramitochondrial apoptotic signaling pathways in cerebrocortical neurons
    • Budd SL, Tenneti L, Lishnak T and Lipton SA. Mitochondrial and extramitochondrial apoptotic signaling pathways in cerebrocortical neurons. Proc Natl Acad Sci U S A 97: 6161-6166 (2000).
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6161-6166
    • Budd, S.L.1    Tenneti, L.2    Lishnak, T.3    Lipton, S.A.4
  • 57
    • 29144494879 scopus 로고    scopus 로고
    • Beyond apoptosis: Nonapoptotic cell death in physiology and disease
    • Hetz CA, Torres V and Quest AF. Beyond apoptosis: nonapoptotic cell death in physiology and disease. Biochem Cell Biol 83: 579-588 (2005).
    • (2005) Biochem Cell Biol , vol.83 , pp. 579-588
    • Hetz, C.A.1    Torres, V.2    Quest, A.F.3
  • 58
    • 22544444514 scopus 로고    scopus 로고
    • Csp-independent cell death
    • Kroemer G and Martin SJ. Csp-independent cell death. Nat Med 11: 725-730 (2005).
    • (2005) Nat Med , vol.11 , pp. 725-730
    • Kroemer, G.1    Martin, S.J.2
  • 59
    • 33645420460 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization: The sine qua non for cell death
    • Armstrong JS. Mitochondrial membrane permeabilization: the sine qua non for cell death. Bioessays 28: 253-260 (2006).
    • (2006) Bioessays , vol.28 , pp. 253-260
    • Armstrong, J.S.1
  • 60
    • 0037025256 scopus 로고    scopus 로고
    • Mitochondria, Ca2+ and neurodegenerative disease
    • Krieger C and Duchen MR. Mitochondria, Ca2+ and neurodegenerative disease. Eur J Pharmacol 447: 177-188 (2002).
    • (2002) Eur J Pharmacol , vol.447 , pp. 177-188
    • Krieger, C.1    Duchen, M.R.2
  • 61
    • 18744431459 scopus 로고    scopus 로고
    • Mitochondrial control of neuron death and its role in neurodegenerative disorders
    • Jordan J, Cena V and Prehn JH. Mitochondrial control of neuron death and its role in neurodegenerative disorders. J Physiol Biochem 59: 129-141 (2003).
    • (2003) J Physiol Biochem , vol.59 , pp. 129-141
    • Jordan, J.1    Cena, V.2    Prehn, J.H.3
  • 62
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM and Korsmeyer SJ. BCL-2 family members and the mitochondria in apoptosis. Genes Dev 13: 1899-1911 (1999).
    • (1999) Genes Dev , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 63
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G and Reed JC. Mitochondrial control of cell death. Nat Med 6: 513-519 (2000).
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 64
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H, Li Y, Liu X and Wang X. An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J Biol Chem 274: 11549-11556 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 65
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1
    • Qin H, Srinivasula SM, Wu G, Fernandes-Alnemri T, Alnemri ES and Shi Y. Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. Nature 399: 549-557 (1999).
    • (1999) Nature , vol.399 , pp. 549-557
    • Qin, H.1    Srinivasula, S.M.2    Wu, G.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5    Shi, Y.6
  • 66
    • 0033613143 scopus 로고    scopus 로고
    • Csp activation: The induced-proximity model
    • Salvesen GS and Dixit VM. Csp activation: the induced-proximity model. Proc Natl Acad Sci U S A 96: 10964-10967 (1999).
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 67
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature 407: 770-776 (2000).
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 68
    • 13544273998 scopus 로고    scopus 로고
    • Csp-dependent and -independent neuronal death: Two distinct pathways to neuronal injury
    • Stefanis L. Csp-dependent and -independent neuronal death: two distinct pathways to neuronal injury. Neuroscientist 11: 50-62 (2005).
    • (2005) Neuroscientist , vol.11 , pp. 50-62
    • Stefanis, L.1
  • 69
    • 32244433775 scopus 로고    scopus 로고
    • Regulation and interplay of apoptotic and non-apoptotic cell death
    • [64a] Kim R, Emi M, Tanabe K, Murakami S, Uchida Y and Arihiro K. Regulation and interplay of apoptotic and non-apoptotic cell death. J Pathol 208: 319-326 (2006).
    • (2006) J Pathol , vol.208 , pp. 319-326
    • Kim, R.1    Emi, M.2    Tanabe, K.3    Murakami, S.4    Uchida, Y.5    Arihiro, K.6
  • 70
    • 0035967169 scopus 로고    scopus 로고
    • Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death
    • Joza N, Susin SA, Daugas E, Stanford WL, Cho SK, Li CY, et al. Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature 410: 549-554 (2001).
    • (2001) Nature , vol.410 , pp. 549-554
    • Joza, N.1    Susin, S.A.2    Daugas, E.3    Stanford, W.L.4    Cho, S.K.5    Li, C.Y.6
  • 71
    • 12244298623 scopus 로고    scopus 로고
    • Implication of bax in apoptosis depends on microtubule network mobility
    • Longuet M, Serduc R and Riva C. Implication of bax in apoptosis depends on microtubule network mobility. Int J Oncol 25: 309-317 (2004).
    • (2004) Int J Oncol , vol.25 , pp. 309-317
    • Longuet, M.1    Serduc, R.2    Riva, C.3
  • 74
    • 0033593230 scopus 로고    scopus 로고
    • Bax-induced Csp activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL
    • Finucane DM, Bossy-Wetzel E, Waterhouse NJ, Cotter TG and Green DR. Bax-induced Csp activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL. J Biol Chem 274: 2225-2233 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 2225-2233
    • Finucane, D.M.1    Bossy-Wetzel, E.2    Waterhouse, N.J.3    Cotter, T.G.4    Green, D.R.5
  • 75
    • 0034790768 scopus 로고    scopus 로고
    • Molecular chaperone targeting and regulation by BAG family proteins
    • Takayama S and Reed JC. Molecular chaperone targeting and regulation by BAG family proteins. Nat Cell Biol 3: E237-241 (2001).
    • (2001) Nat Cell Biol , vol.3
    • Takayama, S.1    Reed, J.C.2
  • 77
    • 0141893377 scopus 로고    scopus 로고
    • Bifunctional apoptosis inhibitor (BAR) protects neurons from diverse cell death pathways
    • Roth W, Kermer P, Krajewska M, Welsh K, Davis S, Krajewski S, et al. Bifunctional apoptosis inhibitor (BAR) protects neurons from diverse cell death pathways. Cell Death Differ 10: 1178-1187 (2003).
    • (2003) Cell Death Differ , vol.10 , pp. 1178-1187
    • Roth, W.1    Kermer, P.2    Krajewska, M.3    Welsh, K.4    Davis, S.5    Krajewski, S.6
  • 78
    • 0033062724 scopus 로고    scopus 로고
    • Apoptosis in neuronal development and transplantation: Role of caspases and trophic factors
    • Boonman Z and Isacson O. Apoptosis in neuronal development and transplantation: role of caspases and trophic factors. Exp Neurol 156: 1-15 (1999).
    • (1999) Exp Neurol , vol.156 , pp. 1-15
    • Boonman, Z.1    Isacson, O.2
  • 79
    • 24944535336 scopus 로고    scopus 로고
    • Proteasome inhibition elicits a biphasic effect on neuronal apoptosis via differential regulation of pro-survival and proapoptotic transcription factors
    • [73a] Butts BD, Hudson HR, Linseman DA, Le SS, Ryan KR, Bouchard RJ, et al. Proteasome inhibition elicits a biphasic effect on neuronal apoptosis via differential regulation of pro-survival and proapoptotic transcription factors. Mol Cell Neurosci 30: 279-289 (2005).
    • (2005) Mol Cell Neurosci , vol.30 , pp. 279-289
    • Butts, B.D.1    Hudson, H.R.2    Linseman, D.A.3    Le, S.S.4    Ryan, K.R.5    Bouchard, R.J.6
  • 80
    • 0033384476 scopus 로고    scopus 로고
    • Par-4: An emerging pivotal player in neuronal apoptosis and neurodegenerative disorders
    • Mattson MP, Duan W, Chan SL and Camandola S. Par-4: an emerging pivotal player in neuronal apoptosis and neurodegenerative disorders. J Mol Neurosci 13: 17-30 (1999).
    • (1999) J Mol Neurosci , vol.13 , pp. 17-30
    • Mattson, M.P.1    Duan, W.2    Chan, S.L.3    Camandola, S.4
  • 82
    • 21844470751 scopus 로고    scopus 로고
    • Adult motor neuron apoptosis is mediated by nitric oxide and Fas death receptor linked by DNA damage and p53 activation
    • Martin LJ, Chen K and Liu Z. Adult motor neuron apoptosis is mediated by nitric oxide and Fas death receptor linked by DNA damage and p53 activation. J Neurosci 25: 6449-6459 (2005).
    • (2005) J Neurosci , vol.25 , pp. 6449-6459
    • Martin, L.J.1    Chen, K.2    Liu, Z.3
  • 84
    • 33645014708 scopus 로고    scopus 로고
    • p53, Apaf-1, Csp-3, and -9 are dispensable for Cdk5 activation during cell death
    • Lin L, Ye Y and Zakeri Z. p53, Apaf-1, Csp-3, and -9 are dispensable for Cdk5 activation during cell death. Cell Death Differ: 13: 141-150 (2005).
    • (2005) Cell Death Differ , vol.13 , pp. 141-150
    • Lin, L.1    Ye, Y.2    Zakeri, Z.3
  • 85
    • 27844495164 scopus 로고    scopus 로고
    • Molecular basis of programmed cell death involved in neurodegeneration
    • [78a] Krantic S, Mechawar N, Reix S and Quirion R. Molecular basis of programmed cell death involved in neurodegeneration. Trends Neurosci 28: 670-676 (2005).
    • (2005) Trends Neurosci , vol.28 , pp. 670-676
    • Krantic, S.1    Mechawar, N.2    Reix, S.3    Quirion, R.4
  • 86
  • 87
    • 0035809792 scopus 로고    scopus 로고
    • Hippocampal neurons of mice deficient in DNA-dependent protein kinase exhibit increased vulnerability to DNA damage, oxidative stress and excitotoxicity
    • Culmsee C, Bondada S and Mattson MP. Hippocampal neurons of mice deficient in DNA-dependent protein kinase exhibit increased vulnerability to DNA damage, oxidative stress and excitotoxicity. Brain Res Mol Brain Res 87: 257-262 (2001).
    • (2001) Brain Res Mol Brain Res , vol.87 , pp. 257-262
    • Culmsee, C.1    Bondada, S.2    Mattson, M.P.3
  • 88
    • 0034160047 scopus 로고    scopus 로고
    • Cell birth, cell death, cell diversity and DNA breaks: How do they all fit together?
    • Gilmore EC, Nowakowski RS, Caviness VS, Jr. and Herrup K. Cell birth, cell death, cell diversity and DNA breaks: how do they all fit together? Trends Neurosci 23: 100-105 (2000).
    • (2000) Trends Neurosci , vol.23 , pp. 100-105
    • Gilmore, E.C.1    Nowakowski, R.S.2    Caviness Jr., V.S.3    Herrup, K.4
  • 89
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent Csp activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L and Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent Csp activation by eliminating IAP inhibition. Cell 102: 33-42 (2000).
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 90
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of Csp-3-like proteases
    • Jaattela M, Wissing D, Kokholm K, Kallunki T and Egeblad M. Hsp70 exerts its anti-apoptotic function downstream of Csp-3-like proteases. Embo J 17: 6124-6134 (1998).
    • (1998) Embo J , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 92
    • 0033830186 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 in the nervous system
    • Ha HC and Snyder SH. Poly(ADP-ribose) polymerase-1 in the nervous system. Neurobiol Dis 7: 225-239 (2000).
    • (2000) Neurobiol Dis , vol.7 , pp. 225-239
    • Ha, H.C.1    Snyder, S.H.2
  • 93
    • 0141816712 scopus 로고    scopus 로고
    • Involvement of poly ADP ribosyl polymerase-1 in acute but not chronic zinc toxicity
    • Sheline CT, Wang H, Cai AL, Dawson VL and Choi DW. Involvement of poly ADP ribosyl polymerase-1 in acute but not chronic zinc toxicity. Eur J Neurosci 18: 1402-1409 (2003).
    • (2003) Eur J Neurosci , vol.18 , pp. 1402-1409
    • Sheline, C.T.1    Wang, H.2    Cai, A.L.3    Dawson, V.L.4    Choi, D.W.5
  • 94
    • 0031149046 scopus 로고    scopus 로고
    • The c-Jun transcription factor - Bipotential mediator of neuronal death, survival and regeneration
    • Herdegen T, Skene P and Bahr M. The c-Jun transcription factor - bipotential mediator of neuronal death, survival and regeneration. Trends Neurosci 20: 227-231 (1997).
    • (1997) Trends Neurosci , vol.20 , pp. 227-231
    • Herdegen, T.1    Skene, P.2    Bahr, M.3
  • 95
    • 0030751604 scopus 로고    scopus 로고
    • Kainic acid-induced excitotoxicity is associated with a complex c-Fos and c-Jun response which does not preclude either cell death or survival
    • Pozas E, Ballabriga J, Planas AM and Ferrer I. Kainic acid-induced excitotoxicity is associated with a complex c-Fos and c-Jun response which does not preclude either cell death or survival. J Neurobiol 33: 232-246 (1997).
    • (1997) J Neurobiol , vol.33 , pp. 232-246
    • Pozas, E.1    Ballabriga, J.2    Planas, A.M.3    Ferrer, I.4
  • 97
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson MP. Apoptosis in neurodegenerative disorders. Nat Rev Mol Cell Biol 1: 120-129 (2000).
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 98
    • 4444277253 scopus 로고    scopus 로고
    • Oxidative stress-induced death in the nervous system: Cell cycle dependent or independent?
    • [90a] Langley B and Ratan RR. Oxidative stress-induced death in the nervous system: cell cycle dependent or independent? J Neurosci Res 77: 621-629 (2004).
    • (2004) J Neurosci Res , vol.77 , pp. 621-629
    • Langley, B.1    Ratan, R.R.2
  • 100
    • 0034123691 scopus 로고    scopus 로고
    • Mechanisms of neurodegenerative disorders: Part 1: protein aggregates
    • Wolozin B and Behl C. Mechanisms of neurodegenerative disorders: Part 1: protein aggregates. Arch Neurol 57: 793-796 (2000).
    • (2000) Arch Neurol , vol.57 , pp. 793-796
    • Wolozin, B.1    Behl, C.2
  • 101
    • 85046909683 scopus 로고    scopus 로고
    • Cell death mechanisms in neurodegeneration
    • Jellinger KA. Cell death mechanisms in neurodegeneration. J Cell Mol Med 5: 1-17 (2001).
    • (2001) J Cell Mol Med , vol.5 , pp. 1-17
    • Jellinger, K.A.1
  • 104
    • 0042886045 scopus 로고    scopus 로고
    • Cell cycle aberrations by alpha-synuclein over-expression and cyclin B immunoreactivity in Lewy bodies
    • Lee SS, Kim YM, Junn E, Lee G, Park KH, Tanaka M, et al. Cell cycle aberrations by alpha-synuclein over-expression and cyclin B immunoreactivity in Lewy bodies. Neurobiol Aging 24: 687-696 (2003).
    • (2003) Neurobiol Aging , vol.24 , pp. 687-696
    • Lee, S.S.1    Kim, Y.M.2    Junn, E.3    Lee, G.4    Park, K.H.5    Tanaka, M.6
  • 105
    • 0034489853 scopus 로고    scopus 로고
    • Alpha-synuclein and Parkinson's disease
    • Lucking CB and Brice A. Alpha-synuclein and Parkinson's disease. Cell Mol Life Sci 57: 1894-1908 (2000).
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1894-1908
    • Lucking, C.B.1    Brice, A.2
  • 106
    • 31444449462 scopus 로고    scopus 로고
    • Role of the unfolded protein response in cell death
    • [96a] Kim R, Emi M, Tanabe K and Murakami S. Role of the unfolded protein response in cell death. Apoptosis 11: 5-13 (2006).
    • (2006) Apoptosis , vol.11 , pp. 5-13
    • Kim, R.1    Emi, M.2    Tanabe, K.3    Murakami, S.4
  • 107
    • 28244442462 scopus 로고    scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in human disease
    • [96b] Fadeel B and Orrenius S. Apoptosis: a basic biological phenomenon with wide-ranging implications in human disease. J Intern Med 258: 479-517 (2005).
    • (2005) J Intern Med , vol.258 , pp. 479-517
    • Fadeel, B.1    Orrenius, S.2
  • 108
    • 22144491587 scopus 로고    scopus 로고
    • Apoptosis in amyotrophic lateral sclerosis - What is the evidence?
    • Sathasivam S and Shaw PJ. Apoptosis in amyotrophic lateral sclerosis - what is the evidence? Lancet Neurol 4: 500-509 (2005).
    • (2005) Lancet Neurol , vol.4 , pp. 500-509
    • Sathasivam, S.1    Shaw, P.J.2
  • 110
    • 0345856174 scopus 로고    scopus 로고
    • Aging and dementia
    • (Eds Graham DI, Lantos PL). E. Arnold, London
    • Mirra SS and Hyman BT. Aging and dementia. In 'Greenfield's Neuropathology, 7th Ed.' (Eds Graham DI, Lantos PL). E. Arnold, London, pp. 195-271 (2002).
    • (2002) Greenfield's Neuropathology, 7th Ed. , pp. 195-271
    • Mirra, S.S.1    Hyman, B.T.2
  • 111
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Berl
    • Braak H and Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol (Berl) 82: 239-259. (1991).
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 112
    • 5644231977 scopus 로고    scopus 로고
    • Neuropathologic criteria for diagnosing Alzheimer disease in persons with pure dementia of Alzheimer type
    • McKeel DW, Price JL, Miller JP, Grant EA, Xiong C, Berg L, et al. Neuropathologic criteria for diagnosing Alzheimer disease in persons with pure dementia of Alzheimer type. J Neuropathol Exp Neurol 63: 1028-1037 (2004).
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 1028-1037
    • McKeel, D.W.1    Price, J.L.2    Miller, J.P.3    Grant, E.A.4    Xiong, C.5    Berg, L.6
  • 114
    • 33645805187 scopus 로고    scopus 로고
    • Alzheimer's disease
    • (Eds Esiri M, Lee VMY, Trojanowski JQ). Cambridge University Press, Cambridge
    • Morris JH and Nagy Z. Alzheimer's disease. In 'The Neuropathology of Dementia' (Eds Esiri M, Lee VMY, Trojanowski JQ). Cambridge University Press, Cambridge, pp. 161-206 (2004).
    • (2004) The Neuropathology of Dementia , pp. 161-206
    • Morris, J.H.1    Nagy, Z.2
  • 117
    • 0037072278 scopus 로고    scopus 로고
    • Nonoverlapping but synergetic tau and APP pathologies in sporadic Alzheimer's disease
    • Delacourte A, Sergeant N, Champain D, Wattez A, Maurage CA, Lebert F, et al. Nonoverlapping but synergetic tau and APP pathologies in sporadic Alzheimer's disease. Neurology 59: 398-407. (2002).
    • (2002) Neurology , vol.59 , pp. 398-407
    • Delacourte, A.1    Sergeant, N.2    Champain, D.3    Wattez, A.4    Maurage, C.A.5    Lebert, F.6
  • 118
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J and Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356 (2002).
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 119
    • 3042576053 scopus 로고    scopus 로고
    • The Amyloid Hypothesis and the clearance and degradation of Alzheimer's beta-peptide
    • LeVine H, 3rd. The Amyloid Hypothesis and the clearance and degradation of Alzheimer's beta-peptide. J Alzheimers Dis 6: 303-314 (2004).
    • (2004) J Alzheimers Dis , vol.6 , pp. 303-314
    • LeVine III, H.1
  • 120
    • 0141960033 scopus 로고    scopus 로고
    • Beta-Amyloid induces paired helical filament-like tau filaments in tissue culture
    • Ferrari A, Hoerndli F, Baechi T, Nitsch RM and Gotz J. beta-Amyloid induces paired helical filament-like tau filaments in tissue culture. J Biol Chem 278: 40162-40168 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 40162-40168
    • Ferrari, A.1    Hoerndli, F.2    Baechi, T.3    Nitsch, R.M.4    Gotz, J.5
  • 123
    • 4344669435 scopus 로고    scopus 로고
    • Cell degeneration induced by amyloid-beta peptides: Implications for Alzheimer's disease
    • Pereira C, Ferreiro E, Cardoso SM and de Oliveira CR. Cell degeneration induced by amyloid-beta peptides: implications for Alzheimer's disease. J Mol Neurosci 23: 97-104 (2004).
    • (2004) J Mol Neurosci , vol.23 , pp. 97-104
    • Pereira, C.1    Ferreiro, E.2    Cardoso, S.M.3    De Oliveira, C.R.4
  • 124
    • 21544459062 scopus 로고    scopus 로고
    • The role of calcineurin in amyloid-beta-peptides-mediated cell death
    • Cardoso SM and Oliveira CR. The role of calcineurin in amyloid-beta-peptides-mediated cell death. Brain Res 1050: 1-7 (2005).
    • (2005) Brain Res , vol.1050 , pp. 1-7
    • Cardoso, S.M.1    Oliveira, C.R.2
  • 125
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation
    • Gervais FG, Xu D, Robertson GS, Vaillancourt JP, Zhu Y, Huang J, et al. Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation. Cell 97: 395-406 (1999).
    • (1999) Cell , vol.97 , pp. 395-406
    • Gervais, F.G.1    Xu, D.2    Robertson, G.S.3    Vaillancourt, J.P.4    Zhu, Y.5    Huang, J.6
  • 127
    • 0036869740 scopus 로고    scopus 로고
    • Csp Activation in the Alzheimer's Disease Brain: Tortuous and Torturous
    • Rohn TT, Rissman RA, Head E and Cotman CW. Csp Activation in the Alzheimer's Disease Brain: Tortuous and Torturous. Drug News Perspect 15: 549-557 (2002).
    • (2002) Drug News Perspect , vol.15 , pp. 549-557
    • Rohn, T.T.1    Rissman, R.A.2    Head, E.3    Cotman, C.W.4
  • 130
    • 3242811902 scopus 로고    scopus 로고
    • Active Csp-6 and Csp-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • Guo H, Albrecht S, Bourdeau M, Petzke T, Bergeron C and Le-Blanc AC. Active Csp-6 and Csp-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am J Pathol 165: 523-531 (2004).
    • (2004) Am J Pathol , vol.165 , pp. 523-531
    • Guo, H.1    Albrecht, S.2    Bourdeau, M.3    Petzke, T.4    Bergeron, C.5    Le-Blanc, A.C.6
  • 131
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S, Billings L, Kesslak JP, Cribbs DH and LaFerla FM. Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43: 321-332 (2004).
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 133
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J, Chen F, van Dorpe J and Nitsch RM. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science 293: 1491-1495 (2001).
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 134
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • Oddo S, Caccamo A, Kitazawa M, Tseng BP and LaFerla FM. Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol Aging 24: 1063-1070 (2003).
    • (2003) Neurobiol Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 135
    • 25844458239 scopus 로고    scopus 로고
    • Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies
    • Ferrer I, Gomez-Isla T, Puig B, Freixes M, Ribé E, Dalfó E, et al. Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies. Curr Alzheimer Res 2: 3-18 (2005).
    • (2005) Curr Alzheimer Res , vol.2 , pp. 3-18
    • Ferrer, I.1    Gomez-Isla, T.2    Puig, B.3    Freixes, M.4    Ribé, E.5    Dalfó, E.6
  • 136
    • 0942265972 scopus 로고    scopus 로고
    • Amyloid-beta-induced toxicity of primary neurons is dependent upon differentiation-associated increases in tau and cyclin-dependent kinase 5 expression
    • Liu T, Perry G, Chan HW, Verdile G, Martins RN, Smith MA, et al. Amyloid-beta-induced toxicity of primary neurons is dependent upon differentiation-associated increases in tau and cyclin-dependent kinase 5 expression. J Neurochem 88: 554-563 (2004).
    • (2004) J Neurochem , vol.88 , pp. 554-563
    • Liu, T.1    Perry, G.2    Chan, H.W.3    Verdile, G.4    Martins, R.N.5    Smith, M.A.6
  • 137
    • 0042679510 scopus 로고    scopus 로고
    • Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice
    • Kins S, Kurosinski P, Nitsch RM and Gotz J. Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice. Am J Pathol 163: 833-843 (2003).
    • (2003) Am J Pathol , vol.163 , pp. 833-843
    • Kins, S.1    Kurosinski, P.2    Nitsch, R.M.3    Gotz, J.4
  • 139
    • 0035659377 scopus 로고    scopus 로고
    • Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies
    • Ferrer I, Blanco R, Carmona M and Puig B. Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress-activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies. J Neural Transm 108: 1397-1415 (2001).
    • (2001) J Neural Transm , vol.108 , pp. 1397-1415
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Puig, B.4
  • 140
    • 0035094403 scopus 로고    scopus 로고
    • Phosphorylated map kinase (ERK1, ERK2) expression is associated with early tau deposition in neurones and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration
    • Ferrer I, Blanco R, Carmona M, Ribera R, Goutan E, Puig B, et al. Phosphorylated map kinase (ERK1, ERK2) expression is associated with early tau deposition in neurones and glial cells, but not with increased nuclear DNA vulnerability and cell death, in Alzheimer disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration. Brain Pathol 11: 144-158 (2001).
    • (2001) Brain Pathol , vol.11 , pp. 144-158
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Ribera, R.4    Goutan, E.5    Puig, B.6
  • 141
    • 0033928035 scopus 로고    scopus 로고
    • The neuronal microtubule-associated protein tau is a substrate for Csp-3 and an effector of apoptosis
    • Fasulo L, Ugolini G, Visintin M, Bradbury A, Brancolini C, Verzillo V, et al. The neuronal microtubule-associated protein tau is a substrate for Csp-3 and an effector of apoptosis. J Neurochem 75: 624-633 (2000).
    • (2000) J Neurochem , vol.75 , pp. 624-633
    • Fasulo, L.1    Ugolini, G.2    Visintin, M.3    Bradbury, A.4    Brancolini, C.5    Verzillo, V.6
  • 143
    • 0037445602 scopus 로고    scopus 로고
    • Association of phosphorylation site of tau protein with neuronal apoptosis in Alzheimer's disease
    • Kobayashi K, Nakano H, Hayashi M, Shimazaki M, Fukutani Y, Sasaki K, et al. Association of phosphorylation site of tau protein with neuronal apoptosis in Alzheimer's disease. J Neurol Sci 208: 17-24 (2003).
    • (2003) J Neurol Sci , vol.208 , pp. 17-24
    • Kobayashi, K.1    Nakano, H.2    Hayashi, M.3    Shimazaki, M.4    Fukutani, Y.5    Sasaki, K.6
  • 144
    • 14744300176 scopus 로고    scopus 로고
    • Csp-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: An implication to Alzheimer's disease
    • Kang HJ, Yoon WJ, Moon GJ, Kim DY, Sohn S, Kwon HJ, et al. Csp-3-mediated cleavage of PHF-1 tau during apoptosis irrespective of excitotoxicity and oxidative stress: an implication to Alzheimer's disease. Neurobiol Dis 18: 450-458 (2005).
    • (2005) Neurobiol Dis , vol.18 , pp. 450-458
    • Kang, H.J.1    Yoon, W.J.2    Moon, G.J.3    Kim, D.Y.4    Sohn, S.5    Kwon, H.J.6
  • 145
    • 0031760611 scopus 로고    scopus 로고
    • Csp dependent DNA fragmentation might be associated with excitotoxicity in Alzheimer disease
    • Masliah E, Mallory M, Alford M, Tanaka S and Hansen LA. Csp dependent DNA fragmentation might be associated with excitotoxicity in Alzheimer disease. J Neuropathol Exp Neurol 57: 1041-1052 (1998).
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 1041-1052
    • Masliah, E.1    Mallory, M.2    Alford, M.3    Tanaka, S.4    Hansen, L.A.5
  • 146
    • 0042837889 scopus 로고    scopus 로고
    • Csp activation in the limbic cortex of subjects with early Alzheimer's disease
    • Gastard MC, Troncoso JC and Koliatsos VE. Csp activation in the limbic cortex of subjects with early Alzheimer's disease. Ann Neurol 54: 393-398 (2003).
    • (2003) Ann Neurol , vol.54 , pp. 393-398
    • Gastard, M.C.1    Troncoso, J.C.2    Koliatsos, V.E.3
  • 147
    • 0037336851 scopus 로고    scopus 로고
    • Csp gene expression in the brain as a function of the clinical progression of Alzheimer disease
    • Pompl PN, Yemul S, Xiang Z, Ho L, Haroutunian V, Purohit D, et al. Csp gene expression in the brain as a function of the clinical progression of Alzheimer disease. Arch Neurol 60: 369-376 (2003).
    • (2003) Arch Neurol , vol.60 , pp. 369-376
    • Pompl, P.N.1    Yemul, S.2    Xiang, Z.3    Ho, L.4    Haroutunian, V.5    Purohit, D.6
  • 149
    • 11144227267 scopus 로고    scopus 로고
    • Linking alterations in tau phosphorylation and cleavage during neuronal apoptosis
    • Rametti A, Esclaire F, Yardin C and Terro F. Linking alterations in tau phosphorylation and cleavage during neuronal apoptosis. J Biol Chem 279: 54518-54528 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 54518-54528
    • Rametti, A.1    Esclaire, F.2    Yardin, C.3    Terro, F.4
  • 150
    • 85047693458 scopus 로고    scopus 로고
    • Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: Cause or effect?
    • Dickson DW. Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: cause or effect? J Clin Invest 114: 23-27 (2004).
    • (2004) J Clin Invest , vol.114 , pp. 23-27
    • Dickson, D.W.1
  • 152
    • 0030805991 scopus 로고    scopus 로고
    • Frequency of stages of Alzheimer-related lesions in different age categories
    • Braak H and Braak E. Frequency of stages of Alzheimer-related lesions in different age categories. Neurobiol Aging 18: 351-357 (1997).
    • (1997) Neurobiol Aging , vol.18 , pp. 351-357
    • Braak, H.1    Braak, E.2
  • 153
    • 0030823304 scopus 로고    scopus 로고
    • Prevalence, incidence and duration of Braak's stages in the general population: Can we know?
    • Duyckaerts C and Hauw JJ. Prevalence, incidence and duration of Braak's stages in the general population: can we know? Neurobiol Aging 18: 362-369; discussion 389-392 (1997).
    • (1997) Neurobiol Aging , vol.18 , pp. 362-369
    • Duyckaerts, C.1    Hauw, J.J.2
  • 154
    • 3142516228 scopus 로고    scopus 로고
    • Microtubule-dependent transport in neurons: Steps towards an understanding of regulation, function and dysfunction
    • Guzik BW and Goldstein LS. Microtubule-dependent transport in neurons: steps towards an understanding of regulation, function and dysfunction. Curr Opin Cell Biol 16: 443-450 (2004).
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 443-450
    • Guzik, B.W.1    Goldstein, L.S.2
  • 155
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow EM, Stamer K, Vogel R, Thies E and Mandelkow E. Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol Aging 24: 1079-1085 (2003).
    • (2003) Neurobiol Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 156
    • 14244261725 scopus 로고    scopus 로고
    • Axonal transport defects: A common theme in neurodegenerative diseases
    • Berl
    • Roy S, Zhang B, Lee VM and Trojanowski JQ. Axonal transport defects: a common theme in neurodegenerative diseases. Acta Neuropathol (Berl) 109: 5-13 (2005).
    • (2005) Acta Neuropathol , vol.109 , pp. 5-13
    • Roy, S.1    Zhang, B.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 157
    • 20044385920 scopus 로고    scopus 로고
    • Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease
    • Stokin GB, Lillo C, Falzone TL, Brusch RG, Rockenstein E, Mount SL, et al. Axonopathy and transport deficits early in the pathogenesis of Alzheimer's disease. Science 307: 1282-1288 (2005).
    • (2005) Science , vol.307 , pp. 1282-1288
    • Stokin, G.B.1    Lillo, C.2    Falzone, T.L.3    Brusch, R.G.4    Rockenstein, E.5    Mount, S.L.6
  • 158
    • 33645461302 scopus 로고    scopus 로고
    • NF-kappaB pathway: A target for preventing beta-amyloid (Abeta)-induced neuronal damage and Abeta42 production
    • [146a] Valerio A, Boroni F, Benarese M, Sarnico I, Ghisi V, Bresciani LG, et al. NF-kappaB pathway: a target for preventing beta-amyloid (Abeta)-induced neuronal damage and Abeta42 production. Eur J Neurosci 23: 1711-1720 (2006).
    • (2006) Eur J Neurosci , vol.23 , pp. 1711-1720
    • Valerio, A.1    Boroni, F.2    Benarese, M.3    Sarnico, I.4    Ghisi, V.5    Bresciani, L.G.6
  • 159
    • 25844458981 scopus 로고    scopus 로고
    • Protein aggregation in Alzheimer's disease and other neuropathological disorders
    • Dimakopoulos AC. Protein aggregation in Alzheimer's disease and other neuropathological disorders. Curr Alzheimer Res 2: 19-28 (2005).
    • (2005) Curr Alzheimer Res , vol.2 , pp. 19-28
    • Dimakopoulos, A.C.1
  • 160
    • 0346025493 scopus 로고    scopus 로고
    • Functional neurochemistry of Alzheimer's disease
    • Gsell W, Jungkunz G and Riederer P. Functional neurochemistry of Alzheimer's disease. Curr Pharm Design 9: 265-293 (2003).
    • (2003) Curr Pharm Design , vol.9 , pp. 265-293
    • Gsell, W.1    Jungkunz, G.2    Riederer, P.3
  • 162
    • 0037172826 scopus 로고    scopus 로고
    • Phases of a beta-deposition in the human brain and its relevance for the development of AD
    • Thal DR, Rub U, Orantes M and Braak H. Phases of A beta-deposition in the human brain and its relevance for the development of AD. Neurology 58: 1791-1800 (2002).
    • (2002) Neurology , vol.58 , pp. 1791-1800
    • Thal, D.R.1    Rub, U.2    Orantes, M.3    Braak, H.4
  • 163
    • 21144433508 scopus 로고    scopus 로고
    • Association of cyclin-dependent kinase 5 and neuronal activators p35 and p39 complex in early-onset Alzheimer's disease
    • Rademakers R, Sleegers K, Theuns J, Van den Broeck M, Bel Kacem S, Nilsson LG, et al. Association of cyclin-dependent kinase 5 and neuronal activators p35 and p39 complex in early-onset Alzheimer's disease. Neurobiol Aging 26: 1145-1151 (2005).
    • (2005) Neurobiol Aging , vol.26 , pp. 1145-1151
    • Rademakers, R.1    Sleegers, K.2    Theuns, J.3    Van Den Broeck, M.4    Bel Kacem, S.5    Nilsson, L.G.6
  • 164
    • 0035933279 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice
    • Wirths O, Multhaup G, Czech C, Blanchard V, Moussaoui S, Tremp G, et al. Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 double-transgenic mice. Neurosci Lett 306: 116-120 (2001).
    • (2001) Neurosci Lett , vol.306 , pp. 116-120
    • Wirths, O.1    Multhaup, G.2    Czech, C.3    Blanchard, V.4    Moussaoui, S.5    Tremp, G.6
  • 165
    • 0035019371 scopus 로고    scopus 로고
    • CEP-1347/KT-7515, an inhibitor of SAPK/JNK pathway activation, promotes survival and blocks multiple events associated with Abeta-induced cortical neuron apoptosis
    • Bozyczko-Coyne D, O'Kane TM, Wu ZL, Dobrzanski P, Murthy S, Vaught JL, et al. CEP-1347/KT-7515, an inhibitor of SAPK/JNK pathway activation, promotes survival and blocks multiple events associated with Abeta-induced cortical neuron apoptosis. J Neurochem 77: 849-863 (2001).
    • (2001) J Neurochem , vol.77 , pp. 849-863
    • Bozyczko-Coyne, D.1    O'Kane, T.M.2    Wu, Z.L.3    Dobrzanski, P.4    Murthy, S.5    Vaught, J.L.6
  • 166
    • 0038584865 scopus 로고    scopus 로고
    • A role for c-Jun N-terminal kinase 1 (JNK1), but not JNK2, in the beta-amyloid-mediated stabilization of protein p53 and induction of the apoptotic cascade in cultured cortical neurons
    • Fogarty MP, Downer EJ and Campbell V. A role for c-Jun N-terminal kinase 1 (JNK1), but not JNK2, in the beta-amyloid-mediated stabilization of protein p53 and induction of the apoptotic cascade in cultured cortical neurons. Biochem J 371: 789-798 (2003).
    • (2003) Biochem J , vol.371 , pp. 789-798
    • Fogarty, M.P.1    Downer, E.J.2    Campbell, V.3
  • 167
    • 0036959437 scopus 로고    scopus 로고
    • beta-Amyloid induces oxidative DNA damage and cell death through activation of c-Jun N terminal kinase
    • Jang JH and Surh YJ. beta-Amyloid induces oxidative DNA damage and cell death through activation of c-Jun N terminal kinase. Ann N Y Acad Sci 973: 228-236 (2002).
    • (2002) Ann N Y Acad Sci , vol.973 , pp. 228-236
    • Jang, J.H.1    Surh, Y.J.2
  • 168
    • 0037382957 scopus 로고    scopus 로고
    • H2O2 and 4-hydroxynonenal mediate amyloid beta-induced neuronal apoptosis by activating JNKs and p38MAPK
    • Tamagno E, Robino G, Obbili A, Bardini P, Aragno M, Parola M, et al. H2O2 and 4-hydroxynonenal mediate amyloid beta-induced neuronal apoptosis by activating JNKs and p38MAPK. Exp Neurol 180: 144-155 (2003).
    • (2003) Exp Neurol , vol.180 , pp. 144-155
    • Tamagno, E.1    Robino, G.2    Obbili, A.3    Bardini, P.4    Aragno, M.5    Parola, M.6
  • 170
    • 0036707528 scopus 로고    scopus 로고
    • Abeta 17-42 in Alzheimer's disease activates JNK and Csp-8 leading to neuronal apoptosis
    • Wei W, Norton DD, Wang X and Kusiak JW. Abeta 17-42 in Alzheimer's disease activates JNK and Csp-8 leading to neuronal apoptosis. Brain 125: 2036-2043 (2002).
    • (2002) Brain , vol.125 , pp. 2036-2043
    • Wei, W.1    Norton, D.D.2    Wang, X.3    Kusiak, J.W.4
  • 171
    • 0035215568 scopus 로고    scopus 로고
    • The role of the MAP-kinase superfamily in beta-amyloid toxicity
    • Daniels WM, Hendricks J, Salie R and Taljaard JJ. The role of the MAP-kinase superfamily in beta-amyloid toxicity. Metab Brain Dis 16: 175-185 (2001).
    • (2001) Metab Brain Dis , vol.16 , pp. 175-185
    • Daniels, W.M.1    Hendricks, J.2    Salie, R.3    Taljaard, J.J.4
  • 172
    • 0035478618 scopus 로고    scopus 로고
    • Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand
    • Morishima Y, Gotoh Y, Zieg J, Barrett T, Takano H, Flavell R, et al. Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand. J Neurosci 21: 7551-7560 (2001).
    • (2001) J Neurosci , vol.21 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    Barrett, T.4    Takano, H.5    Flavell, R.6
  • 174
    • 0142139355 scopus 로고    scopus 로고
    • Oxidative stress and neuronal adaptation in Alzheimer disease: The role of SAPK pathways
    • Zhu X, Raina AK, Lee HG, Chao M, Nunomura A, Tabaton M, et al. Oxidative stress and neuronal adaptation in Alzheimer disease: the role of SAPK pathways. Antioxid Redox Signal 5: 571-576 (2003).
    • (2003) Antioxid Redox Signal , vol.5 , pp. 571-576
    • Zhu, X.1    Raina, A.K.2    Lee, H.G.3    Chao, M.4    Nunomura, A.5    Tabaton, M.6
  • 175
    • 0642375800 scopus 로고    scopus 로고
    • Neurofibrillary degeneration of the Alzheimer-type: An alternate pathway to neuronal apoptosis?
    • Hamdane M, Delobel P, Sambo AV, Smet C, Begard S, Violleau A, et al. Neurofibrillary degeneration of the Alzheimer-type: an alternate pathway to neuronal apoptosis? Biochem Pharmacol 66: 1619-1625 (2003).
    • (2003) Biochem Pharmacol , vol.66 , pp. 1619-1625
    • Hamdane, M.1    Delobel, P.2    Sambo, A.V.3    Smet, C.4    Begard, S.5    Violleau, A.6
  • 177
    • 0030806869 scopus 로고    scopus 로고
    • DNA damage distribution in the human brain as shown by in situ end labeling; area-specific differences in aging and Alzheimer disease in the absence of apoptotic morphology
    • Lucassen PJ, Chung WC, Kamphorst W and Swaab DF. DNA damage distribution in the human brain as shown by in situ end labeling; area-specific differences in aging and Alzheimer disease in the absence of apoptotic morphology. J Neuropathol Exp Neurol 56: 887-900 (1997).
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 887-900
    • Lucassen, P.J.1    Chung, W.C.2    Kamphorst, W.3    Swaab, D.F.4
  • 178
    • 0031009367 scopus 로고    scopus 로고
    • Topographic associations between DNA fragmentation and Alzheimer's disease neuropathology in the hippocampus
    • Sugaya K, Reeves M and McKinney M. Topographic associations between DNA fragmentation and Alzheimer's disease neuropathology in the hippocampus. Neurochem Int 31: 275-281 (1997).
    • (1997) Neurochem Int , vol.31 , pp. 275-281
    • Sugaya, K.1    Reeves, M.2    McKinney, M.3
  • 179
    • 0029852587 scopus 로고    scopus 로고
    • In situ labeling of dying cortical neurons in normal aging and in Alzheimer's disease: Correlations with senile plaques and disease progression
    • Troncoso JC, Sukhov RR, Kawas CH and Koliatsos VE. In situ labeling of dying cortical neurons in normal aging and in Alzheimer's disease: correlations with senile plaques and disease progression. J Neuropathol Exp Neurol 55: 1134-1142 (1996).
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1134-1142
    • Troncoso, J.C.1    Sukhov, R.R.2    Ch, K.3    Koliatsos, V.E.4
  • 180
    • 33646489799 scopus 로고    scopus 로고
    • No difference in expression of apoptosis-related proteins and apoptotic morphology in controls, pathologically aged and Alzheimer's disease cases
    • Woodhouse A, Dickson TC, West AK, McLean CA and Vickers JC. No difference in expression of apoptosis-related proteins and apoptotic morphology in controls, pathologically aged and Alzheimer's disease cases. Neurobiol Dis 22: 323-333 (2005).
    • (2005) Neurobiol Dis , vol.22 , pp. 323-333
    • Woodhouse, A.1    Dickson, T.C.2    West, A.K.3    McLean, C.A.4    Vickers, J.C.5
  • 181
    • 0036934466 scopus 로고    scopus 로고
    • Csp-cleaved amyloid precursor protein and activated Csp-3 are co-localized in the granules of granulovacuolar degeneration in Alzheimer's disease and Down's syndrome brain
    • Berl
    • Su JH, Kesslak JP, Head E and Cotman CW. Csp-cleaved amyloid precursor protein and activated Csp-3 are co-localized in the granules of granulovacuolar degeneration in Alzheimer's disease and Down's syndrome brain. Acta Neuropathol (Berl) 104: 1-6 (2002).
    • (2002) Acta Neuropathol , vol.104 , pp. 1-6
    • Su, J.H.1    Kesslak, J.P.2    Head, E.3    Cotman, C.W.4
  • 182
    • 0032870947 scopus 로고    scopus 로고
    • A new molecular link between the fibrillar and granulovacuolar lesions of Alzheimer's disease
    • Ghoshal N, Smiley JF, DeMaggio AJ, Hoekstra MF, Cochran EJ, Binder LI, et al. A new molecular link between the fibrillar and granulovacuolar lesions of Alzheimer's disease. Am J Pathol 155: 1163-1172 (1999).
    • (1999) Am J Pathol , vol.155 , pp. 1163-1172
    • Ghoshal, N.1    Smiley, J.F.2    DeMaggio, A.J.3    Hoekstra, M.F.4    Cochran, E.J.5    Binder, L.I.6
  • 183
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay
    • Anderson AJ, Su JH and Cotman CW. DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay. J Neurosci 16: 1710-1719 (1996).
    • (1996) J Neurosci , vol.16 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 184
    • 0344326254 scopus 로고    scopus 로고
    • Differential distribution of presenilin-1, Bax, and Bcl-X(L) in Alzheimer's disease and frontotemporal dementia
    • Berl
    • Giannakopoulos P, Kovari E, Savioz A, de Bilbao F, Dubois-Dauphin M, Hof PR, et al. Differential distribution of presenilin-1, Bax, and Bcl-X(L) in Alzheimer's disease and frontotemporal dementia. Acta Neuropathol (Berl) 98: 141-149 (1999).
    • (1999) Acta Neuropathol , vol.98 , pp. 141-149
    • Giannakopoulos, P.1    Kovari, E.2    Savioz, A.3    De Bilbao, F.4    Dubois-Dauphin, M.5    Hof, P.R.6
  • 185
    • 0032509773 scopus 로고    scopus 로고
    • Alteration of proteins regulating apoptosis, Bcl-2, Bcl-x, Bax, Bak, Bad, ICH-1 and CPP32, in Alzheimer's disease
    • Kitamura Y, Shimohama S, Kamoshima W, Ota T, Matsuoka Y, Nomura Y, et al. Alteration of proteins regulating apoptosis, Bcl-2, Bcl-x, Bax, Bak, Bad, ICH-1 and CPP32, in Alzheimer's disease. Brain Res 780: 260-269 (1998).
    • (1998) Brain Res , vol.780 , pp. 260-269
    • Kitamura, Y.1    Shimohama, S.2    Kamoshima, W.3    Ota, T.4    Matsuoka, Y.5    Nomura, Y.6
  • 186
    • 0034805535 scopus 로고    scopus 로고
    • Alteration of caspases and apoptosis-related proteins in brains of patients with Alzheimer's disease
    • Engidawork E, Gulesserian T, Yoo BC, Cairns N and Lubec G. Alteration of caspases and apoptosis-related proteins in brains of patients with Alzheimer's disease. Biochem Biophys Res Commun 281: 84-93 (2001).
    • (2001) Biochem Biophys Res Commun , vol.281 , pp. 84-93
    • Engidawork, E.1    Gulesserian, T.2    Yoo, B.C.3    Cairns, N.4    Lubec, G.5
  • 187
    • 0031471277 scopus 로고    scopus 로고
    • Apoptosis-related protein expression in the hippocampus in Alzheimer's disease
    • Nagy ZS and Esiri MM. Apoptosis-related protein expression in the
    • (1997) Neurobiol Aging , vol.18 , pp. 565-571
    • Nagy, Z.S.1    Esiri, M.M.2
  • 188
    • 0035871660 scopus 로고    scopus 로고
    • DNA replication precedes neuronal cell death in Alzheimer's disease
    • Yang Y, Geldmacher DS and Herrup K. DNA replication precedes neuronal cell death in Alzheimer's disease. J Neurosci 21: 2661-2668 (2001).
    • (2001) J Neurosci , vol.21 , pp. 2661-2668
    • Yang, Y.1    Geldmacher, D.S.2    Herrup, K.3
  • 189
    • 0032526652 scopus 로고    scopus 로고
    • Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Abeta1-42 pathogenesis
    • Yang AJ, Chandswangbhuvana D, Margol L and Glabe CG. Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Abeta1-42 pathogenesis. J Neurosci Res 52: 691-698 (1998).
    • (1998) J Neurosci Res , vol.52 , pp. 691-698
    • Yang, A.J.1    Chandswangbhuvana, D.2    Margol, L.3    Glabe, C.G.4
  • 190
    • 2642680857 scopus 로고    scopus 로고
    • Alzheimer disease: DNA fragmentation indicates increased neuronal vulnerability, but not apoptosis
    • Stadelmann C, Bruck W, Bancher C, Jellinger K and Lassmann H. Alzheimer disease: DNA fragmentation indicates increased neuronal vulnerability, but not apoptosis. J Neuropathol Exp Neurol 57: 456-464 (1998).
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 456-464
    • Stadelmann, C.1    Bruck, W.2    Bancher, C.3    Jellinger, K.4    Lassmann, H.5
  • 191
    • 0032747486 scopus 로고    scopus 로고
    • Activation of Csp-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death
    • Stadelmann C, Deckwerth TL, Srinivasan A, Bancher C, Bruck W, Jellinger K, et al. Activation of Csp-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death. Am J Pathol 155: 1459-1466 (1999).
    • (1999) Am J Pathol , vol.155 , pp. 1459-1466
    • Stadelmann, C.1    Deckwerth, T.L.2    Srinivasan, A.3    Bancher, C.4    Bruck, W.5    Jellinger, K.6
  • 192
    • 1642570212 scopus 로고    scopus 로고
    • Down-regulation of DENN/MADD, a TNF receptor binding protein, correlates with neuronal cell death in Alzheimer's disease brain and hippocampal neurons
    • Del Villar K and Miller CA. Down-regulation of DENN/MADD, a TNF receptor binding protein, correlates with neuronal cell death in Alzheimer's disease brain and hippocampal neurons. Proc Natl Acad Sci U S A 101: 4210-4215 (2004).
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4210-4215
    • Del Villar, K.1    Miller, C.A.2
  • 193
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction
    • Takuma K, Yao J, Huang J, Xu H, Chen X, Luddy J, et al. ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction. FASEB J 19: 597-598 (2005).
    • (2005) FASEB J , vol.19 , pp. 597-598
    • Takuma, K.1    Yao, J.2    Huang, J.3    Xu, H.4    Chen, X.5    Luddy, J.6
  • 194
    • 0027373764 scopus 로고
    • Programmed cell death and the control of cell survival: Lessons from the nervous system
    • Raff MC, Barres BA, Burne JF, Coles HS, Ishizaki Y and Jacobson MD. Programmed cell death and the control of cell survival: lessons from the nervous system. Science 262: 695-700 (1993).
    • (1993) Science , vol.262 , pp. 695-700
    • Raff, M.C.1    Barres, B.A.2    Burne, J.F.3    Coles, H.S.4    Ishizaki, Y.5    Jacobson, M.D.6
  • 195
    • 19944434132 scopus 로고    scopus 로고
    • Intracellular Abeta42 activates p53 promoter: A pathway to neurodegeneration in Alzheimer's disease
    • Ohyagi Y, Asahara H, Chui DH, Tsuruta Y, Sakae N, Miyoshi K, et al. Intracellular Abeta42 activates p53 promoter: a pathway to neurodegeneration in Alzheimer's disease. FASEB J 19: 255-257 (2005).
    • (2005) FASEB J , vol.19 , pp. 255-257
    • Ohyagi, Y.1    Asahara, H.2    Chui, D.H.3    Tsuruta, Y.4    Sakae, N.5    Miyoshi, K.6
  • 196
    • 0033903441 scopus 로고    scopus 로고
    • Mitochondrial DNA damage as a mechanism of cell loss in Alzheimer's disease
    • de la Monte SM, Luong T, Neely TR, Robinson D and Wands JR. Mitochondrial DNA damage as a mechanism of cell loss in Alzheimer's disease. Lab Invest 80: 1323-1335 (2000).
    • (2000) Lab Invest , vol.80 , pp. 1323-1335
    • De La Monte, S.M.1    Luong, T.2    Neely, T.R.3    Robinson, D.4    Wands, J.R.5
  • 198
    • 0033028074 scopus 로고    scopus 로고
    • Neurons may live for decades with neurofibrillary tangles
    • Morsch R, Simon W and Coleman PD. Neurons may live for decades with neurofibrillary tangles. J Neuropathol Exp Neurol 58: 188-197 (1999).
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 188-197
    • Morsch, R.1    Simon, W.2    Coleman, P.D.3
  • 199
    • 0031149760 scopus 로고    scopus 로고
    • The cellular basis for the relative resistance of parvalbumin and calretinin immunoreactive neocortical neurons to the pathology of Alzheimer's disease
    • Sampson VL, Morrison JH and Vickers JC. The cellular basis for the relative resistance of parvalbumin and calretinin immunoreactive neocortical neurons to the pathology of Alzheimer's disease. Exp Neurol 145: 295-302 (1997).
    • (1997) Exp Neurol , vol.145 , pp. 295-302
    • Sampson, V.L.1    Morrison, J.H.2    Vickers, J.C.3
  • 200
    • 0037414407 scopus 로고    scopus 로고
    • Direct determination of the proportion of intra- and extra-cellular neocortical neurofibrillary tangles in Alzheimer's disease
    • Vickers JC, Tan A and Dickson TC. Direct determination of the proportion of intra- and extra-cellular neocortical neurofibrillary tangles in Alzheimer's disease. Brain Res 971: 135-137 (2003).
    • (2003) Brain Res , vol.971 , pp. 135-137
    • Vickers, J.C.1    Tan, A.2    Dickson, T.C.3
  • 201
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • Andorfer C, Acker CM, Kress Y, Hof PR, Duff K and Davies P. Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J Neurosci 25: 5446-5454 (2005).
    • (2005) J Neurosci , vol.25 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5    Davies, P.6
  • 202
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz K, Lewis J, Spires T, Paulson J, Kotilinek L, Ingelsson M, et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309: 476-481 (2005).
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3    Paulson, J.4    Kotilinek, L.5    Ingelsson, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.