메뉴 건너뛰기




Volumn 22, Issue 1, 2012, Pages 99-109

Autophagy in dementias

Author keywords

aging; alpha synuclein; Alzheimer's disease; clearance; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; BAFILOMYCIN A1; BECLIN 1; GLYCOPROTEIN GP 120; NEF PROTEIN; PARKIN; TAR DNA BINDING PROTEIN; TAU CRYSTALLIN;

EID: 83455243345     PISSN: 10156305     EISSN: 17503639     Source Type: Journal    
DOI: 10.1111/j.1750-3639.2011.00545.x     Document Type: Conference Paper
Times cited : (57)

References (191)
  • 1
    • 4344643801 scopus 로고    scopus 로고
    • Are Parkinson's disease with dementia and dementia with Lewy bodies the same entity?
    • DOI 10.1177/0891988704267470
    • Aarsland D, Ballard CG, Halliday G, (2004) Are Parkinson's disease with dementia and dementia with Lewy bodies the same entity? J Geriatr Psychiatry Neurol 17: 137-145. (Pubitemid 39128223)
    • (2004) Journal of Geriatric Psychiatry and Neurology , vol.17 , Issue.3 , pp. 137-145
    • Aarsland, D.1    Ballard, C.G.2    Halliday, G.3
  • 3
    • 51449119611 scopus 로고    scopus 로고
    • Disruption of neuronal autophagy by infected microglia results in neurodegeneration
    • Alirezaei M, Kiosses WB, Flynn CT, Brady NR, Fox HS, (2008) Disruption of neuronal autophagy by infected microglia results in neurodegeneration. PLoS ONE 3: e2906.
    • (2008) PLoS ONE , vol.3
    • Alirezaei, M.1    Kiosses, W.B.2    Flynn, C.T.3    Brady, N.R.4    Fox, H.S.5
  • 4
    • 53549096775 scopus 로고    scopus 로고
    • Decreased neuronal autophagy in HIV dementia: A mechanism of indirect neurotoxicity
    • Alirezaei M, Kiosses WB, Fox HS, (2008) Decreased neuronal autophagy in HIV dementia: a mechanism of indirect neurotoxicity. Autophagy 4: 963-966.
    • (2008) Autophagy , vol.4 , pp. 963-966
    • Alirezaei, M.1    Kiosses, W.B.2    Fox, H.S.3
  • 5
    • 78049244477 scopus 로고    scopus 로고
    • VCP associated inclusion body myopathy and paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease
    • e13183.
    • Badadani M, Nalbandian A, Watts GD, Vesa J, Kitazawa M, Su H, et al, (2010) VCP associated inclusion body myopathy and paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease. PLoS ONE 5:e13183.
    • (2010) PLoS ONE , vol.5
    • Badadani, M.1    Nalbandian, A.2    Watts, G.D.3    Vesa, J.4    Kitazawa, M.5    Su, H.6
  • 6
    • 0036830228 scopus 로고    scopus 로고
    • The neuropathogenic contributions of lysosomal dysfunction
    • DOI 10.1046/j.1471-4159.2002.01192.x
    • Bahr BA, Bendiske J, (2002) The neuropathogenic contributions of lysosomal dysfunction. J Neurochem 83: 481-489. (Pubitemid 35231802)
    • (2002) Journal of Neurochemistry , vol.83 , Issue.3 , pp. 481-489
    • Bahr, B.A.1    Bendiske, J.2
  • 7
    • 77956902003 scopus 로고    scopus 로고
    • CHMP2B mutants linked to frontotemporal dementia impair maturation of dendritic spines
    • (Pt 17).
    • Belly A, Bodon G, Blot B, Bouron A, Sadoul R, Goldberg Y, (2010) CHMP2B mutants linked to frontotemporal dementia impair maturation of dendritic spines. J Cell Sci 123 (Pt 17): 2943-2954.
    • (2010) J Cell Sci , vol.123 , pp. 2943-2954
    • Belly, A.1    Bodon, G.2    Blot, B.3    Bouron, A.4    Sadoul, R.5    Goldberg, Y.6
  • 8
    • 0037989761 scopus 로고    scopus 로고
    • Lysosomal activation is a compensatory response against protein accumulation and associated synaptopathogenesis - An approach for slowing Alzheimer disease?
    • Bendiske J, Bahr BA, (2003) Lysosomal activation is a compensatory response against protein accumulation and associated synaptopathogenesis-an approach for slowing Alzheimer disease? J Neuropathol Exp Neurol 62: 451-463. (Pubitemid 36560187)
    • (2003) Journal of Neuropathology and Experimental Neurology , vol.62 , Issue.5 , pp. 451-463
    • Bendiske, J.1    Bahr, B.A.2
  • 9
    • 0032555641 scopus 로고    scopus 로고
    • Isolation and characterization of rat liver amphisomes: Evidence for fusion of autophagosomes with both early and late endosomes
    • DOI 10.1074/jbc.273.34.21883
    • Berg TO, Fengsrud M, Stromhaug PE, Berg T, Seglen PO, (1998) Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes. J Biol Chem 273: 21883-21892. (Pubitemid 28405366)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.34 , pp. 21883-21892
    • Berg, T.O.1    Fengsrud, M.2    Stromhaug, P.E.3    Berg, T.4    Seglen, P.O.5
  • 10
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • Boland B, Kumar A, Lee S, Platt FM, Wegiel J, Yu WH, Nixon RA, (2008) Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J Neurosci 28: 6926-6937.
    • (2008) J Neurosci , vol.28 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6    Nixon, R.A.7
  • 11
    • 33645642679 scopus 로고    scopus 로고
    • Clinical features of frontotemporal dementia
    • DOI 10.1097/01.wad.0000183086.99691.91, PII 0000209320051000100002
    • Boxer AL, Miller BL, (2005) Clinical features of frontotemporal dementia. Alzheimer Dis Assoc Disord 19 (Suppl. 1): S3-S6. (Pubitemid 44378500)
    • (2005) Alzheimer Disease and Associated Disorders , vol.19 , Issue.SUPPL. 1
    • Boxer, A.L.1    Miller, B.L.2
  • 12
    • 0034007822 scopus 로고    scopus 로고
    • Pathoanatomy of Parkinson's disease
    • (Suppl.).
    • Braak H, Braak E, (2000) Pathoanatomy of Parkinson's disease. J Neurol 247 (Suppl. 2): II3-II10.
    • (2000) J Neurol , vol.247 , Issue.2
    • Braak, H.1    Braak, E.2
  • 14
    • 33751031873 scopus 로고    scopus 로고
    • Cortical Lewy body disease and Parkinson's disease dementia
    • DOI 10.1097/01.wco.0000247607.34697.a2, PII 0001905220061200000012
    • Burn DJ, (2006) Cortical Lewy body disease and Parkinson's disease dementia. Curr Opin Neurol 19: 572-579. (Pubitemid 44760441)
    • (2006) Current Opinion in Neurology , vol.19 , Issue.6 , pp. 572-579
    • Burn, D.J.1
  • 17
    • 33645986472 scopus 로고    scopus 로고
    • Gamma interferon primes productive human immunodeficiency virus infection in astrocytes
    • Carroll-Anzinger D, Al-Harthi L, (2006) Gamma interferon primes productive human immunodeficiency virus infection in astrocytes. J Virol 80: 541-544.
    • (2006) J Virol , vol.80 , pp. 541-544
    • Carroll-Anzinger, D.1    Al-Harthi, L.2
  • 18
    • 79952104480 scopus 로고    scopus 로고
    • The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells
    • Casarejos MJ, Solano RM, Gomez A, Perucho J, de Yebenes JG, Mena MA, (2011) The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells. Neurochem Int 58: 512-520.
    • (2011) Neurochem Int , vol.58 , pp. 512-520
    • Casarejos, M.J.1    Solano, R.M.2    Gomez, A.3    Perucho, J.4    De Yebenes, J.G.5    Mena, M.A.6
  • 21
    • 18244399344 scopus 로고    scopus 로고
    • Pathophysiological roles of amyloidogenic carboxy-terminal fragments of the beta-amyloid precursor protein in Alzheimer's disease
    • Chang KA, Suh YH, (2005) Pathophysiological roles of amyloidogenic carboxy-terminal fragments of the beta-amyloid precursor protein in Alzheimer's disease. J Pharmacol Sci 97: 461-471.
    • (2005) J Pharmacol Sci , vol.97 , pp. 461-471
    • Chang, K.A.1    Suh, Y.H.2
  • 22
    • 33745866310 scopus 로고    scopus 로고
    • Autophagic stress in neuronal injury and disease
    • DOI 10.1097/01.jnen.0000229233.75253.be, PII 0000507220060500000001
    • Chu CT, (2006) Autophagic stress in neuronal injury and disease. J Neuropathol Exp Neurol 65: 423-432. (Pubitemid 44297264)
    • (2006) Journal of Neuropathology and Experimental Neurology , vol.65 , Issue.5 , pp. 423-432
    • Chu, C.T.1
  • 23
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: Relationship to alpha-synuclein inclusions
    • Chu Y, Dodiya H, Aebischer P, Olanow CW, Kordower JH, (2009) Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions. Neurobiol Dis 35: 385-398.
    • (2009) Neurobiol Dis , vol.35 , pp. 385-398
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 27
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy
    • Crews L, Spencer B, Desplats P, Patrick C, Paulino A, Rockenstein E, et al, (2010) Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy. PLoS ONE 5: e9313.
    • (2010) PLoS ONE , vol.5
    • Crews, L.1    Spencer, B.2    Desplats, P.3    Patrick, C.4    Paulino, A.5    Rockenstein, E.6
  • 28
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • DOI 10.1016/j.tcb.2003.12.002
    • Cuervo AM, (2004) Autophagy: in sickness and in health. Trends Cell Biol 14: 70-77. (Pubitemid 38186640)
    • (2004) Trends in Cell Biology , vol.14 , Issue.2 , pp. 70-77
    • Cuervo, A.M.1
  • 29
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy
    • DOI 10.1126/science.1101738
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D, (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305: 1292-1295. (Pubitemid 39129234)
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stafanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 30
    • 64949185378 scopus 로고    scopus 로고
    • Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo
    • Cullen V, Lindfors M, Ng J, Paetau A, Swinton E, Kolodziej P, et al, (2009) Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo. Mol Brain 2: 5.
    • (2009) Mol Brain , vol.2 , pp. 5
    • Cullen, V.1    Lindfors, M.2    Ng, J.3    Paetau, A.4    Swinton, E.5    Kolodziej, P.6
  • 31
    • 77952486387 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone
    • Custer SK, Neumann M, Lu H, Wright AC, Taylor JP, (2010) Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone. Hum Mol Genet 19: 1741-1755.
    • (2010) Hum Mol Genet , vol.19 , pp. 1741-1755
    • Custer, S.K.1    Neumann, M.2    Lu, H.3    Wright, A.C.4    Taylor, J.P.5
  • 32
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • DOI 10.1016/S0896-6273(03)00568-3
    • Dauer W, Przedborski S, (2003) Parkinson's disease: mechanisms and models. Neuron 39: 889-909. (Pubitemid 37130207)
    • (2003) Neuron , vol.39 , Issue.6 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 34
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in parkinson's disease
    • DOI 10.1126/science.1087753
    • Dawson TM, Dawson VL, (2003) Molecular pathways of neurodegeneration in Parkinson's disease. Science 302: 819-822. (Pubitemid 37339614)
    • (2003) Science , vol.302 , Issue.5646 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 36
    • 0025363276 scopus 로고
    • Studies on the mechanisms of autophagy: Formation of the autophagic vacuole
    • Dunn WA Jr, (1990) Studies on the mechanisms of autophagy: formation of the autophagic vacuole. J Cell Biol 110: 1923-1933.
    • (1990) J Cell Biol , vol.110 , pp. 1923-1933
    • Dunn, Jr.W.A.1
  • 37
    • 0025340880 scopus 로고
    • Studies on the mechanisms of autophagy: Maturation of the autophagic vacuole
    • Dunn WA Jr, (1990) Studies on the mechanisms of autophagy: maturation of the autophagic vacuole. J Cell Biol 110: 1935-1945.
    • (1990) J Cell Biol , vol.110 , pp. 1935-1945
    • Dunn, Jr.W.A.1
  • 38
    • 7744235672 scopus 로고    scopus 로고
    • Death by design: Apoptosis, necrosis and autophagy
    • DOI 10.1016/j.ceb.2004.09.011, PII S0955067404001474
    • Edinger AL, Thompson CB, (2004) Death by design: apoptosis, necrosis and autophagy. Curr Opin Cell Biol 16: 663-669. (Pubitemid 39463117)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.6 , pp. 663-669
    • Edinger, A.L.1    Thompson, C.B.2
  • 39
    • 77249095323 scopus 로고    scopus 로고
    • Synaptic proteins linked to HIV-1 infection and immunoproteasome induction: Proteomic analysis of human synaptosomes
    • Gelman BB, Nguyen TP, (2010) Synaptic proteins linked to HIV-1 infection and immunoproteasome induction: proteomic analysis of human synaptosomes. J Neuroimmune Pharmacol 5: 92-102.
    • (2010) J Neuroimmune Pharmacol , vol.5 , pp. 92-102
    • Gelman, B.B.1    Nguyen, T.P.2
  • 41
    • 77949897022 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: A spectrum of TDP-43 proteinopathies
    • Geser F, Lee VM, Trojanowski JQ, (2010) Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: a spectrum of TDP-43 proteinopathies. Neuropathology 30: 103-112.
    • (2010) Neuropathology , vol.30 , pp. 103-112
    • Geser, F.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 42
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
    • Giasson BI, Duda JE, Murray IV, Chen Q, Souza JM, Hurtig HI, et al, (2000) Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science 290: 985-989.
    • (2000) Science , vol.290 , pp. 985-989
    • Giasson, B.I.1    Duda, J.E.2    Murray, I.V.3    Chen, Q.4    Souza, J.M.5    Hurtig, H.I.6
  • 44
  • 46
    • 2442482810 scopus 로고    scopus 로고
    • Autophagy as a cell death and tumor suppressor mechanism
    • DOI 10.1038/sj.onc.1207521
    • Gozuacik D, Kimchi A, (2004) Autophagy as a cell death and tumor suppressor mechanism. Oncogene 23: 2891-2906. (Pubitemid 38638851)
    • (2004) Oncogene , vol.23 , Issue.16 , pp. 2891-2906
    • Gozuacik, D.1    Kimchi, A.2
  • 48
    • 15944397586 scopus 로고    scopus 로고
    • Brain deposition of beta-amyloid is a common pathologic feature in HIV positive patients
    • Green DA, Masliah E, Vinters HV, Beizai P, Moore DJ, Achim CL, (2005) Brain deposition of beta-amyloid is a common pathologic feature in HIV positive patients. AIDS 19: 407-411. (Pubitemid 40446187)
    • (2005) AIDS , vol.19 , Issue.4 , pp. 407-411
    • Green, D.A.1    Masliah, E.2    Vinters, H.V.3    Beizai, P.4    Moore, D.J.5    Achim, C.L.6
  • 50
    • 0023410588 scopus 로고
    • Neuropsychiatric studies in a family with presenile dementia different from Alzheimer and Pick disease
    • Gydesen S, Hagen S, Klinken L, Abelskov J, Sorensen SA, (1987) Neuropsychiatric studies in a family with presenile dementia different from Alzheimer and Pick disease. Acta Psychiatr Scand 76: 276-284.
    • (1987) Acta Psychiatr Scand , vol.76 , pp. 276-284
    • Gydesen, S.1    Hagen, S.2    Klinken, L.3    Abelskov, J.4    Sorensen, S.A.5
  • 51
    • 0034633729 scopus 로고    scopus 로고
    • Evidence of a source of HIV type 1 within the central nervous system by ultraintensive sampling of cerebrospinal fluid and plasma
    • Haas DW, Clough LA, Johnson BW, Harris VL, Spearman P, Wilkinson GR, et al, (2000) Evidence of a source of HIV type 1 within the central nervous system by ultraintensive sampling of cerebrospinal fluid and plasma. AIDS Res Hum Retroviruses 16: 1491-1502.
    • (2000) AIDS Res Hum Retroviruses , vol.16 , pp. 1491-1502
    • Haas, D.W.1    Clough, L.A.2    Johnson, B.W.3    Harris, V.L.4    Spearman, P.5    Wilkinson, G.R.6
  • 52
    • 0028922667 scopus 로고
    • The vacuolar H(+)-ATPase inhibitor bafilomycin A1 differentially affects proteolytic processing of mutant and wild-type beta-amyloid precursor protein
    • Haass C, Capell A, Citron M, Teplow DB, Selkoe DJ, (1995) The vacuolar H(+)-ATPase inhibitor bafilomycin A1 differentially affects proteolytic processing of mutant and wild-type beta-amyloid precursor protein. J Biol Chem 270: 6186-6192.
    • (1995) J Biol Chem , vol.270 , pp. 6186-6192
    • Haass, C.1    Capell, A.2    Citron, M.3    Teplow, D.B.4    Selkoe, D.J.5
  • 53
    • 77951641578 scopus 로고    scopus 로고
    • Frontotemporal dementia or frontotemporal lobar degeneration-overview of a group of proteinopathies
    • Haberland C, (2010) Frontotemporal dementia or frontotemporal lobar degeneration-overview of a group of proteinopathies. Ideggyogy Sz 63: 87-93.
    • (2010) Ideggyogy Sz , vol.63 , pp. 87-93
    • Haberland, C.1
  • 54
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R, et al, (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441: 885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 55
    • 0032491408 scopus 로고    scopus 로고
    • Genetic classification of primary neurodegenerative disease
    • Hardy J, Gwinn-Hardy K, (1998) Genetic classification of primary neurodegenerative disease. Science 282: 1075-1079. (Pubitemid 28516229)
    • (1998) Science , vol.282 , Issue.5391 , pp. 1075-1079
    • Hardy, J.1    Gwinn-Hardy, K.2
  • 56
    • 0032888789 scopus 로고    scopus 로고
    • Alpha-synuclein in Lewy body disease and Alzheimer's disease
    • Hashimoto M, Masliah E, (1999) Alpha-synuclein in Lewy body disease and Alzheimer's disease. Brain Pathol 9: 707-720. (Pubitemid 29470963)
    • (1999) Brain Pathology , vol.9 , Issue.4 , pp. 707-720
    • Hashimoto, M.1    Masliah, E.2
  • 59
    • 0036800480 scopus 로고    scopus 로고
    • Calcium dysregulation and neuronal apoptosis by the HIV-1 proteins Tat and gp120
    • Haughey NJ, Mattson MP, (2002) Calcium dysregulation and neuronal apoptosis by the HIV-1 proteins Tat and gp120. J Acquir Immune Defic Syndr 31 (Suppl. 2): S55-S61. (Pubitemid 35190559)
    • (2002) Journal of Acquired Immune Deficiency Syndromes , vol.31 , Issue.SUPPL. 2
    • Haughey, N.J.1    Mattson, M.P.2
  • 60
    • 0034909804 scopus 로고    scopus 로고
    • HIV-1 Tat through phosphorylation of NMDA receptors potentiates glutamate excitotoxicity
    • DOI 10.1046/j.1471-4159.2001.00396.x
    • Haughey NJ, Nath A, Mattson MP, Slevin JT, Geiger JD, (2001) HIV-1 Tat through phosphorylation of NMDA receptors potentiates glutamate excitotoxicity. J Neurochem 78: 457-467. (Pubitemid 32729974)
    • (2001) Journal of Neurochemistry , vol.78 , Issue.3 , pp. 457-467
    • Haughey, N.J.1    Nath, A.2    Mattson, M.P.3    Slevin, J.T.4    Geiger, J.D.5
  • 61
    • 78650834306 scopus 로고    scopus 로고
    • HIV-associated neurocognitive disorders persist in the era of potent antiretroviral therapy: CHARTER Study
    • Heaton RK, Clifford DB, Franklin DR Jr, Woods SP, Ake C, Vaida F, et al, (2010) HIV-associated neurocognitive disorders persist in the era of potent antiretroviral therapy: CHARTER Study. Neurology 75: 2087-2096.
    • (2010) Neurology , vol.75 , pp. 2087-2096
    • Heaton, R.K.1    Clifford, D.B.2    Franklin, Jr.D.R.3    Woods, S.P.4    Ake, C.5    Vaida, F.6
  • 62
    • 79952921819 scopus 로고    scopus 로고
    • HIV-associated neurocognitive disorders before and during the era of combination antiretroviral therapy: Differences in rates, nature, and predictors
    • Heaton RK, Franklin DR, Ellis RJ, McCutchan JA, Letendre SL, Leblanc S, et al, (2011) HIV-associated neurocognitive disorders before and during the era of combination antiretroviral therapy: differences in rates, nature, and predictors. J Neurovirol 17: 3-16.
    • (2011) J Neurovirol , vol.17 , pp. 3-16
    • Heaton, R.K.1    Franklin, D.R.2    Ellis, R.J.3    McCutchan, J.A.4    Letendre, S.L.5    Leblanc, S.6
  • 63
    • 66349120877 scopus 로고    scopus 로고
    • Autophagy protects neuron from Abeta-induced cytotoxicity
    • Hung SY, Huang WP, Liou HC, Fu WM, (2009) Autophagy protects neuron from Abeta-induced cytotoxicity. Autophagy 5: 502-510.
    • (2009) Autophagy , vol.5 , pp. 502-510
    • Hung, S.Y.1    Huang, W.P.2    Liou, H.C.3    Fu, W.M.4
  • 65
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • Itakura E, Kishi C, Inoue K, Mizushima N, (2008) Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol Biol Cell 19: 5360-5372.
    • (2008) Mol Biol Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 66
    • 77957969657 scopus 로고    scopus 로고
    • Beclin 1 complex in autophagy and Alzheimer disease
    • Jaeger PA, Wyss-Coray T, (2010) Beclin 1 complex in autophagy and Alzheimer disease. Arch Neurol 67: 1181-1184.
    • (2010) Arch Neurol , vol.67 , pp. 1181-1184
    • Jaeger, P.A.1    Wyss-Coray, T.2
  • 69
    • 40449139980 scopus 로고    scopus 로고
    • The itinerary of autophagosomes: From peripheral formation to kiss-and-run fusion with lysosomes
    • DOI 10.1111/j.1600-0854.2008.00701.x
    • Jahreiss L, Menzies FM, Rubinsztein DC, (2008) The itinerary of autophagosomes: from peripheral formation to kiss-and-run fusion with lysosomes. Traffic 9: 574-587. (Pubitemid 351351616)
    • (2008) Traffic , vol.9 , Issue.4 , pp. 574-587
    • Jahreiss, L.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 70
    • 33645552854 scopus 로고    scopus 로고
    • Cognitive profiles of individual patients with Parkinson's disease and dementia: Comparison with dementia with lewy bodies and Alzheimer's disease
    • Janvin CC, Larsen JP, Salmon DP, Galasko D, Hugdahl K, Aarsland D, (2006) Cognitive profiles of individual patients with Parkinson's disease and dementia: comparison with dementia with lewy bodies and Alzheimer's disease. Mov Disord 21: 337-342.
    • (2006) Mov Disord , vol.21 , pp. 337-342
    • Janvin, C.C.1    Larsen, J.P.2    Salmon, D.P.3    Galasko, D.4    Hugdahl, K.5    Aarsland, D.6
  • 71
    • 33747762262 scopus 로고    scopus 로고
    • Does striatal pathology distinguish Parkinson disease with dementia and dementia with Lewy bodies?
    • DOI 10.1007/s00401-006-0088-2
    • Jellinger KA, Attems J, (2006)) Does striatal pathology distinguish Parkinson disease with dementia and dementia with Lewy bodies? Acta Neuropathol (Berl) 112: 253-260. (Pubitemid 44275880)
    • (2006) Acta Neuropathologica , vol.112 , Issue.3 , pp. 253-260
    • Jellinger, K.A.1    Attems, J.2
  • 72
    • 0032575551 scopus 로고    scopus 로고
    • Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae
    • DOI 10.1074/jbc.273.35.22284
    • Kametaka S, Okano T, Ohsumi M, Ohsumi Y, (1998) Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae. J Biol Chem 273: 22284-22291. (Pubitemid 28399786)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.35 , pp. 22284-22291
    • Kametaka, S.1    Okano, T.2    Ohsumi, M.3    Ohsumi, Y.4
  • 73
    • 33845764425 scopus 로고    scopus 로고
    • HIV-1 gp120 compromises blood-brain barrier integrity and enhance monocyte migration across blood-brain barrier: Implication for viral neuropathogenesis
    • DOI 10.1038/sj.jcbfm.9600330, PII 9600330
    • Kanmogne GD, Schall K, Leibhart J, Knipe B, Gendelman HE, Persidsky Y, (2007) HIV-1 gp120 compromises blood-brain barrier integrity and enhances monocyte migration across blood-brain barrier: implication for viral neuropathogenesis. J Cereb Blood Flow Metab 27: 123-134. (Pubitemid 46006590)
    • (2007) Journal of Cerebral Blood Flow and Metabolism , vol.27 , Issue.1 , pp. 123-134
    • Kanmogne, G.D.1    Schall, K.2    Leibhart, J.3    Knipe, B.4    Gendelman, H.E.5    Persidsky, Y.6
  • 74
    • 0035912198 scopus 로고    scopus 로고
    • Pathways to neuronal injury and apoptosis in HIV-associated dementia
    • DOI 10.1038/35073667
    • Kaul M, Garden GA, Lipton SA, (2001) Pathways to neuronal injury and apoptosis in HIV-associated dementia. Nature 410: 988-994. (Pubitemid 32335850)
    • (2001) Nature , vol.410 , Issue.6831 , pp. 988-994
    • Kaul, M.1    Garden, G.A.2    Lipton, S.A.3
  • 75
    • 79956223920 scopus 로고    scopus 로고
    • Inhibition of Tat-mediated HIV-1 replication and neurotoxicity by novel GSK3-beta inhibitors
    • Kehn-Hall K, Guendel I, Carpio L, Skaltsounis L, Meijer L, Al-Harthi L, et al, (2011) Inhibition of Tat-mediated HIV-1 replication and neurotoxicity by novel GSK3-beta inhibitors. Virology 415: 56-68.
    • (2011) Virology , vol.415 , pp. 56-68
    • Kehn-Hall, K.1    Guendel, I.2    Carpio, L.3    Skaltsounis, L.4    Meijer, L.5    Al-Harthi, L.6
  • 76
    • 77952532559 scopus 로고    scopus 로고
    • Frontotemporal dementia, Pick's disease
    • Kertesz A, (2010) Frontotemporal dementia, Pick's disease. Ideggyogy Sz 63: 4-12.
    • (2010) Ideggyogy Sz , vol.63 , pp. 4-12
    • Kertesz, A.1
  • 77
    • 67650309767 scopus 로고    scopus 로고
    • Increased frequency of alpha-synuclein in the substantia nigra in human immunodeficiency virus infection
    • Khanlou N, Moore DJ, Chana G, Cherner M, Lazzaretto D, Dawes S, et al, (2009) Increased frequency of alpha-synuclein in the substantia nigra in human immunodeficiency virus infection. J Neurovirol 15: 131-138.
    • (2009) J Neurovirol , vol.15 , pp. 131-138
    • Khanlou, N.1    Moore, D.J.2    Chana, G.3    Cherner, M.4    Lazzaretto, D.5    Dawes, S.6
  • 78
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • DOI 10.1093/embo-reports/kve061
    • Kihara A, Kabeya Y, Ohsumi Y, Yoshimori T, (2001) Beclin- phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep 2: 330-335. (Pubitemid 32401529)
    • (2001) EMBO Reports , vol.2 , Issue.4 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 79
    • 47149089713 scopus 로고    scopus 로고
    • Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes
    • Kimura S, Noda T, Yoshimori T, (2008) Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes. Cell Struct Funct 33: 109-122.
    • (2008) Cell Struct Funct , vol.33 , pp. 109-122
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 80
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small A β oligomers: The solution to an Alzheimer's disease conundrum?
    • DOI 10.1016/S0166-2236(00)01749-5, PII S0166223600017495
    • Klein WL, Krafft GA, Finch CE, (2001) Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 24: 219-224. (Pubitemid 32204378)
    • (2001) Trends in Neurosciences , vol.24 , Issue.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 81
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • DOI 10.1126/science.290.5497.1717
    • Klionsky DJ, Emr SD, (2000) Autophagy as a regulated pathway of cellular degradation. Science 290: 1717-1721. (Pubitemid 32004796)
    • (2000) Science , vol.290 , Issue.5497 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 82
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I, et al, (2006) Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441: 880-884.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 84
    • 67649585835 scopus 로고    scopus 로고
    • Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
    • Kyei GB, Dinkins C, Davis AS, Roberts E, Singh SB, Dong C, et al, (2009) Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages. J Cell Biol 186: 255-268.
    • (2009) J Cell Biol , vol.186 , pp. 255-268
    • Kyei, G.B.1    Dinkins, C.2    Davis, A.S.3    Roberts, E.4    Singh, S.B.5    Dong, C.6
  • 87
    • 0037044835 scopus 로고    scopus 로고
    • New class of inhibitors of amyloid-β fibril formation: Implications for the mechanism of pathogenesis in Alzheimer's disease
    • DOI 10.1074/jbc.M206593200
    • Lashuel HA, Hartley DM, Balakhaneh D, Aggarwal A, Teichberg S, Callaway DJ, (2002) New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease. J Biol Chem 277: 42881-42890. (Pubitemid 35285665)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 42881-42890
    • Lashuel, H.A.1    Hartley, D.M.2    Balakhaneh, D.3    Aggarwal, A.4    Teichberg, S.5    Callaway, D.J.E.6
  • 88
    • 0036415838 scopus 로고    scopus 로고
    • α-synuclein, especially the parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • DOI 10.1016/S0022-2836(02)00735-0
    • Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, Lansbury PT Jr, (2002) Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J Mol Biol 322: 1089-1102. (Pubitemid 35266514)
    • (2002) Journal of Molecular Biology , vol.322 , Issue.5 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury Jr., P.T.7
  • 89
    • 38949214734 scopus 로고    scopus 로고
    • Roles of ESCRT in autophagy-associated neurodegeneration
    • Lee JA, Gao FB, (2008) Roles of ESCRT in autophagy-associated neurodegeneration. Autophagy 4: 230-232.
    • (2008) Autophagy , vol.4 , pp. 230-232
    • Lee, J.A.1    Gao, F.B.2
  • 90
    • 67649996222 scopus 로고    scopus 로고
    • Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia
    • Lee JA, Gao FB, (2009) Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia. J Neurosci 29: 8506-8511.
    • (2009) J Neurosci , vol.29 , pp. 8506-8511
    • Lee, J.A.1    Gao, F.B.2
  • 91
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • DOI 10.1016/j.cub.2007.07.029, PII S0960982207017071
    • Lee JA, Beigneux A, Ahmad ST, Young SG, Gao FB, (2007) ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr Biol 17: 1561-1567. (Pubitemid 47380392)
    • (2007) Current Biology , vol.17 , Issue.18 , pp. 1561-1567
    • Lee, J.-A.1    Beigneux, A.2    Ahmad, S.T.3    Young, S.G.4    Gao, F.-B.5
  • 92
    • 0035109909 scopus 로고    scopus 로고
    • Effect of the overexpression of wild-type or mutant α-synuclein on cell susceptibility to insult
    • DOI 10.1046/j.1471-4159.2001.00149.x
    • Lee M, Hyun D, Halliwell B, Jenner P, (2001) Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult. J Neurochem 76: 998-1009. (Pubitemid 32167373)
    • (2001) Journal of Neurochemistry , vol.76 , Issue.4 , pp. 998-1009
    • Lee, M.1    Hyun, D.-H.2    Halliwell, B.3    Jenner, P.4
  • 94
    • 12944308330 scopus 로고    scopus 로고
    • Eating oneself and uninvited guests: Autophagy-related pathways in cellular defense
    • DOI 10.1016/j.cell.2005.01.005, PII S0092867405000437
    • Levine B, (2005) Eating oneself and uninvited guests: autophagy-related pathways in cellular defense. Cell 120: 159-162. (Pubitemid 40174758)
    • (2005) Cell , vol.120 , Issue.2 , pp. 159-162
    • Levine, B.1
  • 95
    • 50249089984 scopus 로고    scopus 로고
    • Beyond autophagy: The role of UVRAG in membrane trafficking
    • Liang C, Sir D, Lee S, Ou JH, Jung JU, (2008) Beyond autophagy: the role of UVRAG in membrane trafficking. Autophagy 4: 817-820.
    • (2008) Autophagy , vol.4 , pp. 817-820
    • Liang, C.1    Sir, D.2    Lee, S.3    Ou, J.H.4    Jung, J.U.5
  • 97
  • 100
    • 0032798589 scopus 로고    scopus 로고
    • HIV-1 Tat-mediated activation of glycogen synthase kinase-3β contributes to Tat-mediated neurotoxicity
    • DOI 10.1046/j.1471-4159.1999.0730578.x
    • Maggirwar SB, Tong N, Ramirez S, Gelbard HA, Dewhurst S, (1999) HIV-1 Tat-mediated activation of glycogen synthase kinase-3beta contributes to Tat-mediated neurotoxicity. J Neurochem 73: 578-586. (Pubitemid 29339830)
    • (1999) Journal of Neurochemistry , vol.73 , Issue.2 , pp. 578-586
    • Maggirwar, S.B.1    Tong, N.2    Ramirez, S.3    Gelbard, H.A.4    Dewhurst, S.5
  • 102
    • 33748584602 scopus 로고    scopus 로고
    • Interaction between Aβ peptide and α synuclein: Molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease
    • DOI 10.1007/s11064-006-9140-9
    • Mandal PK, Pettegrew JW, Masliah E, Hamilton RL, Mandal R, (2006) Interaction between Abeta peptide and alpha synuclein: molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease. Neurochem Res 31: 1153-1162. (Pubitemid 44379676)
    • (2006) Neurochemical Research , vol.31 , Issue.9 , pp. 1153-1162
    • Mandal, P.K.1    Pettegrew, J.W.2    Masliah, E.3    Hamilton, R.L.4    Mandal, R.5
  • 103
    • 0036847012 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Tat protein and methamphetamine interact synergistically to impair striatal dopaminergic function
    • DOI 10.1046/j.1471-4159.2002.01212.x
    • Maragos WF, Young KL, Turchan JT, Guseva M, Pauly JR, Nath A, Cass WA, (2002) Human immunodeficiency virus-1 Tat protein and methamphetamine interact synergistically to impair striatal dopaminergic function. J Neurochem 83: 955-963. (Pubitemid 35316046)
    • (2002) Journal of Neurochemistry , vol.83 , Issue.4 , pp. 955-963
    • Maragos, W.F.1    Young, K.L.2    Turchan, J.T.3    Guseva, M.4    Pauly, J.R.5    Nath, A.6    Cass, W.A.7
  • 105
    • 0037196894 scopus 로고    scopus 로고
    • Progression and staging of Lewy pathology in brains from patients with dementia with Lewy bodies
    • PII S0022510X02000060
    • Marui W, Iseki E, Nakai T, Miura S, Kato M, Ueda K, Kosaka K, (2002) Progression and staging of Lewy pathology in brains from patients with dementia with Lewy bodies. J Neurol Sci 195: 153-159. (Pubitemid 34202293)
    • (2002) Journal of the Neurological Sciences , vol.195 , Issue.2 , pp. 153-159
    • Marui, W.1    Iseki, E.2    Nakai, T.3    Miura, S.4    Kato, M.5    Ueda, K.6    Kosaka, K.7
  • 106
    • 0033897170 scopus 로고    scopus 로고
    • Incidence and prevalence of neurological disorders associated with HIV since the introduction of highly active antiretroviral therapy (HAART)
    • DOI 10.1136/jnnp.69.3.376
    • Maschke M, Kastrup O, Esser S, Ross B, Hengge U, Hufnagel A, (2000) Incidence and prevalence of neurological disorders associated with HIV since the introduction of highly active antiretroviral therapy (HAART). J Neurol Neurosurg Psychiatry 69: 376-380. (Pubitemid 30636242)
    • (2000) Journal of Neurology Neurosurgery and Psychiatry , vol.69 , Issue.3 , pp. 376-380
    • Maschke, M.1    Kastrup, O.2    Esser, S.3    Ross, B.4    Hengge, U.5    Hufnagel, A.6
  • 108
    • 77949336151 scopus 로고    scopus 로고
    • 2010 Alzheimer's disease facts and figures
    • Maslow K, (2010) 2010 Alzheimer's disease facts and figures. Alzheimers Dement 6: 158-194.
    • (2010) Alzheimers Dement , vol.6 , pp. 158-194
    • Maslow, K.1
  • 109
    • 83455210612 scopus 로고    scopus 로고
    • Extensive distribution of glial cytoplasmic inclusions in an autopsied case of multiple system atrophy with a prolonged 18-year clinical course
    • doi: 10.1111/j.1440-1789.2011.01222.x [epub ahead of print].
    • Masui K, Nakata Y, Fujii N, Iwaki T, (2011) Extensive distribution of glial cytoplasmic inclusions in an autopsied case of multiple system atrophy with a prolonged 18-year clinical course. Neuropathology doi: 10.1111/j.1440-1789.2011.01222.x [epub ahead of print].
    • (2011) Neuropathology
    • Masui, K.1    Nakata, Y.2    Fujii, N.3    Iwaki, T.4
  • 110
    • 0036954488 scopus 로고    scopus 로고
    • Oxidative stress, perturbed calcium homeostasis, and immune dysfunction in Alzheimer's disease
    • DOI 10.1080/13550280290100978
    • Mattson MP, (2002) Oxidative stress, perturbed calcium homeostasis, and immune dysfunction in Alzheimer's disease. J Neurovirol 8: 539-550. (Pubitemid 36104719)
    • (2002) Journal of NeuroVirology , vol.8 , Issue.6 , pp. 539-550
    • Mattson, M.P.1
  • 113
    • 77952940200 scopus 로고    scopus 로고
    • Human immunodeficiency virus-associated neurocognitive disorders: Mind the gap
    • McArthur JC, Steiner J, Sacktor N, Nath A, (2010) Human immunodeficiency virus-associated neurocognitive disorders: mind the gap. Ann Neurol 67: 699-714.
    • (2010) Ann Neurol , vol.67 , pp. 699-714
    • McArthur, J.C.1    Steiner, J.2    Sacktor, N.3    Nath, A.4
  • 114
    • 0034518238 scopus 로고    scopus 로고
    • Spectrum of Parkinson's disease, Parkinson's dementia, and Lewy body dementia
    • McKeith IG, (2000) Spectrum of Parkinson's disease, Parkinson's dementia, and Lewy body dementia. Neurol Clin 18: 865-902.
    • (2000) Neurol Clin , vol.18 , pp. 865-902
    • McKeith, I.G.1
  • 117
    • 0037159608 scopus 로고    scopus 로고
    • Lysosomal malfunction accompanies alpha-synuclein aggregation in a progressive mouse model of Parkinson's disease
    • DOI 10.1016/S0006-8993(02)03514-X, PII S000689930203514X
    • Meredith GE, Totterdell S, Petroske E, Santa Cruz K, Callison RC Jr, Lau YS, (2002) Lysosomal malfunction accompanies alpha-synuclein aggregation in a progressive mouse model of Parkinson's disease. Brain Res 956: 156-165. (Pubitemid 35335568)
    • (2002) Brain Research , vol.956 , Issue.1 , pp. 156-165
    • Meredith, G.E.1    Totterdell, S.2    Petroske, E.3    Santa Cruz, K.4    Callison Jr., R.C.5    Lau, Y.-S.6
  • 120
    • 0033515471 scopus 로고    scopus 로고
    • Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation
    • Narhi L, Wood SJ, Steavenson S, Jiang Y, Wu GM, Anafi D, et al, (1999) Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation. J Biochem 274: 9843-9846.
    • (1999) J Biochem , vol.274 , pp. 9843-9846
    • Narhi, L.1    Wood, S.J.2    Steavenson, S.3    Jiang, Y.4    Wu, G.M.5    Anafi, D.6
  • 121
    • 0036891081 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) proteins in neuropathogenesis of HIV dementia
    • DOI 10.1086/344528
    • Nath A, (2002) Human immunodeficiency virus (HIV) proteins in neuropathogenesis of HIV dementia. J Infect Dis 186 (Suppl. 2): S193-S198. (Pubitemid 35370481)
    • (2002) Journal of Infectious Diseases , vol.186 , Issue.SUPPL. 2
    • Nath, A.1
  • 122
    • 0035970642 scopus 로고    scopus 로고
    • Beta amyloid precursor protein and patterns of HIV p24 immunohistochemistry in different brain areas of AIDS patients
    • DOI 10.1097/00002030-200103300-00005
    • Nebuloni M, Pellegrinelli A, Ferri A, Bonetto S, Boldorini R, Vago L, et al, (2001) Beta amyloid precursor protein and patterns of HIV p24 immunohistochemistry in different brain areas of AIDS patients. AIDS 15: 571-575. (Pubitemid 32281351)
    • (2001) AIDS , vol.15 , Issue.5 , pp. 571-575
    • Nebuloni, M.1    Pellegrinelli, A.2    Ferri, A.3    Bonetto, S.4    Boldorini, R.5    Vago, L.6    Grassi, M.P.7    Costanzi, G.8
  • 123
    • 0032504151 scopus 로고    scopus 로고
    • HIV-1 Tat induces neuronal death via tumor necrosis factor-α and activation of non-N-methyl-D-aspartate receptors by a NFκB-independent mechanism
    • DOI 10.1074/jbc.273.28.17852
    • New DR, Maggirwar SB, Epstein LG, Dewhurst S, Gelbard HA, (1998) HIV-1 Tat induces neuronal death via tumor necrosis factor-alpha and activation of non-N-methyl-D-aspartate receptors by a NFkappaB-independent mechanism. J Biol Chem 273: 17852-17858. (Pubitemid 28355131)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.28 , pp. 17852-17858
    • New, D.R.1    Maggirwar, S.B.2    Epstein, L.G.3    Dewhurst, S.4    Gelbard, H.A.5
  • 124
    • 76149101291 scopus 로고    scopus 로고
    • Persistent hijacking of brain proteasomes in HIV-associated dementia
    • Nguyen TP, Soukup VM, Gelman BB, (2010) Persistent hijacking of brain proteasomes in HIV-associated dementia. Am J Pathol 176: 893-902.
    • (2010) Am J Pathol , vol.176 , pp. 893-902
    • Nguyen, T.P.1    Soukup, V.M.2    Gelman, B.B.3
  • 125
    • 38349046973 scopus 로고    scopus 로고
    • Autophagy, amyloidogenesis and Alzheimer disease
    • (Pt 23).
    • Nixon RA, (2007) Autophagy, amyloidogenesis and Alzheimer disease. J Cell Sci 120 (Pt 23): 4081-4091.
    • (2007) J Cell Sci , vol.120 , pp. 4081-4091
    • Nixon, R.A.1
  • 126
    • 33747388358 scopus 로고    scopus 로고
    • Lysosomal system pathways: Genes to neurodegeneration in Alzheimer's disease
    • Nixon RA, Cataldo AM, (2006) Lysosomal system pathways: genes to neurodegeneration in Alzheimer's disease. J Alzheimers Dis 9 (3 Suppl.): 277-289. (Pubitemid 44253321)
    • (2006) Journal of Alzheimer's Disease , vol.9 , Issue.SUPPL. 3 , pp. 277-289
    • Nixon, R.A.1    Cataldo, A.M.2
  • 128
    • 51549086469 scopus 로고    scopus 로고
    • Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement
    • Pan T, Kondo S, Zhu W, Xie W, Jankovic J, Le W, (2008) Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement. Neurobiol Dis 32: 16-25.
    • (2008) Neurobiol Dis , vol.32 , pp. 16-25
    • Pan, T.1    Kondo, S.2    Zhu, W.3    Xie, W.4    Jankovic, J.5    Le, W.6
  • 129
    • 79953666757 scopus 로고    scopus 로고
    • Increased CDK5 expression in HIV encephalitis contributes to neurodegeneration via tau phosphorylation and is reversed with Roscovitine
    • Patrick C, Crews L, Desplats P, Dumaop W, Rockenstein E, Achim CL, et al, (2011) Increased CDK5 expression in HIV encephalitis contributes to neurodegeneration via tau phosphorylation and is reversed with Roscovitine. Am J Pathol 178: 1646-1661.
    • (2011) Am J Pathol , vol.178 , pp. 1646-1661
    • Patrick, C.1    Crews, L.2    Desplats, P.3    Dumaop, W.4    Rockenstein, E.5    Achim, C.L.6
  • 133
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B, Duden R, Rubinsztein DC, (2002) Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet 11: 1107-1117. (Pubitemid 34521091)
    • (2002) Human Molecular Genetics , vol.11 , Issue.9 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 136
    • 15744363144 scopus 로고    scopus 로고
    • HIV-1 Tat inhibits neprilysin and elevates amyloid β
    • Rempel HC, Pulliam L, (2005) HIV-1 Tat inhibits neprilysin and elevates amyloid beta. AIDS 19: 127-135. (Pubitemid 40409531)
    • (2005) AIDS , vol.19 , Issue.2 , pp. 127-135
    • Rempel, H.C.1    Pulliam, L.2
  • 138
    • 77953194507 scopus 로고    scopus 로고
    • TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97
    • Ritson GP, Custer SK, Freibaum BD, Guinto JB, Geffel D, Moore J, et al, (2010) TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97. J Neurosci 30: 7729-7739.
    • (2010) J Neurosci , vol.30 , pp. 7729-7739
    • Ritson, G.P.1    Custer, S.K.2    Freibaum, B.D.3    Guinto, J.B.4    Geffel, D.5    Moore, J.6
  • 141
    • 44349133382 scopus 로고    scopus 로고
    • ESCRT functions in autophagy and associated disease
    • Rusten TE, Simonsen A, (2008) ESCRT functions in autophagy and associated disease. Cell Cycle 7: 1166-1172. (Pubitemid 351749268)
    • (2008) Cell Cycle , vol.7 , Issue.9 , pp. 1166-1172
    • Rusten, T.E.1    Simonsen, A.2
  • 142
    • 0036948147 scopus 로고    scopus 로고
    • The epidemiology of human immunodeficiency virus-associated neurological disease in the era of highly active antiretroviral therapy
    • DOI 10.1080/13550280290101094
    • Sacktor N, (2002) The epidemiology of human immunodeficiency virus-associated neurological disease in the era of highly active antiretroviral therapy. J Neurovirol 8 (Suppl. 2): 115-121. (Pubitemid 36097787)
    • (2002) Journal of NeuroVirology , vol.8 , Issue.SUPPL. 2 , pp. 115-121
    • Sacktor, N.1
  • 144
    • 49749096430 scopus 로고    scopus 로고
    • Small molecule enhancers of autophagy for neurodegenerative diseases
    • Sarkar S, Rubinsztein DC, (2008) Small molecule enhancers of autophagy for neurodegenerative diseases. Mol Biosyst 4: 895-901.
    • (2008) Mol Biosyst , vol.4 , pp. 895-901
    • Sarkar, S.1    Rubinsztein, D.C.2
  • 145
    • 0029972129 scopus 로고    scopus 로고
    • Effect of alkalizing agents on the processing of the β-amyloid precursor protein
    • DOI 10.1016/0006-8993(96)00002-9
    • Schrader-Fischer G, Paganetti PA, (1996) Effect of alkalizing agents on the processing of the beta-amyloid precursor protein. Brain Res 716: 91-100. (Pubitemid 26155223)
    • (1996) Brain Research , vol.716 , Issue.1-2 , pp. 91-100
    • Schrader-Fischer, G.1    Paganetti, P.A.2
  • 146
    • 80052761906 scopus 로고    scopus 로고
    • Neurocognitive consequences of HIV infection in older adults: An evaluation of the "cortical" hypothesis
    • Scott JC, Woods SP, Carey CL, Weber E, Bondi MW, Grant I, (2011) Neurocognitive consequences of HIV infection in older adults: an evaluation of the "cortical" hypothesis. AIDS Behav 15: 1187-1196.
    • (2011) AIDS Behav , vol.15 , pp. 1187-1196
    • Scott, J.C.1    Woods, S.P.2    Carey, C.L.3    Weber, E.4    Bondi, M.W.5    Grant, I.6
  • 148
    • 51549106105 scopus 로고    scopus 로고
    • Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species
    • Sevlever D, Jiang P, Yen SH, (2008) Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species. Biochemistry 47: 9678-9687.
    • (2008) Biochemistry , vol.47 , pp. 9678-9687
    • Sevlever, D.1    Jiang, P.2    Yen, S.H.3
  • 150
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • DOI 10.1126/science.1099993
    • Shintani T, Klionsky DJ, (2004) Autophagy in health and disease: a double-edged sword. Science 306: 990-995. (Pubitemid 39482894)
    • (2004) Science , vol.306 , Issue.5698 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 153
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • Spencer B, Potkar R, Trejo M, Rockenstein E, Patrick C, Gindi R, et al, (2009) Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases. J Neurosci 29: 13578-13588.
    • (2009) J Neurosci , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6
  • 154
    • 77956305343 scopus 로고    scopus 로고
    • Inhibition of mTOR by rapamycin abolishes cognitive deficits and reduces amyloid-beta levels in a mouse model of Alzheimer's disease
    • Spilman P, Podlutskaya N, Hart MJ, Debnath J, Gorostiza O, Bredesen D, et al, (2010) Inhibition of mTOR by rapamycin abolishes cognitive deficits and reduces amyloid-beta levels in a mouse model of Alzheimer's disease. PLoS ONE 5: e9979.
    • (2010) PLoS ONE , vol.5
    • Spilman, P.1    Podlutskaya, N.2    Hart, M.J.3    Debnath, J.4    Gorostiza, O.5    Bredesen, D.6
  • 155
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type α-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L, Larsen KE, Rideout HJ, Sulzer D, Greene LA, (2001) Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J Neurosci 21: 9549-9560. (Pubitemid 34184043)
    • (2001) Journal of Neuroscience , vol.21 , Issue.24 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 156
    • 55949089475 scopus 로고    scopus 로고
    • TDP-43 in cerebrospinal fluid of patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Steinacker P, Hendrich C, Sperfeld AD, Jesse S, von Arnim CA, Lehnert S, et al, (2008) TDP-43 in cerebrospinal fluid of patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Arch Neurol 65: 1481-1487.
    • (2008) Arch Neurol , vol.65 , pp. 1481-1487
    • Steinacker, P.1    Hendrich, C.2    Sperfeld, A.D.3    Jesse, S.4    Von Arnim, C.A.5    Lehnert, S.6
  • 159
    • 0031661141 scopus 로고    scopus 로고
    • Abnormal distribution of the non-Aβ component of Alzheimer's disease amyloid precursor/α-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment
    • Takeda A, Hashimoto M, Mallory M, Sundsmo M, Hansen L, Sisk A, Masliah E, (1998) Abnormal distribution of the non-Ab component of Alzheimer's disease amyloid precursor/a-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment. Lab Invest 78: 1169-1177. (Pubitemid 28440832)
    • (1998) Laboratory Investigation , vol.78 , Issue.9 , pp. 1169-1177
    • Takeda, A.1    Hashimoto, M.2    Mallory, M.3    Sundsumo, M.4    Hansen, L.5    Sisk, A.6    Masliah, E.7
  • 161
    • 0028009187 scopus 로고
    • Central nervous system damage produced by expression of the HIV-1 coat protein gp120 in transgenic mice
    • DOI 10.1038/367188a0
    • Toggas SM, Masliah E, Rockenstein EM, Rall GF, Abraham CR, Mucke L, (1994) Central nervous system damage produced by expression of the HIV-1 coat protein gp120 in transgenic mice. Nature 367: 188-193. (Pubitemid 24031702)
    • (1994) Nature , vol.367 , Issue.6459 , pp. 188-193
    • Toggas, S.M.1    Masliah, E.2    Rockenstein, E.M.3    Rall, G.F.4    Abraham, C.R.5    Mucke, L.6
  • 162
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
    • Tresse E, Salomons FA, Vesa J, Bott LC, Kimonis V, Yao TP, et al, (2010) VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6: 217-227.
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6
  • 163
    • 52349111812 scopus 로고    scopus 로고
    • Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases
    • Tsigelny IF, Crews L, Desplats P, Shaked GM, Sharikov Y, Mizuno H, et al, (2008) Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases. PLoS ONE 3: e3135.
    • (2008) PLoS ONE , vol.3
    • Tsigelny, I.F.1    Crews, L.2    Desplats, P.3    Shaked, G.M.4    Sharikov, Y.5    Mizuno, H.6
  • 165
    • 66849101994 scopus 로고    scopus 로고
    • Aging with HIV. Lessons from CROI 2009
    • Valcour V, (2009) Aging with HIV. Lessons from CROI 2009. Posit Aware 20: 37-39.
    • (2009) Posit Aware , vol.20 , pp. 37-39
    • Valcour, V.1
  • 166
    • 33646447195 scopus 로고    scopus 로고
    • HIV infection and dementia in older adults
    • Valcour V, Paul R, (2006) HIV infection and dementia in older adults. Clin Infect Dis 42: 1449-1454.
    • (2006) Clin Infect Dis , vol.42 , pp. 1449-1454
    • Valcour, V.1    Paul, R.2
  • 167
    • 9244257382 scopus 로고    scopus 로고
    • HIV-associated dementia, mitochondrial dysfunction, and oxidative stress
    • DOI 10.1016/j.mito.2004.05.009, PII S156772490400087X
    • Valcour V, Shiramizu B, (2004) HIV-associated dementia, mitochondrial dysfunction, and oxidative stress. Mitochondrion 4: 119-129. (Pubitemid 39549801)
    • (2004) Mitochondrion , vol.4 , Issue.2-3 , pp. 119-129
    • Valcour, V.1    Shiramizu, B.2
  • 168
  • 170
    • 37849023471 scopus 로고    scopus 로고
    • CHMP2B C-truncating mutations in frontotemporal lobar degeneration are associated with an aberrant endosomal phenotype in vitro
    • van der Zee J, Urwin H, Engelborghs S, Bruyland M, Vandenberghe R, Dermaut B, et al, (2008) CHMP2B C-truncating mutations in frontotemporal lobar degeneration are associated with an aberrant endosomal phenotype in vitro. Hum Mol Genet 17: 313-322.
    • (2008) Hum Mol Genet , vol.17 , pp. 313-322
    • Van Der Zee, J.1    Urwin, H.2    Engelborghs, S.3    Bruyland, M.4    Vandenberghe, R.5    Dermaut, B.6
  • 172
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of α-Synuclein and its mechanism of neurotoxicity in Parkinson's disease
    • DOI 10.1021/bi030086j
    • Volles MJ, Lansbury PT Jr, (2003) Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry 42: 7871-7878. (Pubitemid 36807703)
    • (2003) Biochemistry , vol.42 , Issue.26 , pp. 7871-7878
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 173
    • 33746108503 scopus 로고    scopus 로고
    • Cellular pathology in multiple system atrophy
    • DOI 10.1111/j.1440-1789.2006.00713.x
    • Wakabayashi K, Takahashi H, (2006) Cellular pathology in multiple system atrophy. Neuropathology 26: 338-345. (Pubitemid 44086838)
    • (2006) Neuropathology , vol.26 , Issue.4 , pp. 338-345
    • Wakabayashi, K.1    Takahashi, H.2
  • 174
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers in the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • DOI 10.2174/0929866043407174
    • Walsh DM, Selkoe DJ, (2004) Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett 11: 213-228. (Pubitemid 38689025)
    • (2004) Protein and Peptide Letters , vol.11 , Issue.3 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 175
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers- A decade of discovery
    • Walsh DM, Selkoe DJ, (2007) A beta oligomers-a decade of discovery. J Neurochem 101: 1172-1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 176
    • 30344448866 scopus 로고    scopus 로고
    • Involvement of α1β1 integrin in insulin-like growth factor-1-mediated protection of PC12 neuronal processes from tumor necrosis factor-α-induced injury
    • DOI 10.1002/jnr.20712
    • Wang JY, Grabacka M, Marcinkiewicz C, Staniszewska I, Peruzzi F, Khalili K, et al, (2006) Involvement of alpha1beta1 integrin in insulin-like growth factor-1-mediated protection of PC12 neuronal processes from tumor necrosis factor-alpha-induced injury. J Neurosci Res 83: 7-18. (Pubitemid 43062005)
    • (2006) Journal of Neuroscience Research , vol.83 , Issue.1 , pp. 7-18
    • Wang, J.Y.1    Grabacka, M.2    Marcinkiewicz, C.3    Staniszewska, I.4    Peruzzi, F.5    Khalili, K.6    Amini, S.7    Reiss, K.8
  • 178
    • 67349090057 scopus 로고    scopus 로고
    • Valosin-containing protein disease: Inclusion body myopathy with Paget's disease of the bone and fronto-temporal dementia
    • Weihl CC, Pestronk A, Kimonis VE, (2009) Valosin-containing protein disease: inclusion body myopathy with Paget's disease of the bone and fronto-temporal dementia. Neuromuscul Disord 19: 308-315.
    • (2009) Neuromuscul Disord , vol.19 , pp. 308-315
    • Weihl, C.C.1    Pestronk, A.2    Kimonis, V.E.3
  • 179
    • 0030005329 scopus 로고    scopus 로고
    • Expression of HIV regulatory and structural mRNA in the central nervous system
    • Wiley CA, Baldwin M, Achim CL, (1996) Expression of HIV regulatory and structural mRNA in the central nervous system. AIDS 10: 843-847. (Pubitemid 26229512)
    • (1996) AIDS , vol.10 , Issue.8 , pp. 843-847
    • Wiley Maria Baldwin, C.A.1    Achim, C.L.2
  • 180
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri M, Vogiatzi T, Vekrellis K, Park D, Stefanis L, (2009) Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS ONE 4: e5515.
    • (2009) PLoS ONE , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5
  • 181
    • 60549099349 scopus 로고    scopus 로고
    • HIV-1 gp120 induces cytokine expression, leukocyte adhesion, and transmigration across the blood-brain barrier: Modulatory effects of STAT1 signaling
    • Yang B, Akhter S, Chaudhuri A, Kanmogne GD, (2009) HIV-1 gp120 induces cytokine expression, leukocyte adhesion, and transmigration across the blood-brain barrier: modulatory effects of STAT1 signaling. Microvasc Res 77: 212-219.
    • (2009) Microvasc Res , vol.77 , pp. 212-219
    • Yang, B.1    Akhter, S.2    Chaudhuri, A.3    Kanmogne, G.D.4
  • 182
    • 34648813113 scopus 로고    scopus 로고
    • Multiple system atrophy: α-synuclein and neuronal degeneration
    • DOI 10.1111/j.1440-1789.2007.00841.x
    • Yoshida M, (2007) Multiple system atrophy: alpha-synuclein and neuronal degeneration. Neuropathology 27: 484-493. (Pubitemid 47459721)
    • (2007) Neuropathology , vol.27 , Issue.5 , pp. 484-493
    • Yoshida, M.1
  • 183
    • 4344689871 scopus 로고    scopus 로고
    • Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: Implications for β-amyloid peptide over-production and localization in Alzheimer's disease
    • DOI 10.1016/j.biocel.2004.05.010, PII S1357272504002316
    • Yu WH, Kumar A, Peterhoff C, Shapiro Kulnane L, Uchiyama Y, Lamb BT, et al, (2004) Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for beta-amyloid peptide over-production and localization in Alzheimer's disease. Int J Biochem Cell Biol 36: 2531-2540. (Pubitemid 39119764)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.12 , pp. 2531-2540
    • Yu, W.H.1    Kumar, A.2    Peterhoff, C.3    Shapiro Kulnane, L.4    Uchiyama, Y.5    Lamb, B.T.6    Cuervo, A.M.7    Nixon, R.A.8
  • 185
    • 0037194894 scopus 로고    scopus 로고
    • A novel protein complex linking the delta 2 glutamate receptor and autophagy: Implications for neurodegeneration in lurcher mice
    • Yue Z, Horton A, Bravin M, DeJager PL, Selimi F, Heintz N, (2002) A novel protein complex linking the delta 2 glutamate receptor and autophagy: implications for neurodegeneration in lurcher mice. Neuron 35: 921-933.
    • (2002) Neuron , vol.35 , pp. 921-933
    • Yue, Z.1    Horton, A.2    Bravin, M.3    Dejager, P.L.4    Selimi, F.5    Heintz, N.6
  • 187
    • 32244442749 scopus 로고    scopus 로고
    • Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking
    • DOI 10.1242/jcs.02735
    • Zeng X, Overmeyer JH, Maltese WA, (2006) Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking. J Cell Sci 119 (Pt 2): 259-270. (Pubitemid 43210695)
    • (2006) Journal of Cell Science , vol.119 , Issue.2 , pp. 259-270
    • Zeng, X.1    Overmeyer, J.H.2    Maltese, W.A.3
  • 189
    • 69449085474 scopus 로고    scopus 로고
    • Atg14L and Rubicon: Yin and yang of Beclin 1-mediated autophagy control
    • Zhong Y, Wang QJ, Yue Z, (2009) Atg14L and Rubicon: yin and yang of Beclin 1-mediated autophagy control. Autophagy 5: 890-891.
    • (2009) Autophagy , vol.5 , pp. 890-891
    • Zhong, Y.1    Wang, Q.J.2    Yue, Z.3
  • 190
    • 79956204926 scopus 로고    scopus 로고
    • Autophagy is increased in postmortem brains of persons with HIV-1-associated encephalitis
    • Zhou D, Masliah E, Spector SA, (2011) Autophagy is increased in postmortem brains of persons with HIV-1-associated encephalitis. J Infect Dis 203: 1647-1657.
    • (2011) J Infect Dis , vol.203 , pp. 1647-1657
    • Zhou, D.1    Masliah, E.2    Spector, S.A.3
  • 191
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death
    • DOI 10.2353/ajpath.2007.060524
    • Zhu JH, Horbinski C, Guo F, Watkins S, Uchiyama Y, Chu CT, (2007) Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death. Am J Pathol 170: 75-86. (Pubitemid 47339191)
    • (2007) American Journal of Pathology , vol.170 , Issue.1 , pp. 75-86
    • Zhu, J.-H.1    Horbinski, C.2    Guo, F.3    Watkins, S.4    Uchiyama, Y.5    Chu, C.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.