메뉴 건너뛰기




Volumn 42, Issue , 2014, Pages S153-S162

Golgi apparatus and protein trafficking in Alzheimer's disease

Author keywords

Alzheimer's disease; electron microscopy; Golgi apparatus; proteins trafficking

Indexed keywords

PROTEIN AGGREGATE; TAU PROTEIN; AMYLOID BETA PROTEIN;

EID: 84920587931     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-132660     Document Type: Conference Paper
Times cited : (32)

References (82)
  • 1
    • 0014313861 scopus 로고
    • The association between quantitative measures of dementia and of senile change in the cerebral gray matter of elderly subjects
    • Blessed G, Tomlinson BE, Roth M (1968) The association between quantitative measures of dementia and of senile change in the cerebral gray matter of elderly subjects. Br J Psychiatry 114, 797-811.
    • (1968) Br J Psychiatry , vol.114 , pp. 797-811
    • Blessed, G.1    Tomlinson, B.E.2    Roth, M.3
  • 2
    • 0033302352 scopus 로고    scopus 로고
    • The diagnosis of Alzheimer's disease
    • Villareal DT, Morris JC (1999) The diagnosis of Alzheimer's disease. J Alzheimers Dis 1, 249-263.
    • (1999) J Alzheimers Dis , vol.1 , pp. 249-263
    • Villareal, D.T.1    Morris, J.C.2
  • 3
    • 3042857903 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Cummings JL (2004) Alzheimer's disease. N Engl J Med 351, 56-67.
    • (2004) N Engl J Med , vol.351 , pp. 56-67
    • Cummings, J.L.1
  • 4
    • 0031978246 scopus 로고    scopus 로고
    • Temporal memory for remote events in healthy aging and dementia
    • Storandt M, Kaskie B, Von Dras DD (1998) Temporal memory for remote events in healthy aging and dementia. Psychol Aging 13, 4-7.
    • (1998) Psychol Aging , vol.13 , pp. 4-7
    • Storandt, M.1    Kaskie, B.2    Von Dras, D.D.3
  • 5
    • 0027994752 scopus 로고
    • Prevalence of depression in Alzheimer disease and validity of research diagnostic criteria
    • Vida S, Des Rosiers P, Carrier L, Gauthier S (1994) Prevalence of depression in Alzheimer disease and validity of research diagnostic criteria. J Geriatr Psychiatry Neurol 7, 238-244.
    • (1994) J Geriatr Psychiatry Neurol , vol.7 , pp. 238-244
    • Vida, S.1    Des Rosiers, P.2    Carrier, L.3    Gauthier, S.4
  • 7
    • 0030024379 scopus 로고    scopus 로고
    • Apathy and loss of insight in Alzheimer disease: A SPECT imaging study
    • Ott BR, Noto RB, Fogel BS (1996) Apathy and loss of insight in Alzheimer disease: A SPECT imaging study. J Neuropsychiatr Clin Neurosci 8, 41-46.
    • (1996) J Neuropsychiatr Clin Neurosci , vol.8 , pp. 41-46
    • Ott, B.R.1    Noto, R.B.2    Fogel, B.S.3
  • 9
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA (1992) Alzheimer's disease: The amyloid cascade hypothesis. Science 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 10
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer related changes
    • Braak H, Braak E (1991) Neuropathological stageing of Alzheimer related changes. Acta Neuropathol 82, 239-259.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 11
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDAWork Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
    • McKhann G, Drachman D, Folstein M, Katzman R, Price D, Stadlan EM (1984) Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDAWork Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease. Neurology 34, 939-944.
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 12
    • 0022414054 scopus 로고
    • Diagnosis of Alzheimer's disease
    • Khachaturian ZS (1985) Diagnosis of Alzheimer's disease. Arch Neurol 42, 1097-1105.
    • (1985) Arch Neurol , vol.42 , pp. 1097-1105
    • Khachaturian, Z.S.1
  • 13
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW (1984) Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120, 885-890.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 15
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297, 353.
    • (2002) Science , vol.297 , pp. 353
    • Hardy, J.1    Selkoe, D.J.2
  • 16
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
    • Selkoe DJ (2004) Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases. Nat Cell Biol 6, 154-161.
    • (2004) Nat Cell Biol , vol.6 , pp. 154-161
    • Selkoe, D.J.1
  • 20
    • 0005135719 scopus 로고    scopus 로고
    • Oxidative stress and mitochondria alterations in Alzheimer's disease
    • Baloyannis SJ (2000) Oxidative stress and mitochondria alterations in Alzheimer's disease. Neurobiol Aging 21, 264.
    • (2000) Neurobiol Aging , vol.21 , pp. 264
    • Baloyannis, S.J.1
  • 21
    • 0342615480 scopus 로고    scopus 로고
    • Mitochondrial alterations in Alzheimer's disease
    • Baloyannis SJ (1998) Mitochondrial alterations in Alzheimer's disease Neurobiol Aging 19, S241.
    • (1998) Neurobiol Aging , vol.19 , pp. S241
    • Baloyannis, S.J.1
  • 23
    • 84920566698 scopus 로고    scopus 로고
    • Alterations of mitochondria and golgi apparatus are related to synaptic pathology in Alzheimer's disease
    • Kishore U, ed. In Tech, Rijeka
    • Baloyannis SJ (2013) Alterations of mitochondria and golgi apparatus are related to synaptic pathology in Alzheimer's disease. In Neurodegenerative Diseases, Kishore U, ed. In Tech, Rijeka, pp. 101-123.
    • (2013) Neurodegenerative Diseases , pp. 101-123
    • Baloyannis, S.J.1
  • 24
    • 0027477946 scopus 로고
    • Do defects in mitochondrial energy metabolism underlie the pathology of neurodegenerative diseases?
    • Beal M, Hyman B, Koroshetz W (1993) Do defects in mitochondrial energy metabolism underlie the pathology of neurodegenerative diseases? Trends Neurosci 16, 125-131.
    • (1993) Trends Neurosci , vol.16 , pp. 125-131
    • Beal, M.1    Hyman, B.2    Koroshetz, W.3
  • 25
    • 0032504710 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • Beal M (1998) Mitochondrial dysfunction in neurodegenerative diseases. Biochim Biophys Acta 1366, 211-223.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 211-223
    • Beal, M.1
  • 27
    • 0027949202 scopus 로고
    • Oxidative damage and mitochondrial decay in aging
    • Shigenaga M, Hagen T, Ames B (1994) Oxidative damage and mitochondrial decay in aging. Proc Natl Acad Sci USA 91, 10771-10778.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10771-10778
    • Shigenaga, M.1    Hagen, T.2    Ames, B.3
  • 29
    • 33746256557 scopus 로고    scopus 로고
    • Mitochondrial alterations in Alzheimer's disease
    • Baloyannis SJ (2006) Mitochondrial alterations in Alzheimer's disease. J Alzheimers Dis 9, 119-126.
    • (2006) J Alzheimers Dis , vol.9 , pp. 119-126
    • Baloyannis, S.J.1
  • 32
    • 0030043292 scopus 로고    scopus 로고
    • In Alzheimer's disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic
    • Stieber A, Mourelatos Z, Gonatas NK (1996) In Alzheimer's disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic. Am J Pathol 148, 415-426.
    • (1996) Am J Pathol , vol.148 , pp. 415-426
    • Stieber, A.1    Mourelatos, Z.2    Gonatas, N.K.3
  • 33
    • 1942486075 scopus 로고    scopus 로고
    • The Golgi apparatus of Purkinje cells in Alzheimer's disease
    • Bohl J, ed. Shaker Vertag, Aachen
    • Baloyannis S (2002) The Golgi apparatus of Purkinje cells in Alzheimer's disease. In Neuropathology Back to the Roots, Bohl J, ed. Shaker Vertag, Aachen, pp. 1-10.
    • (2002) Neuropathology Back to the Roots , pp. 1-10
    • Baloyannis, S.1
  • 34
    • 0020313889 scopus 로고
    • Evidence that all newly synthesized proteins destined for fast axonal transport pass through the Golgi apparatus
    • Hammerschlag R, Stone GC, Bolen FA, Lindsey JD, Ellisman MH (1982) Evidence that all newly synthesized proteins destined for fast axonal transport pass through the Golgi apparatus. J Cell Biol 93, 568-575.
    • (1982) J Cell Biol , vol.93 , pp. 568-575
    • Hammerschlag, R.1    Stone, G.C.2    Bolen, F.A.3    Lindsey, J.D.4    Ellisman, M.H.5
  • 35
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran G, Koo EH (2008) Amyloid precursor protein trafficking, processing, and function. J Biol Chem 283, 29615-29619.
    • (2008) J Biol Chem , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 36
    • 0027389118 scopus 로고
    • Identification of the Alzheimer beta/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells
    • Nordstedt C, Caporaso GL, Thyberg J, Gandy SE, Greengard P (1993) Identification of the Alzheimer beta/A4 amyloid precursor protein in clathrin-coated vesicles purified from PC12 cells. J Biol Chem 268, 608-612.
    • (1993) J Biol Chem , vol.268 , pp. 608-612
    • Nordstedt, C.1    Caporaso, G.L.2    Thyberg, J.3    Gandy, S.E.4    Greengard, P.5
  • 37
    • 0030590225 scopus 로고    scopus 로고
    • Purkinje cell loss and astrocytosis in the cerebellum in familial and sporadic Alzheimer's disease
    • FukutaniY, Cairns NJ, RossorMN,LantosPL(1996) Purkinje cell loss and astrocytosis in the cerebellum in familial and sporadic Alzheimer's disease. Neurosci Lett 214, 33-36.
    • (1996) Neurosci Lett , vol.214 , pp. 33-36
    • Fukutani, Y.1    Cairns, N.J.2    Rossor, M.N.3    Lantos, P.L.4
  • 41
    • 0025908356 scopus 로고
    • The consortium to establish a registry for Alzheimer's disease (CERAD): Part II Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, Sumi SM, Crain BJ, Brownlee LM, Vogel FS, Hughes JP, van Belle G, Berg L (1991) The consortium to establish a registry for Alzheimer's disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 41, 479-486.
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6    Vogel, F.S.7    Hughes, J.P.8    Van Belle, G.9    Berg, L.10
  • 42
    • 0029056590 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD Part X. Neuropathology confirmation of the clinical diagnosis of Alzheimer's disease
    • Mirra GM, Hedreen SS, Sumi JC, Hansen SM, Heyman LA, A (1995) The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part X. Neuropathology confirmation of the clinical diagnosis of Alzheimer's disease. Neurology 45, 461-466.
    • (1995) Neurology , vol.45 , pp. 461-466
    • Mirra, G.M.1    Hedreen, S.S.2    Sumi, J.C.3    Hansen, S.M.4    Heyman, L.A.A.5
  • 43
    • 0031255112 scopus 로고    scopus 로고
    • Consensus recommendations for the postmortem diagnosis of Alzheimer disease from the National Institute on Aging and the Reagan InstituteWorking Group on diagnostic criteria for the neuropathological assessment of Alzheimer disease
    • Hyman BT, Trojanowski JQ (1997) Consensus recommendations for the postmortem diagnosis of Alzheimer disease from the National Institute on Aging and the Reagan InstituteWorking Group on diagnostic criteria for the neuropathological assessment of Alzheimer disease. J Neuropathol Exp Neurol 56, 1095-1097.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 1095-1097
    • Hyman, B.T.1    Trojanowski, J.Q.2
  • 45
    • 0033623415 scopus 로고    scopus 로고
    • Aβ-generating enzymes: Recent advances in β-and β-secretase research
    • Vassar R, Citron M (2000) Aβ-generating enzymes: Recent advances in β-and β-secretase research. Neuron 27, 419-422.
    • (2000) Neuron , vol.27 , pp. 419-422
    • Vassar, R.1    Citron, M.2
  • 48
    • 0037117753 scopus 로고    scopus 로고
    • Structure-activity relationship of hydroxamate-based inhibitors on the secretases that cleave the amyloid precursor protein, angiotensin converting enzyme, CD23, and pro-tumor necrosis factor
    • Parkin ET, Trew A, Christie G, Faller A, Mayer R, Turner AJ, Hooper NM (2002) Structure-activity relationship of hydroxamate-based inhibitors on the secretases that cleave the amyloid precursor protein, angiotensin converting enzyme, CD23, and pro-tumor necrosis factor-. Biochemistry 41, 4972-4981.
    • (2002) Biochemistry , vol.41 , pp. 4972-4981
    • Parkin, E.T.1    Trew, A.2    Christie, G.3    Faller, A.4    Mayer, R.5    Turner, A.J.6    Hooper, N.M.7
  • 49
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze MD, Bitan G, Teplow DB (2002) Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J Neurosci Res 69, 567-577.
    • (2002) J Neurosci Res , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 50
    • 0035057838 scopus 로고    scopus 로고
    • Dissection of receptor folding and ligand-binding property with functional minireceptors of LDL receptor-related protein
    • Obermoeller-McCormick LM, Li Y, Osaka H, FitzGerald DJ, Schwartz AL, Bu G (2001) Dissection of receptor folding and ligand-binding property with functional minireceptors of LDL receptor-related protein. J Cell Sci 114, 899-908.
    • (2001) J Cell Sci , vol.114 , pp. 899-908
    • Obermoeller-Mccormick, L.M.1    Li, Y.2    Osaka, H.3    Fitzgerald, D.J.4    Schwartz, A.L.5    Bu, G.6
  • 51
    • 34248202513 scopus 로고    scopus 로고
    • Modulation ofβ-amyloid precursor protein trafficking and processing by the low density lipoprotein receptor family
    • CamJA,BuG(2006) Modulation ofβ-amyloid precursor protein trafficking and processing by the low density lipoprotein receptor family. Mol Neurodegener 1, 8.
    • (2006) Mol Neurodegener , vol.1 , pp. 8
    • Cam, J.A.1    Bu, G.2
  • 52
    • 0035914457 scopus 로고    scopus 로고
    • Recognition of alpha 2-macroglobulin by the low density lipoprotein receptor-related protein requires the cooperation of two ligand binding cluster regions
    • Mikhailenko I, Battey FD, Migliorini M, Ruiz JF, Argraves K, Moayeri M, Strickland DK (2001) Recognition of alpha 2-macroglobulin by the low density lipoprotein receptor-related protein requires the cooperation of two ligand binding cluster regions. J Biol Chem 276, 39484-39491.
    • (2001) J Biol Chem , vol.276 , pp. 39484-39491
    • Mikhailenko, I.1    Battey, F.D.2    Migliorini, M.3    Ruiz, J.F.4    Argraves, K.5    Moayeri, M.6    Strickland, D.K.7
  • 56
    • 0035116513 scopus 로고    scopus 로고
    • Presenilin-1 mutations reduce cytoskeletal association, deregulate neurite growth, and potentiate neuronal dystrophy and tau phosphorylation
    • Pigino G, Pelsman A, Mori H, Busciglio J (2001) Presenilin-1 mutations reduce cytoskeletal association, deregulate neurite growth, and potentiate neuronal dystrophy and tau phosphorylation. J Neurosci 21, 834-842.
    • (2001) J Neurosci , vol.21 , pp. 834-842
    • Pigino, G.1    Pelsman, A.2    Mori, H.3    Busciglio, J.4
  • 58
    • 0029807018 scopus 로고    scopus 로고
    • The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones
    • Uchida N, Honjo Y, Johnson KR, Wheelock MJ, Takeichi M (1996) The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones. J Cell Biol 135, 767-779.
    • (1996) J Cell Biol , vol.135 , pp. 767-779
    • Uchida, N.1    Honjo, Y.2    Johnson, K.R.3    Wheelock, M.J.4    Takeichi, M.5
  • 60
    • 0038721956 scopus 로고    scopus 로고
    • The overexpression of the wild type or mutant forms of the presenilin-1 protein alters glycoprotein processing in a human neuroblastoma cell line
    • Farquhar MJ, Gray CW, Breen KC (2003) The overexpression of the wild type or mutant forms of the presenilin-1 protein alters glycoprotein processing in a human neuroblastoma cell line. Neurosci Lett 346, 53-56.
    • (2003) Neurosci Lett , vol.346 , pp. 53-56
    • Farquhar, M.J.1    Gray, C.W.2    Breen, K.C.3
  • 62
    • 36849001215 scopus 로고    scopus 로고
    • β-Galactoside-2,6-sialyltransferase i cleavage by BACE1 enhances the sialylation of soluble glycoproteins. A novel regulatory mechanism for-2,6-sialylation
    • Sugimoto I, Futakawa S, Oka R, Ogawa K, Marth JD, Miyoshi E, Taniguchi N, Hashimoto Y, Kitazume S (2007) β-Galactoside-2,6-sialyltransferase I cleavage by BACE1 enhances the sialylation of soluble glycoproteins. A novel regulatory mechanism for-2,6-sialylation. J Biol Chem 282, 34896-34903.
    • (2007) J Biol Chem , vol.282 , pp. 34896-34903
    • Sugimoto, I.1    Futakawa, S.2    Oka, R.3    Ogawa, K.4    Marth, J.D.5    Miyoshi, E.6    Taniguchi, N.7    Hashimoto, Y.8    Kitazume, S.9
  • 63
    • 84891836688 scopus 로고    scopus 로고
    • The role of protein glycosylation in Alzheimer disease
    • Schedin-Weiss S, Winblad B, Tjernberg LO (2014) The role of protein glycosylation in Alzheimer disease. FEBS J 281, 46-62.
    • (2014) FEBS J , vol.281 , pp. 46-62
    • Schedin-Weiss, S.1    Winblad, B.2    Tjernberg, L.O.3
  • 64
    • 0031975699 scopus 로고    scopus 로고
    • The Golgi apparatus: 100 years of progress and controversy
    • Farquhar MG, Palade GE (1998) The Golgi apparatus: 100 years of progress and controversy. Trends Cell Biol 8, 2-10.
    • (1998) Trends Cell Biol , vol.8 , pp. 2-10
    • Farquhar, M.G.1    Palade, G.E.2
  • 65
    • 0032974408 scopus 로고    scopus 로고
    • The role of the protein glycosylation state in the control of cellular transport of the amyloid-precursor protein
    • McFarlane I, Georgopoulou N, Coughlan CM, Gillian AM, Breen KC (1999) The role of the protein glycosylation state in the control of cellular transport of the amyloid-precursor protein. Neuroscience 90, 15-25.
    • (1999) Neuroscience , vol.90 , pp. 15-25
    • McFarlane, I.1    Georgopoulou, N.2    Coughlan, C.M.3    Gillian, A.M.4    Breen, K.C.5
  • 66
    • 0025330692 scopus 로고
    • Fragmentation of Golgi apparatus of motor neurons in amyotrophic lateral sclerosis revealed by organelle specific antibodies
    • Mourelatos Z, Adle H, Hirano A, Donnefeld H, Gonatas JO, Gonatas NK (1990) Fragmentation of Golgi apparatus of motor neurons in amyotrophic lateral sclerosis revealed by organelle specific antibodies. Proc Natl Acad Sci USA 87, 4393-4395.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4393-4395
    • Mourelatos, Z.1    Adle, H.2    Hirano, A.3    Donnefeld, H.4    Gonatas, J.O.5    Gonatas, N.K.6
  • 68
    • 0029890685 scopus 로고    scopus 로고
    • The Golgi apparatus of spinal cord neurons in transgenic mice expressing mutant Cu, Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease
    • Mourelatos Z, Gonatas NK, Stieber A, Curvey M, Dal Cando M(1996) The Golgi apparatus of spinal cord neurons in transgenic mice expressing mutant Cu, Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease. Proc Natl Acad Sci USA 93, 5472-5477.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5472-5477
    • Mourelatos, Z.1    Gonatas, N.K.2    Stieber, A.3    Curvey, M.4    Dal Cando, M.5
  • 69
    • 0034653512 scopus 로고    scopus 로고
    • Fragmentation of Golgi apparatus of the anterior horn cells in patients with familial amyotrophic lateral sclerosis with SOD1 mutations and posterior column involvement
    • Fujita Y, Okamoto K, Sakurai A, Gonatas NK, Hirano A (2000) Fragmentation of Golgi apparatus of the anterior horn cells in patients with familial amyotrophic lateral sclerosis with SOD1 mutations and posterior column involvement. J Neurol Sci 174, 137-140.
    • (2000) J Neurol Sci , vol.174 , pp. 137-140
    • Fujita, Y.1    Okamoto, K.2    Sakurai, A.3    Gonatas, N.K.4    Hirano, A.5
  • 72
    • 84880834728 scopus 로고    scopus 로고
    • Molecular mechanisms of dendrite stability
    • Koleske AJ (2013) Molecular mechanisms of dendrite stability. Nat Rev Neurosci 14, 536-550.
    • (2013) Nat Rev Neurosci , vol.14 , pp. 536-550
    • Koleske, A.J.1
  • 73
    • 79953748494 scopus 로고    scopus 로고
    • Local, persistent activation of RhoGTPases during plasticity of single dendritic spines
    • Murakoshi H, Wang H, Yasuda R (2011) Local, persistent activation of RhoGTPases during plasticity of single dendritic spines. Nature 472, 100-104.
    • (2011) Nature , vol.472 , pp. 100-104
    • Murakoshi, H.1    Wang, H.2    Yasuda, R.3
  • 74
    • 84873045444 scopus 로고    scopus 로고
    • Abl2/Arg controls dendritic spine and dendrite arbor stability via distinct cytoskeletal control pathways
    • Lin YC, Yeckel MF, Koleske AJ (2013) Abl2/Arg controls dendritic spine and dendrite arbor stability via distinct cytoskeletal control pathways. J Neurosci 33, 1846-1857.
    • (2013) J Neurosci , vol.33 , pp. 1846-1857
    • Lin, Y.C.1    Yeckel, M.F.2    Koleske, A.J.3
  • 75
    • 84891404544 scopus 로고    scopus 로고
    • APP regulates NGF receptor trafficking and NGF-mediated neuronal differentiation and survival
    • Zhang Y-w, Chen Y, Liu Y, Zhao Y, Liao F-F, Xu H (2013) APP regulates NGF receptor trafficking and NGF-mediated neuronal differentiation and survival. PLoS ONE 8, e80571.
    • (2013) PLoS ONE , vol.8 , pp. e80571
    • Y-W, Z.1    Chen, Y.2    Liu, Y.3    Zhao, Y.4    Liao, F.-F.5    Xu, H.6
  • 76
    • 84876265087 scopus 로고    scopus 로고
    • Mild oxidative stress induces redistribution of BACE1 in non-apoptotic conditions and promotes the amyloidogenic processing of Alzheimer's disease amyloid precursor protein
    • Tan J-L, Li Q-X, Ciccotosto GD, Crouch PJ, Culvenor JG, Crouch PJ, Culvenor JG, White AR, Evin G (2013) Mild oxidative stress induces redistribution of BACE1 in non-apoptotic conditions and promotes the amyloidogenic processing of Alzheimer's disease amyloid precursor protein. PLoS ONE 8, e61246.
    • (2013) PLoS ONE , vol.8 , pp. e61246
    • Tan, J.-L.1    Li, Q.-X.2    Ciccotosto, G.D.3    Crouch, P.J.4    Culvenor, J.G.5    Crouch, P.J.6    Culvenor, J.G.7    White, A.R.8    Evin, G.9
  • 78
    • 0035780141 scopus 로고    scopus 로고
    • Amyloid beta-peptide promotes permeability transition pore in brain mitochondria
    • Moreira PI, Santos MS, Moreno A, Oliveira C (2001) Amyloid beta-peptide promotes permeability transition pore in brain mitochondria. Biosci Reports 21, 789-800.
    • (2001) Biosci Reports , vol.21 , pp. 789-800
    • Moreira, P.I.1    Santos, M.S.2    Moreno, A.3    Oliveira, C.4
  • 79
    • 84886925692 scopus 로고    scopus 로고
    • Mitochondrial alterations near amyloid plaques in an Alzheimer's disease mouse model
    • Xie H, Guan JS, Borrelli LA, Xu J, Serrano-Pozo A, Bacskai BJ (2013) Mitochondrial alterations near amyloid plaques in an Alzheimer's disease mouse model. J Neurosci 33, 17042-17051.
    • (2013) J Neurosci , vol.33 , pp. 17042-17051
    • Xie, H.1    Guan, J.S.2    Borrelli, L.A.3    Xu, J.4    Serrano-Pozo, A.5    Bacskai, B.J.6
  • 81
    • 84868540275 scopus 로고    scopus 로고
    • Close encounter: Mitochondria, endoplasmic reticulum and Alzheimer's disease
    • De Strooper Bart, Scorrano L (2012) Close encounter: Mitochondria, endoplasmic reticulum and Alzheimer's disease. EMBO J 31, 4095-4097.
    • (2012) EMBO J , vol.31 , pp. 4095-4097
    • Bart, D.S.1    Scorrano, L.2
  • 82
    • 81255190781 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease
    • Calkins MJ, Manczak M, Mao P, Shirendeb U, Reddy PH (2011) Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease. Hum Mol Genet 20, 4515-4529.
    • (2011) Hum Mol Genet , vol.20 , pp. 4515-4529
    • Calkins, M.J.1    Manczak, M.2    Mao, P.3    Shirendeb, U.4    Reddy, P.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.