메뉴 건너뛰기




Volumn 23, Issue 15, 2014, Pages 3943-3957

Multiple pathogenic proteins implicated in neuronopathic Gaucher disease mice

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA GLUCOSIDASE; GLUCOSYLCERAMIDE; GLUCOSYLSPHINGOSINE; GLYCOSPHINGOLIPID; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; UBIQUITIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; CONDURITOL EPOXIDE; ENZYME INHIBITOR; INOSITOL; LAMP1 PROTEIN, MOUSE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN; MAP1LC3 PROTEIN, MOUSE; MICROTUBULE ASSOCIATED PROTEIN; MITOCHONDRIAL OUTER MEMBRANE PROTEIN 35-KDA, MOUSE; MITOCHONDRIAL PROTEIN; PROSTAGLANDIN SYNTHASE;

EID: 84903984646     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddu105     Document Type: Article
Times cited : (74)

References (95)
  • 1
    • 79955424976 scopus 로고    scopus 로고
    • Gaucher disease
    • In: Valle, D., Beaudet, A.L., Vogelstein, B., Kinzler, K.W., Antonarakis, S.E. and Ballabio, A. (eds), OMMBID Mark II, New York: McGraw-Hill Companies, Inc
    • Grabowski, G.A., Petsko, G.A. and Kolodny, E.H. (2010) Gaucher disease. In: Valle, D., Beaudet, A.L., Vogelstein, B., Kinzler, K.W., Antonarakis, S.E. and Ballabio, A. (eds), Metabolic and Molecular Bases of InheritedDisease (OMMBID Mark II). New York: McGraw-Hill Companies, Inc.
    • (2010) Metabolic and Molecular Bases of Inherited Disease
    • Grabowski, G.A.1    Petsko, G.A.2    Kolodny, E.H.3
  • 2
    • 0027442703 scopus 로고
    • Phenotype/genotype correlations in Gaucher disease type I, clinical andtherapeutic implications
    • Sibille, A., Eng, C.M., Kim, S.J., Pastores, G. and Grabowski, G.A. (1993) Phenotype/genotype correlations in Gaucher disease type I, clinical andtherapeutic implications. Am. J. Hum. Genet., 52, 1094-1101.
    • (1993) Am. J. Hum. Genet. , vol.52 , pp. 1094-1101
    • Sibille, A.1    Eng, C.M.2    Kim, S.J.3    Pastores, G.4    Grabowski, G.A.5
  • 3
    • 0026465017 scopus 로고
    • Gaucher disease, Clinical, laboratory, radiologic, andgenetic features of 53 patients
    • Zimran, A., Kay, A., Gelbart, T., Garver, P., Thurston, D., Saven, A. andBeutler, E. (1992) Gaucher disease. Clinical, laboratory, radiologic, andgenetic features of 53 patients. Medicine, 71, 337-353.
    • (1992) Medicine , vol.71 , pp. 337-353
    • Zimran, A.1    Kay, A.2    Gelbart, T.3    Garver, P.4    Thurston, D.5    Saven, A.6    Beutler, E.7
  • 4
    • 53049096591 scopus 로고    scopus 로고
    • Phenotype, diagnosis, and treatment of Gaucher'sdisease
    • Grabowski, G.A. (2008) Phenotype, diagnosis, and treatment of Gaucher'sdisease. Lancet, 372, 1263-1271.
    • (2008) Lancet , vol.372 , pp. 1263-1271
    • Grabowski, G.A.1
  • 5
    • 62549133546 scopus 로고    scopus 로고
    • Neuroinflammation in Parkinson'sdisease: a target for neuroprotection?
    • Hirsch, E.C. and Hunot, S. (2009) Neuroinflammation in Parkinson'sdisease: a target for neuroprotection? Lancet Neurol., 8, 382-397.
    • (2009) Lancet Neurol , vol.8 , pp. 382-397
    • Hirsch, E.C.1    Hunot, S.2
  • 6
    • 77950675049 scopus 로고    scopus 로고
    • Neuronopathic Gaucher disease in the mouse: viable combined selectivesaposin C deficiency and mutant glucocerebrosidase (V394L) mice withglucosylsphingosine and glucosylceramide accumulation and progressiveneurological deficits
    • Sun, Y., Liou, B., Ran, H., Skelton, M.R., Williams, M.T., Vorhees, C.V., Kitatani, K., Hannun, Y.A., Witte, D.P., Xu, Y.H. et al. (2010) Neuronopathic Gaucher disease in the mouse: viable combined selectivesaposin C deficiency and mutant glucocerebrosidase (V394L) mice withglucosylsphingosine and glucosylceramide accumulation and progressiveneurological deficits. Hum. Mol. Genet., 19, 1088-1097.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1088-1097
    • Sun, Y.1    Liou, B.2    Ran, H.3    Skelton, M.R.4    Williams, M.T.5    Vorhees, C.V.6    Kitatani, K.7    Hannun, Y.A.8    Witte, D.P.9    Xu, Y.H.10
  • 9
    • 79952619654 scopus 로고    scopus 로고
    • Accumulation and distribution of alpha-synuclein and ubiquitin in the CNSof Gaucher disease mouse models
    • Xu, Y.H., Sun, Y., Ran, H., Quinn, B., Witte, D. and Grabowski, G.A. (2011) Accumulation and distribution of alpha-synuclein and ubiquitin in the CNSof Gaucher disease mouse models. Mol. Genet. Metab., 102, 436-447.
    • (2011) Mol. Genet. Metab. , vol.102 , pp. 436-447
    • Xu, Y.H.1    Sun, Y.2    Ran, H.3    Quinn, B.4    Witte, D.5    Grabowski, G.A.6
  • 10
    • 40449127705 scopus 로고    scopus 로고
    • Neuropathological aspects of Alzheimer disease, Parkinson disease and frontotemporal dementia
    • Jellinger, K.A. (2008) Neuropathological aspects of Alzheimer disease, Parkinson disease and frontotemporal dementia. Neurodegener. Dis., 5, 118-121.
    • (2008) Neurodegener. Dis. , vol.5 , pp. 118-121
    • Jellinger, K.A.1
  • 12
    • 0027327418 scopus 로고
    • Trinucleotide repeat elongation in the Huntingtongene in Huntington disease patients from 71 Danish families
    • Norremolle, A., Riess, O., Epplen, J.T., Fenger, K., Hasholt, L. andSorensen, S.A. (1993) Trinucleotide repeat elongation in the Huntingtongene in Huntington disease patients from 71 Danish families. Hum. Mol. Genet., 2, 1475-1476.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1475-1476
    • Norremolle, A.1    Riess, O.2    Epplen, J.T.3    Fenger, K.4    Hasholt, L.5    Sorensen, S.A.6
  • 18
    • 79956199921 scopus 로고    scopus 로고
    • Acid beta-glucosidase mutantslinked to Gaucher disease, Parkinson disease, and Lewy body dementia alteralpha-synuclein processing
    • Cullen, V., Sardi, S.P., Ng, J., Xu, Y.H., Sun, Y., Tomlinson, J.J., Kolodziej, P., Kahn, I., Saftig, P., Woulfe, J. et al. (2011) Acid beta-glucosidase mutantslinked to Gaucher disease, Parkinson disease, and Lewy body dementia alteralpha-synuclein processing. Ann. Neurol., 69, 940-953.
    • (2011) Ann. Neurol. , vol.69 , pp. 940-953
    • Cullen, V.1    Sardi, S.P.2    Ng, J.3    Xu, Y.H.4    Sun, Y.5    Tomlinson, J.J.6    Kolodziej, P.7    Kahn, I.8    Saftig, P.9    Woulfe, J.10
  • 21
    • 0036777211 scopus 로고    scopus 로고
    • Parkinson's disease and relatedsynucleinopathies are a new class of nervous system amyloidoses
    • Trojanowski, J.Q. and Lee, V.M. (2002) Parkinson's disease and relatedsynucleinopathies are a new class of nervous system amyloidoses. Neurotoxicology, 23, 457-460.
    • (2002) Neurotoxicology , vol.23 , pp. 457-460
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 23
    • 15244348524 scopus 로고    scopus 로고
    • Gaucher disease and parkinsonism
    • Sidransky, E. (2005) Gaucher disease and parkinsonism. Mol. Genet. Metab., 84, 302-304.
    • (2005) Mol. Genet. Metab. , vol.84 , pp. 302-304
    • Sidransky, E.1
  • 24
    • 78649318011 scopus 로고    scopus 로고
    • Gaucher disease and parkinsonism, a molecular linktheory
    • Goldin, E. (2010) Gaucher disease and parkinsonism, a molecular linktheory. Mol. Genet. Metab., 101, 307-310.
    • (2010) Mol. Genet. Metab. , vol.101 , pp. 307-310
    • Goldin, E.1
  • 26
    • 25444512703 scopus 로고    scopus 로고
    • Gaucher diseasemouse models: point mutations at the acid beta-glucosidase locus combinedwith low-level prosaposin expression lead to disease variants
    • Sun, Y., Quinn, B., Witte, D.P. and Grabowski, G.A. (2005) Gaucher diseasemouse models: point mutations at the acid beta-glucosidase locus combinedwith low-level prosaposin expression lead to disease variants. J. Lipid Res., 46, 2102-2113.
    • (2005) J. Lipid Res. , vol.46 , pp. 2102-2113
    • Sun, Y.1    Quinn, B.2    Witte, D.P.3    Grabowski, G.A.4
  • 27
    • 77954933661 scopus 로고    scopus 로고
    • The role ofglucocerebrosidase mutations in Parkinson disease and Lewy bodydisorders
    • Velayati, A., Yu, W.H. and Sidransky, E. (2010) The role ofglucocerebrosidase mutations in Parkinson disease and Lewy bodydisorders. Curr. Neurol. Neurosci. Rep., 10, 190-198.
    • (2010) Curr. Neurol. Neurosci. Rep. , vol.10 , pp. 190-198
    • Velayati, A.1    Yu, W.H.2    Sidransky, E.3
  • 30
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursorprotein in the mitochondrial import channels of human Alzheimer'sdisease brain is associated with mitochondrial dysfunction
    • Devi, L., Prabhu, B.M., Galati, D.F., Avadhani, N.G. andAnandatheerthavarada, H.K. (2006) Accumulation of amyloid precursorprotein in the mitochondrial import channels of human Alzheimer'sdisease brain is associated with mitochondrial dysfunction. J. Neurosci., 26, 9057-9068.
    • (2006) J. Neurosci. , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 34
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A beta accumulation inAlzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression
    • Manczak, M., Anekonda, T.S., Henson, E., Park, B.S., Quinn, J. and Reddy, P.H. (2006) Mitochondria are a direct site of A beta accumulation inAlzheimer's disease neurons: implications for free radical generation andoxidativedamage in disease progression. Hum.Mol. Genet., 15, 1437-1449.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 35
    • 35948969760 scopus 로고    scopus 로고
    • Amyloid precursor proteinand mitochondrial dysfunction in Alzheimer's disease
    • Anandatheerthavarada, H.K. and Devi, L. (2007) Amyloid precursor proteinand mitochondrial dysfunction in Alzheimer's disease. Neuroscientist, 13, 626-638.
    • (2007) Neuroscientist , vol.13 , pp. 626-638
    • Anandatheerthavarada, H.K.1    Devi, L.2
  • 36
    • 0035834076 scopus 로고    scopus 로고
    • beta-amyloid peptides enhancealpha-synuclein accumulation and neuronal deficits in a transgenic mousemodel linking Alzheimer's disease and Parkinson's disease
    • Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M. and Mucke, L. (2001) beta-amyloid peptides enhancealpha-synuclein accumulation and neuronal deficits in a transgenic mousemodel linking Alzheimer's disease and Parkinson's disease. Proc. Natl. Acad. Sci. USA, 98, 12245-12250.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12245-12250
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Sagara, Y.4    Mallory, M.5    Hashimoto, M.6    Mucke, L.7
  • 37
    • 33748584602 scopus 로고    scopus 로고
    • Interaction between Abeta peptide and alpha synuclein: molecularmechanisms in overlapping pathology of Alzheimer's and Parkinson's indementia with Lewy body disease
    • Mandal, P.K., Pettegrew, J.W., Masliah, E., Hamilton, R.L. and Mandal, R. (2006) Interaction between Abeta peptide and alpha synuclein: molecularmechanisms in overlapping pathology of Alzheimer's and Parkinson's indementia with Lewy body disease. Neurochem. Res., 31, 1153-1162.
    • (2006) Neurochem. Res. , vol.31 , pp. 1153-1162
    • Mandal, P.K.1    Pettegrew, J.W.2    Masliah, E.3    Hamilton, R.L.4    Mandal, R.5
  • 38
    • 84859928720 scopus 로고    scopus 로고
    • Examining the mechanisms thatlink beta-amyloid and alpha-synuclein pathologies
    • Marsh, S.E. and Blurton-Jones, M. (2012) Examining the mechanisms thatlink beta-amyloid and alpha-synuclein pathologies. Alzheimers Res. Ther., 4, 11.
    • (2012) Alzheimers Res. Ther. , vol.4 , pp. 11
    • Marsh, S.E.1    Blurton-Jones, M.2
  • 39
    • 0036392385 scopus 로고    scopus 로고
    • Prosaposin: threshold rescue and analysis of the "neuritogenic" region in transgenic mice
    • Sun, Y., Qi, X., Witte, D.P., Ponce, E., Kondoh, K., Quinn, B. andGrabowski, G.A. (2002) Prosaposin: threshold rescue and analysis of the "neuritogenic" region in transgenic mice. Mol. Genet. Metab., 76, 271-286.
    • (2002) Mol. Genet. Metab. , vol.76 , pp. 271-286
    • Sun, Y.1    Qi, X.2    Witte, D.P.3    Ponce, E.4    Kondoh, K.5    Quinn, B.6    Grabowski, G.A.7
  • 40
    • 0142244182 scopus 로고    scopus 로고
    • Viable mousemodels of acid beta-glucosidase deficiency: the defect in Gaucher disease
    • Xu, Y.H., Quinn, B., Witte, D. and Grabowski, G.A. (2003) Viable mousemodels of acid beta-glucosidase deficiency: the defect in Gaucher disease. Am. J. Pathol., 163, 2093-2101.
    • (2003) Am. J. Pathol. , vol.163 , pp. 2093-2101
    • Xu, Y.H.1    Quinn, B.2    Witte, D.3    Grabowski, G.A.4
  • 41
    • 84865963204 scopus 로고    scopus 로고
    • Blocking of bradykinin receptor B1 protects from focal closed head injury in mice by reducing axonal damageand astroglia activation
    • Albert-Weissenberger, C., Stetter, C., Meuth, S.G., Gobel, K., Bader, M., Siren, A.L. and Kleinschnitz, C. (2012) Blocking of bradykinin receptor B1 protects from focal closed head injury in mice by reducing axonal damageand astroglia activation. J. Cereb. Blood Flow Metab., 32, 1747-1756.
    • (2012) J. Cereb. Blood Flow Metab. , vol.32 , pp. 1747-1756
    • Albert-Weissenberger, C.1    Stetter, C.2    Meuth, S.G.3    Gobel, K.4    Bader, M.5    Siren, A.L.6    Kleinschnitz, C.7
  • 44
    • 77950495123 scopus 로고    scopus 로고
    • Physiological significance of selectivedegradation of p62 by autophagy
    • Komatsu,M. and Ichimura, Y. (2010) Physiological significance of selectivedegradation of p62 by autophagy. FEBS Lett., 584, 1374-1378.
    • (2010) FEBS Lett. , vol.584 , pp. 1374-1378
    • Komatsu, M.1    Ichimura, Y.2
  • 46
    • 0025943418 scopus 로고
    • Hippocampal degeneration differentiates diffuse Lewybody disease (DLBD) from Alzheimer's disease: light and electronmicroscopic immunocytochemistry of CA2-3 neurites specific to DLBD
    • Dickson, D.W., Ruan, D., Crystal, H., Mark, M.H., Davies, P., Kress, Y. andYen, S.H. (1991) Hippocampal degeneration differentiates diffuse Lewybody disease (DLBD) from Alzheimer's disease: light and electronmicroscopic immunocytochemistry of CA2-3 neurites specific to DLBD. Neurology, 41, 1402-1409.
    • (1991) Neurology , vol.41 , pp. 1402-1409
    • Dickson, D.W.1    Ruan, D.2    Crystal, H.3    Mark, M.H.4    Davies, P.5    Kress, Y.6    Yen, S.H.7
  • 47
    • 18344417178 scopus 로고    scopus 로고
    • Lewy bodies contain altered alpha-synuclein in brains of manyfamilial Alzheimer's disease patients with mutations in presenilin andamyloid precursor protein genes
    • Lippa, C.F., Fujiwara, H., Mann, D.M., Giasson, B., Baba, M., Schmidt, M.L., Nee, L.E., O'Connell, B., Pollen, D.A., St George-Hyslop, P. et al. (1998) Lewy bodies contain altered alpha-synuclein in brains of manyfamilial Alzheimer's disease patients with mutations in presenilin andamyloid precursor protein genes. Am. J. Pathol., 153, 1365-1370.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1365-1370
    • Lippa, C.F.1    Fujiwara, H.2    Mann, D.M.3    Giasson, B.4    Baba, M.5    Schmidt, M.L.6    Nee, L.E.7    O'Connell, B.8    Pollen, D.A.9    St George-Hyslop, P.10
  • 48
    • 0032990543 scopus 로고    scopus 로고
    • Antibodies to alpha-synuclein detect Lewy bodies in many Down'ssyndrome brains with Alzheimer's disease
    • Lippa, C.F., Schmidt, M.L., Lee, V.M. and Trojanowski, J.Q. (1999) Antibodies to alpha-synuclein detect Lewy bodies in many Down'ssyndrome brains with Alzheimer's disease. Ann. Neurol., 45, 353-357.
    • (1999) Ann. Neurol. , vol.45 , pp. 353-357
    • Lippa, C.F.1    Schmidt, M.L.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 49
    • 21244456941 scopus 로고    scopus 로고
    • X-ray structure ofhuman acid-beta-glucosidase covalently bound to conduritol-B-epoxide, Implications for Gaucher disease
    • Premkumar, L., Sawkar, A.R., Boldin-Adamsky, S., Toker, L., Silman, I., Kelly, J.W., Futerman, A.H. and Sussman, J.L. (2005) X-ray structure ofhuman acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease. J. Biol. Chem., 280, 23815-23819.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23815-23819
    • Premkumar, L.1    Sawkar, A.R.2    Boldin-Adamsky, S.3    Toker, L.4    Silman, I.5    Kelly, J.W.6    Futerman, A.H.7    Sussman, J.L.8
  • 51
    • 0037250282 scopus 로고    scopus 로고
    • Prevalence of amyloid-beta deposition in the cerebral cortex in Parkinson'sdisease
    • Mastaglia, F.L., Johnsen, R.D., Byrnes, M.L. and Kakulas, B.A. (2003) Prevalence of amyloid-beta deposition in the cerebral cortex in Parkinson'sdisease. Mov. Disord., 18, 81-86.
    • (2003) Mov. Disord. , vol.18 , pp. 81-86
    • Mastaglia, F.L.1    Johnsen, R.D.2    Byrnes, M.L.3    Kakulas, B.A.4
  • 52
    • 0030777850 scopus 로고    scopus 로고
    • Alterations inglutamate receptor 2/3 subunits and amyloid precursor protein expressionduring the course of Alzheimer's disease and Lewy body variant
    • Thorns, V., Mallory, M., Hansen, L. and Masliah, E. (1997) Alterations inglutamate receptor 2/3 subunits and amyloid precursor protein expressionduring the course of Alzheimer's disease and Lewy body variant. ActaNeuropathol., 94, 539-548.
    • (1997) ActaNeuropathol. , vol.94 , pp. 539-548
    • Thorns, V.1    Mallory, M.2    Hansen, L.3    Masliah, E.4
  • 54
    • 1642372780 scopus 로고    scopus 로고
    • Phthalocyanine tetrasulfonates affect the amyloid formation andcytotoxicity of alpha-synuclein
    • Lee, E.N., Cho, H.J., Lee, C.H., Lee, D., Chung, K.C. and Paik, S.R. (2004) Phthalocyanine tetrasulfonates affect the amyloid formation andcytotoxicity of alpha-synuclein. Biochemistry, 43, 3704-3715.
    • (2004) Biochemistry , vol.43 , pp. 3704-3715
    • Lee, E.N.1    Cho, H.J.2    Lee, C.H.3    Lee, D.4    Chung, K.C.5    Paik, S.R.6
  • 55
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest ofAlzheimer's amyloid precursor protein impairs mitochondrial function inneuronal cells
    • Anandatheerthavarada, H.K., Biswas, G., Robin, M.A. and Avadhani, N.G. (2003) Mitochondrial targeting and a novel transmembrane arrest ofAlzheimer's amyloid precursor protein impairs mitochondrial function inneuronal cells. J. Cell Biol., 161, 41-54.
    • (2003) J. Cell Biol. , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 56
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import andaccumulation of alpha-synuclein impair complex I in human dopaminergicneuronal cultures and Parkinson disease brain
    • Devi, L., Raghavendran, V., Prabhu, B.M., Avadhani, N.G. andAnandatheerthavarada, H.K. (2008) Mitochondrial import andaccumulation of alpha-synuclein impair complex I in human dopaminergicneuronal cultures and Parkinson disease brain. J. Biol. Chem., 283, 9089-9100.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 57
    • 0033396991 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms underlying perturbed energymetabolism and neuronal degeneration in Alzheimer's and Parkinson'sdiseases
    • Mattson, M.P., Pedersen, W.A., Duan, W., Culmsee, C. and Camandola, S. (1999) Cellular and molecular mechanisms underlying perturbed energymetabolism and neuronal degeneration in Alzheimer's and Parkinson'sdiseases. Ann. N. Y. Acad. Sci., 893, 154-175.
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 154-175
    • Mattson, M.P.1    Pedersen, W.A.2    Duan, W.3    Culmsee, C.4    Camandola, S.5
  • 58
    • 0035871971 scopus 로고    scopus 로고
    • Elevated vulnerability to oxidative stress-induced celldeath and activation of caspase-3 by the Swedish amyloid precursor proteinmutation
    • Eckert, A., Steiner, B., Marques, C., Leutz, S., Romig, H., Haass, C. andMuller, W.E. (2001) Elevated vulnerability to oxidative stress-induced celldeath and activation of caspase-3 by the Swedish amyloid precursor proteinmutation. J. Neurosci. Res., 64, 183-192.
    • (2001) J. Neurosci. Res. , vol.64 , pp. 183-192
    • Eckert, A.1    Steiner, B.2    Marques, C.3    Leutz, S.4    Romig, H.5    Haass, C.6    Muller, W.E.7
  • 59
    • 0042847291 scopus 로고    scopus 로고
    • Neurotoxic mechanisms caused by the Alzheimer'sdisease-linked Swedish amyloid precursor protein mutation: oxidativestress, caspases, and the JNK pathway
    • Marques, C.A., Keil, U., Bonert, A., Steiner, B., Haass, C., Muller, W.E. andEckert, A. (2003) Neurotoxic mechanisms caused by the Alzheimer'sdisease-linked Swedish amyloid precursor protein mutation: oxidativestress, caspases, and the JNK pathway. J. Biol. Chem., 278, 28294-28302.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28294-28302
    • Marques, C.A.1    Keil, U.2    Bonert, A.3    Steiner, B.4    Haass, C.5    Muller, W.E.6    Eckert, A.7
  • 60
    • 34247158550 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrialdysfunction in neurodegenerative diseases
    • Trushina, E. and McMurray, C.T. (2007) Oxidative stress and mitochondrialdysfunction in neurodegenerative diseases. Neuroscience, 145, 1233-1248.
    • (2007) Neuroscience , vol.145 , pp. 1233-1248
    • Trushina, E.1    McMurray, C.T.2
  • 62
    • 14744305520 scopus 로고    scopus 로고
    • Mitochondrial associated metabolic proteins areselectively oxidized in A30P alpha-synuclein transgenic mice-a model offamilial Parkinson's disease
    • Poon, H.F., Frasier, M., Shreve, N., Calabrese, V., Wolozin, B. andButterfield, D.A. (2005) Mitochondrial associated metabolic proteins areselectively oxidized in A30P alpha-synuclein transgenic mice-a model offamilial Parkinson's disease. Neurobiol. Dis., 18, 492-498.
    • (2005) Neurobiol. Dis. , vol.18 , pp. 492-498
    • Poon, H.F.1    Frasier, M.2    Shreve, N.3    Calabrese, V.4    Wolozin, B.5    Butterfield, D.A.6
  • 63
    • 0020320060 scopus 로고
    • Accumulation of glucosylceramideand glucosylsphingosine (psychosine) in cerebrum and cerebellum ininfantile and juvenile Gaucher disease
    • Nilsson, O. and Svennerholm, L. (1982) Accumulation of glucosylceramideand glucosylsphingosine (psychosine) in cerebrum and cerebellum ininfantile and juvenile Gaucher disease. J. Neurochem., 39, 709-718.
    • (1982) J. Neurochem. , vol.39 , pp. 709-718
    • Nilsson, O.1    Svennerholm, L.2
  • 64
    • 0023891786 scopus 로고
    • Inhibition of cytochrome coxidase and hemolysis caused by lysosphingolipids
    • Igisu, H., Hamasaki, N., Ito, A. and Ou,W.(1988) Inhibition of cytochrome coxidase and hemolysis caused by lysosphingolipids. Lipids, 23, 345-348.
    • (1988) Lipids , vol.23 , pp. 345-348
    • Igisu, H.1    Hamasaki, N.2    Ito, A.3    Ou, W.4
  • 65
    • 0029133790 scopus 로고
    • Cellular injury induced by oxidativestress is mediated through lysosomal damage
    • Ollinger, K. and Brunk, U.T. (1995) Cellular injury induced by oxidativestress is mediated through lysosomal damage. Free Radic. Biol. Med., 19, 565-574.
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 565-574
    • Ollinger, K.1    Brunk, U.T.2
  • 66
    • 77449115085 scopus 로고    scopus 로고
    • Mitochondrial accumulation of APP and Abeta: significance for Alzheimerdisease pathogenesis
    • Pavlov, P.F., Hansson Petersen, C., Glaser, E. and Ankarcrona, M. (2009) Mitochondrial accumulation of APP and Abeta: significance for Alzheimerdisease pathogenesis. J. Cell Mol. Med., 13, 4137-4145.
    • (2009) J. Cell Mol. Med. , vol.13 , pp. 4137-4145
    • Pavlov, P.F.1    Hansson Petersen, C.2    Glaser, E.3    Ankarcrona, M.4
  • 72
    • 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, F.M., Wegiel, J., Yu, W.H. and Nixon, R.A. (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
  • 75
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transferactivates autophagy and ameliorates the neurodegenerative pathology inalpha-synuclein models of Parkinson's and Lewy body diseases
    • Spencer, B., Potkar, R., Trejo, M., Rockenstein, E., Patrick, C., Gindi, R., Adame, A., Wyss-Coray, T. and Masliah, E. (2009) Beclin 1 gene transferactivates autophagy and ameliorates the neurodegenerative pathology inalpha-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    Adame, A.7    Wyss-Coray, T.8    Masliah, E.9
  • 76
    • 79952325543 scopus 로고    scopus 로고
    • Endosomal accumulation of APP in wobblermotor neurons reflects impaired vesicle trafficking: implications for humanmotor neuron disease
    • Palmisano, R., Golfi, P., Heimann, P., Shaw, C., Troakes, C., Schmitt-John, T. and Bartsch, J.W. (2011) Endosomal accumulation of APP in wobblermotor neurons reflects impaired vesicle trafficking: implications for humanmotor neuron disease. BMC Neurosci., 12, 24.
    • (2011) BMC Neurosci. , vol.12 , pp. 24
    • Palmisano, R.1    Golfi, P.2    Heimann, P.3    Shaw, C.4    Troakes, C.5    Schmitt-John, T.6    Bartsch, J.W.7
  • 77
    • 77956131970 scopus 로고    scopus 로고
    • Altered expression anddistribution of cathepsins in neuronopathic forms of Gaucher disease and inother sphingolipidoses
    • Vitner, E.B., Dekel, H., Zigdon, H., Shachar, T., Farfel-Becker, T., Eilam, R., Karlsson, S. and Futerman, A.H. (2010) Altered expression anddistribution of cathepsins in neuronopathic forms of Gaucher disease and inother sphingolipidoses. Hum. Mol. Genet., 19, 3583-3590.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3583-3590
    • Vitner, E.B.1    Dekel, H.2    Zigdon, H.3    Shachar, T.4    Farfel-Becker, T.5    Eilam, R.6    Karlsson, S.7    Futerman, A.H.8
  • 78
    • 6044221306 scopus 로고    scopus 로고
    • GM1 ganglioside regulates the proteolysis of amyloid precursor protein
    • Zha, Q., Ruan, Y., Hartmann, T., Beyreuther, K. and Zhang, D. (2004) GM1 ganglioside regulates the proteolysis of amyloid precursor protein. Mol. Psychiatry, 9, 946-952.
    • (2004) Mol. Psychiatry , vol.9 , pp. 946-952
    • Zha, Q.1    Ruan, Y.2    Hartmann, T.3    Beyreuther, K.4    Zhang, D.5
  • 80
    • 78549273390 scopus 로고    scopus 로고
    • Macroautophagy is not directly involved in the metabolism ofamyloid precursor protein
    • Boland, B., Smith, D.A., Mooney, D., Jung, S.S., Walsh, D.M. and Platt, F.M. (2010) Macroautophagy is not directly involved in the metabolism ofamyloid precursor protein. J. Biol. Chem., 285, 37415-37426.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37415-37426
    • Boland, B.1    Smith, D.A.2    Mooney, D.3    Jung, S.S.4    Walsh, D.M.5    Platt, F.M.6
  • 81
    • 1842615071 scopus 로고    scopus 로고
    • Aberrantphosphorylation of alpha-synuclein in human Niemann-Pick type C1 disease
    • Saito, Y., Suzuki, K., Hulette, C.M. and Murayama, S. (2004) Aberrantphosphorylation of alpha-synuclein in human Niemann-Pick type C1 disease. J. Neuropathol. Exp. Neurol., 63, 323-328.
    • (2004) J. Neuropathol. Exp. Neurol. , vol.63 , pp. 323-328
    • Saito, Y.1    Suzuki, K.2    Hulette, C.M.3    Murayama, S.4
  • 83
    • 23044510465 scopus 로고    scopus 로고
    • Inhibition of glycosphingolipid biosynthesis reduces secretion of thebeta-amyloid precursor protein and amyloid beta-peptide
    • Tamboli, I.Y., Prager, K., Barth, E., Heneka, M., Sandhoff, K. and Walter, J. (2005) Inhibition of glycosphingolipid biosynthesis reduces secretion of thebeta-amyloid precursor protein and amyloid beta-peptide. J. Biol. Chem., 280, 28110-28117.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28110-28117
    • Tamboli, I.Y.1    Prager, K.2    Barth, E.3    Heneka, M.4    Sandhoff, K.5    Walter, J.6
  • 84
    • 77949360652 scopus 로고    scopus 로고
    • How cholesterol constrainsglycolipid conformation for optimal recognition of Alzheimer's betaamyloid peptide (Abeta1-40)
    • Yahi, N., Aulas, A. and Fantini, J. (2010) How cholesterol constrainsglycolipid conformation for optimal recognition of Alzheimer's betaamyloid peptide (Abeta1-40). PLoS One, 5, e9079.
    • (2010) PLoS One , vol.5
    • Yahi, N.1    Aulas, A.2    Fantini, J.3
  • 85
    • 34250718676 scopus 로고    scopus 로고
    • Isolation and culture of adult neuronsand neurospheres
    • Brewer, G.J. and Torricelli, J.R. (2007) Isolation and culture of adult neuronsand neurospheres. Nat. Protoc., 2, 1490-1498.
    • (2007) Nat. Protoc. , vol.2 , pp. 1490-1498
    • Brewer, G.J.1    Torricelli, J.R.2
  • 86
    • 0033660735 scopus 로고    scopus 로고
    • Effects of carbonions on primary cultures of mouse brain cells
    • Nojima, K., Ando, K., Fujiwara, H. and Ando, S. (2000) Effects of carbonions on primary cultures of mouse brain cells. Adv. Space Res., 25, 2051-2056.
    • (2000) Adv. Space Res. , vol.25 , pp. 2051-2056
    • Nojima, K.1    Ando, K.2    Fujiwara, H.3    Ando, S.4
  • 87
    • 84859853954 scopus 로고    scopus 로고
    • Culture of rodent cortical and hippocampalneurons
    • Facci, L. and Skaper, S.D. (2012) Culture of rodent cortical and hippocampalneurons. Methods Mol. Biol., 846, 49-56.
    • (2012) Methods Mol. Biol. , vol.846 , pp. 49-56
    • Facci, L.1    Skaper, S.D.2
  • 88
    • 0003698235 scopus 로고    scopus 로고
    • The Mouse Brain in StereotaxicCoordinates
    • San Diego: Academic Press
    • Paxinos, G. and Franklin, K.B.J. The Mouse Brain in StereotaxicCoordinates. San Diego: Academic Press, 2001.
    • (2001)
    • Paxinos, G.1    Franklin, K.B.J.2
  • 89
    • 0022975258 scopus 로고
    • Human acid beta-glucosidase, Use ofconduritol B epoxide derivatives to investigate the catalytically activenormal and Gaucher disease enzymes
    • Grabowski, G.A., Osiecki-Newman, K., Dinur, T., Fabbro, D., Legler, G., Gatt, S. and Desnick, R.J. (1986) Human acid beta-glucosidase. Use ofconduritol B epoxide derivatives to investigate the catalytically activenormal and Gaucher disease enzymes. J. Biol. Chem., 261, 8263-8269.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8263-8269
    • Grabowski, G.A.1    Osiecki-Newman, K.2    Dinur, T.3    Fabbro, D.4    Legler, G.5    Gatt, S.6    Desnick, R.J.7
  • 91
    • 0021962297 scopus 로고
    • Quantitative and continuous analysis of ATP release from bloodplatelets with firefly luciferase luminescence
    • Higashi, T., Isomoto, A., Tyuma, I., Kakishita, E., Uomoto,M.and Nagai, K. (1985) Quantitative and continuous analysis of ATP release from bloodplatelets with firefly luciferase luminescence. Thromb.Haemost., 53, 65-69.
    • (1985) Thromb.Haemost. , vol.53 , pp. 65-69
    • Higashi, T.1    Isomoto, A.2    Tyuma, I.3    Kakishita, E.4    Uomoto, M.5    Nagai, K.6
  • 93
    • 0027499070 scopus 로고
    • The use ofATP bioluminescence as a measure of cell proliferation and cytotoxicity
    • Crouch, S.P., Kozlowski, R., Slater, K.J. and Fletcher, J. (1993) The use ofATP bioluminescence as a measure of cell proliferation and cytotoxicity. J. Immunol. Methods, 160, 81-88.
    • (1993) J. Immunol. Methods , vol.160 , pp. 81-88
    • Crouch, S.P.1    Kozlowski, R.2    Slater, K.J.3    Fletcher, J.4
  • 94
    • 0023016136 scopus 로고
    • Extraction of adenosine triphosphate from microbialand somatic cells
    • Stanley, P.E. (1986) Extraction of adenosine triphosphate from microbialand somatic cells. Methods Enzymol., 133, 14-22.
    • (1986) Methods Enzymol. , vol.133 , pp. 14-22
    • Stanley, P.E.1
  • 95
    • 77950653171 scopus 로고    scopus 로고
    • Humanmitochondrial leucyl-tRNA synthetasecorrects mitochondrial dysfunctions due to the tRNALeu(UUR) A3243Gmutation, associated with mitochondrial encephalomyopathy, lacticacidosis, and stroke-like symptoms and diabetes
    • Li, R. and Guan,M.X.(2010) Humanmitochondrial leucyl-tRNA synthetasecorrects mitochondrial dysfunctions due to the tRNALeu(UUR) A3243Gmutation, associated with mitochondrial encephalomyopathy, lacticacidosis, and stroke-like symptoms and diabetes. Mol. Cell Biol., 30, 2147-2154.
    • (2010) Mol. Cell Biol. , vol.30 , pp. 2147-2154
    • Li, R.1    Guan, M.X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.