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Volumn 389, Issue , 1996, Pages 261-269

Endosome-lysosomes, ubiquitin and neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; OVIS ARIES;

EID: 0030345833     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4613-0335-0_33     Document Type: Article
Times cited : (42)

References (36)
  • 1
    • 0029346911 scopus 로고
    • The abnormal form of the prion protein accumulates in endosome/lysosome-like organelles in scrapie-infected mouse brain
    • In press
    • Arnold JE, Tipler C, Laszlo L, Hope J, Landon M, Mayer RJ. The abnormal form of the prion protein accumulates in endosome/lysosome-like organelles in scrapie-infected mouse brain. J. Pathol. 1995; In press.
    • (1995) J. Pathol.
    • Arnold, J.E.1    Tipler, C.2    Laszlo, L.3    Hope, J.4    Landon, M.5    Mayer, R.J.6
  • 2
    • 0024815331 scopus 로고
    • The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects
    • Benowitz LI, Rodriguez W, Paskevich P, Mufson EJ, Schenk D, Neve RL. The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects. Exp. Neurol. 1989;106:237-250.
    • (1989) Exp. Neurol. , vol.106 , pp. 237-250
    • Benowitz, L.I.1    Rodriguez, W.2    Paskevich, P.3    Mufson, E.J.4    Schenk, D.5    Neve, R.L.6
  • 3
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt DR, Taraboulos A, Prusiner SB. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 1992;267:16188-16199.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 4
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993;73:1339-1347.
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3
  • 5
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Bueler H, Fischer M, Lang Y, et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992;356:577-582.
    • (1992) Nature , vol.356 , pp. 577-582
    • Bueler, H.1    Fischer, M.2    Lang, Y.3
  • 6
    • 0003304739 scopus 로고
    • Dementia associated with cortical Lewy bodies: Proposed clinical diagnostic criteria
    • Byrne EJ, Lennox GG, Godwin-Austen RB, et al. Dementia associated with cortical Lewy bodies: proposed clinical diagnostic criteria. Dementia 1991;2:283-284.
    • (1991) Dementia , vol.2 , pp. 283-284
    • Byrne, E.J.1    Lennox, G.G.2    Godwin-Austen, R.B.3
  • 7
    • 0026327404 scopus 로고
    • Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease
    • Cataldo AM, Paskevich PA, Kominami E, Nixon RA. Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proc. Natl. Acad. Sci. USA 1991;88:10998-11002.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10998-11002
    • Cataldo, A.M.1    Paskevich, P.A.2    Kominami, E.3    Nixon, R.A.4
  • 8
    • 0026756460 scopus 로고
    • Activation-induced ubiquitination of the T-cell antigen receptor
    • Cenciarelli C, Hou D, Hsu KC, et al. Activation-induced ubiquitination of the T-cell antigen receptor. Science 1992;257:795-797.
    • (1992) Science , vol.257 , pp. 795-797
    • Cenciarelli, C.1    Hou, D.2    Hsu, K.C.3
  • 9
    • 0025330687 scopus 로고
    • Prion dementia without characteristic pathology
    • Collinge J, Owen F, Poulter M, et al. Prion dementia without characteristic pathology. Lancet 1990;336:7-9.
    • (1990) Lancet , vol.336 , pp. 7-9
    • Collinge, J.1    Owen, F.2    Poulter, M.3
  • 10
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late-onset families
    • Corder E H , Saunders A M , Strittmatter, W.J., et. al. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late-onset families. Science 1993;261:921-923
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1    Saunders, A.M.2    Strittmatter, W.J.3
  • 11
    • 0027374785 scopus 로고
    • Alzheimer's disease and Creutzfeldt-Jakob disease: Overlap of pathogenic mechanisms
    • DeArmond SJ. Alzheimer's disease and Creutzfeldt-Jakob disease: overlap of pathogenic mechanisms. Current Opinion in Neurology 1993;6:872-881.
    • (1993) Current Opinion in Neurology , vol.6 , pp. 872-881
    • DeArmond, S.J.1
  • 13
    • 0025295039 scopus 로고
    • Cleavage of amyloid b-peptide during constitutive processing of its precursor
    • Esch FS, Keim PS, Beattie EC, et al. Cleavage of amyloid b-peptide during constitutive processing of its precursor. Science 1990;248:1122-1124.
    • (1990) Science , vol.248 , pp. 1122-1124
    • Esch, F.S.1    Keim, P.S.2    Beattie, E.C.3
  • 14
    • 0025818893 scopus 로고
    • The ubiquitin-activating enzyme, El, is required for stress-induced lysosomal degradation of cellular proteins
    • Gropper R, Brandt RA, Elias S, et al. The ubiquitin-activating enzyme, El, is required for stress-induced lysosomal degradation of cellular proteins. J. Biol. Chem. 1991;266:3602-3610.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3602-3610
    • Gropper, R.1    Brandt, R.A.2    Elias, S.3
  • 15
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ. Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 1992;357:500-503.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 16
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta-amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP, Lansbury PT. The carboxy terminus of the beta-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993;32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 17
    • 0028114782 scopus 로고
    • Apolipoprotein E uptake and degradation via chloroquine-sensitive pathway in cultivated monkey cells overexpressing low density lipoprotein receptor
    • Jensen T G, Roses A D and Jorgensen A L. Apolipoprotein E uptake and degradation via chloroquine-sensitive pathway in cultivated monkey cells overexpressing low density lipoprotein receptor. Neurosci. Lett. 1994;180:193-196
    • (1994) Neurosci. Lett. , vol.180 , pp. 193-196
    • Jensen, T.G.1    Roses, A.D.2    Jorgensen, A.L.3
  • 18
    • 0025760931 scopus 로고
    • Multicatalytic proteinase is present in Lewy bodies in neurofibrillary tangles in diffuse Lewy body disease brains
    • Kwak S , Masaki T , Ishiura S. and Sugita H. Multicatalytic proteinase is present in Lewy bodies in neurofibrillary tangles in diffuse Lewy body disease brains. Neurosci. Lett. 1991;128:21-24
    • (1991) Neurosci. Lett. , vol.128 , pp. 21-24
    • Kwak, S.1    Masaki, T.2    Ishiura, S.3    Sugita, H.4
  • 19
    • 0026605853 scopus 로고
    • Lysosomes are key organelles in the pathogensis of prion encephalopathies
    • Laszlo L, Lowe J, Self T, et al. Lysosomes are key organelles in the pathogensis of prion encephalopathies. J. Pathol. 1992;166:333-341.
    • (1992) J. Pathol. , vol.166 , pp. 333-341
    • Laszlo, L.1    Lowe, J.2    Self, T.3
  • 20
    • 0025785896 scopus 로고
    • The latent membrane protein-1 in Epstein-Barr virus-transformed lymphoblastoid cells is found with ubiquitin-protein conjugates and heat-shock protein-70 in lysosomes oriented around the microtubule organizing centre
    • Laszlo L, Tuckwell J, Self T, et al. The latent membrane protein-1 in Epstein-Barr virus-transformed lymphoblastoid cells is found with ubiquitin-protein conjugates and heat-shock protein-70 in lysosomes oriented around the microtubule organizing centre. J. Pathol. 1991;164:203-214.
    • (1991) J. Pathol. , vol.164 , pp. 203-214
    • Laszlo, L.1    Tuckwell, J.2    Self, T.3
  • 22
    • 0024596151 scopus 로고
    • Anti-ubiquitin immunocytochemistry is more sensitive than conventional techniques in the detection of diffuse Lewy body disease
    • Lennox G, Lowe J, Morrell K, Landon M, Mayer RJ. Anti-ubiquitin immunocytochemistry is more sensitive than conventional techniques in the detection of diffuse Lewy body disease. J.Neurol.Neurosurg.Psychiatr. 1989b;52:67-71.
    • (1989) J.Neurol.Neurosurg.Psychiatr. , vol.52 , pp. 67-71
    • Lennox, G.1    Lowe, J.2    Morrell, K.3    Landon, M.4    Mayer, R.J.5
  • 23
    • 0027498124 scopus 로고
    • Immunogold localisation of ubiquitin-protein conjugates in Sf9 insect cells: Implications for the biogenesis of lysosome-related organelles
    • Low P, Doherty FJ, Sass M, Kovacs J, Mayer RJ, Laszlo L. Immunogold localisation of ubiquitin-protein conjugates in Sf9 insect cells: implications for the biogenesis of lysosome-related organelles. FEBS Lett. 1993;316:152-156.
    • (1993) FEBS Lett. , vol.316 , pp. 152-156
    • Low, P.1    Doherty, F.J.2    Sass, M.3    Kovacs, J.4    Mayer, R.J.5    Laszlo, L.6
  • 24
    • 0027407247 scopus 로고
    • Ubiquitin in neurodegenerative diseases
    • Lowe J, Mayer RJ, Landon M. Ubiquitin in neurodegenerative diseases. Brain Pathol. 1993;3:55-65.
    • (1993) Brain Pathol. , vol.3 , pp. 55-65
    • Lowe, J.1    Mayer, R.J.2    Landon, M.3
  • 25
    • 0026452020 scopus 로고
    • Immunoreactivity to ubiquitin-protein conjugates is present early in the disease process in the brains of scrapie-infected mice
    • Lowe J, Fergusson J, Kenward N, et al. Immunoreactivity to ubiquitin-protein conjugates is present early in the disease process in the brains of scrapie-infected mice. J. Pathol. 1992;168:169-177.
    • (1992) J. Pathol. , vol.168 , pp. 169-177
    • Lowe, J.1    Fergusson, J.2    Kenward, N.3
  • 26
    • 0024992208 scopus 로고
    • Ubiquitin, cell stress and diseases of the nervous system
    • Lowe J, Mayer RJ. Ubiquitin, cell stress and diseases of the nervous system. Neuropathol. Appl. Neurobiol. 1990;16:281-291.
    • (1990) Neuropathol. Appl. Neurobiol. , vol.16 , pp. 281-291
    • Lowe, J.1    Mayer, R.J.2
  • 27
    • 0028173205 scopus 로고
    • 1-antichymotrypsin and apolipoprotein e promote assembly of Alzheimer b- Protein into filaments
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer b- protein into filaments. Nature 1994;372:92-94
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer Jr., H.B.3    Das, S.4    Potter, H.5
  • 28
    • 0026777580 scopus 로고
    • Protein processing in lysosomes - The new therapeutic target in neurodegenerative disease
    • Mayer RJ, Landon M, Laszlo L, Lennox G, Lowe J. Protein processing in lysosomes - the new therapeutic target in neurodegenerative disease. Lancet 1992;340:156-159.
    • (1992) Lancet , vol.340 , pp. 156-159
    • Mayer, R.J.1    Landon, M.2    Laszlo, L.3    Lennox, G.4    Lowe, J.5
  • 30
    • 0026326210 scopus 로고
    • Ultrastructural localisation of scrapie prions in cytoplasmic vesicles of infected cultured cells
    • McKinley MP, Taraboulos A, Kenaga L, et al. Ultrastructural localisation of scrapie prions in cytoplasmic vesicles of infected cultured cells. Lab. Invest. 1991;65:622-630.
    • (1991) Lab. Invest. , vol.65 , pp. 622-630
    • McKinley, M.P.1    Taraboulos, A.2    Kenaga, L.3
  • 31
    • 0025971426 scopus 로고
    • Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and Kuru plaque amyloid in Creutzfeldt-Jakob disease
    • Namba Y, Tomonaga M , Kawasaki H , Otomo E and Ikeda K. Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and Kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res. 1991;541:163-166
    • (1991) Brain Res. , vol.541 , pp. 163-166
    • Namba, Y.1    Tomonaga, M.2    Kawasaki, H.3    Otomo, E.4    Ikeda, K.5
  • 32
    • 0027001034 scopus 로고
    • Chemistry and biology of prions
    • Prusiner SB. Chemistry and biology of prions. Biochemistiy 1992;31:12277-12288.
    • (1992) Biochemistiy , vol.31 , pp. 12277-12288
    • Prusiner, S.B.1
  • 33
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB. Molecular biology of prion diseases. Science 1991;252:1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 34
    • 0027459686 scopus 로고
    • Secretion of b-amyloid precursor protein cleaved at the amino terminus of the b-amyloid peptide
    • Seubert P, Oltersdorf T, Lee MG, et al. Secretion of b-amyloid precursor protein cleaved at the amino terminus of the b-amyloid peptide. Nature 1993;361:260-263.
    • (1993) Nature , vol.361 , pp. 260-263
    • Seubert, P.1    Oltersdorf, T.2    Lee, M.G.3
  • 35
    • 0028305135 scopus 로고
    • A glycolipid-anchored prion protein is endocytosed via clathrin coated pits
    • Shyng S -L , Heuser J E and Harris D A. A glycolipid-anchored prion protein is endocytosed via clathrin coated pits. J. Cell Biol. 1994;125:1239-1250
    • (1994) J. Cell Biol. , vol.125 , pp. 1239-1250
    • Shyng, S.L.1    Heuser, J.E.2    Harris, D.A.3
  • 36
    • 0027250352 scopus 로고
    • Processing of the b-amyloid precursor
    • Siman R, Mistretta S, Durkin JT, et al. Processing of the b-amyloid precursor. J. Biol. Chem. 1993;268:16602-16609.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16602-16609
    • Siman, R.1    Mistretta, S.2    Durkin, J.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.