{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T05:34:13Z","timestamp":1779341653514,"version":"3.51.4"},"publisher-location":"Boston, MA","reference-count":36,"publisher":"Springer US","isbn-type":[{"value":"9781461380030","type":"print"},{"value":"9781461303350","type":"electronic"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1996]]},"DOI":"10.1007\/978-1-4613-0335-0_33","type":"book-chapter","created":{"date-parts":[[2011,9,19]],"date-time":"2011-09-19T17:41:45Z","timestamp":1316454105000},"page":"261-269","source":"Crossref","is-referenced-by-count":40,"title":["Endosome-Lysosomes, Ubiquitin and Neurodegeneration"],"prefix":"10.1007","author":[{"given":"R. John","family":"Mayer","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carron","family":"Tipler","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jane","family":"Arnold","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lajos","family":"Laszlo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Abdulaziz","family":"Al-Khedhairy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"James","family":"Lowe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Landon","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","reference":[{"key":"33_CR1","doi-asserted-by":"crossref","unstructured":"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.","DOI":"10.1002\/path.1711760412"},{"key":"33_CR2","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1016\/0014-4886(89)90156-8","volume":"106","author":"LI Benowitz","year":"1989","unstructured":"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\u2013250.","journal-title":"Exp. Neurol"},{"key":"33_CR3","doi-asserted-by":"crossref","first-page":"16188","DOI":"10.1016\/S0021-9258(18)41985-0","volume":"267","author":"DR Borchelt","year":"1992","unstructured":"Borchelt DR, Taraboulos A, Prusiner SB. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 1992;267:16188\u201316199.","journal-title":"J. Biol. Chem"},{"key":"33_CR4","doi-asserted-by":"publisher","first-page":"1339","DOI":"10.1016\/0092-8674(93)90360-3","volume":"73","author":"H Bueler","year":"1993","unstructured":"Bueler H, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993;73:1339\u20131347.","journal-title":"Cell"},{"key":"33_CR5","doi-asserted-by":"publisher","first-page":"577","DOI":"10.1038\/356577a0","volume":"356","author":"H Bueler","year":"1992","unstructured":"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\u2013582.","journal-title":"Nature"},{"key":"33_CR6","first-page":"283","volume":"2","author":"EJ Byrne","year":"1991","unstructured":"Byrne EJ, Lennox GG, Godwin-Austen RB, et al. Dementia associated with cortical Lewy bodies: proposed clinical diagnostic criteria. Dementia 1991;2:283\u2013284.","journal-title":"Dementia"},{"key":"33_CR7","doi-asserted-by":"publisher","first-page":"10998","DOI":"10.1073\/pnas.88.24.10998","volume":"88","author":"AM Cataldo","year":"1991","unstructured":"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\u201311002.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"33_CR8","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1126\/science.1323144","volume":"257","author":"C Cenciarelli","year":"1992","unstructured":"Cenciarelli C, Hou D, Hsu KC, et al. Activation-induced ubiquitination of the T-cell antigen receptor. Science 1992;257:795\u2013797.","journal-title":"Science"},{"key":"33_CR9","first-page":"7","volume":"336","author":"J Collinge","year":"1990","unstructured":"Collinge J, Owen F, Poulter M, et al. Prion dementia without characteristic pathology. Lancet 1990;336:7\u20139.","journal-title":"Prion dementia without characteristic pathology. Lancet"},{"key":"33_CR10","doi-asserted-by":"publisher","first-page":"921","DOI":"10.1126\/science.8346443","volume":"261","author":"EH Corder","year":"1993","unstructured":"Corder E H, Saunders AM, Strittmatter, W.J., et al. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer\u2019s disease in late-onset families. Science 1993;261:921\u2013923.","journal-title":"Science"},{"key":"33_CR11","doi-asserted-by":"publisher","first-page":"872","DOI":"10.1097\/00019052-199312000-00008","volume":"6","author":"SJ DeArmond","year":"1993","unstructured":"DeArmond SJ. Alzheimer\u2019s disease and Creutzfeldt-Jakob disease: overlap of pathogenic mechanisms. Current Opinion in Neurology 1993;6:872\u2013881.","journal-title":"Current Opinion in Neurology"},{"key":"33_CR12","first-page":"87","volume":"63","author":"DW Dickson","year":"1990","unstructured":"Dickson DW, Wertkin A, Kress Y, Ksiezak-Reding H, Yen S-H. Ubiquitin immunoreactive structures in normal human brains. Lab. Invest. 1990;63:87\u201399.","journal-title":"Lab. Invest"},{"key":"33_CR13","doi-asserted-by":"publisher","first-page":"1122","DOI":"10.1126\/science.2111583","volume":"248","author":"FS Esch","year":"1990","unstructured":"Esch FS, Keim PS, Beattie EC, et al. Cleavage of amyloid b-peptide during constitutive processing of its precursor. Science 1990;248:1122\u20131124.","journal-title":"Science"},{"key":"33_CR14","doi-asserted-by":"crossref","first-page":"3602","DOI":"10.1016\/S0021-9258(19)67837-3","volume":"266","author":"R Gropper","year":"1991","unstructured":"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\u20133610.","journal-title":"J. Biol. Chem"},{"key":"33_CR15","doi-asserted-by":"publisher","first-page":"500","DOI":"10.1038\/357500a0","volume":"357","author":"C Haass","year":"1992","unstructured":"Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ. Targeting of cell-surface \u00df-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 1992;357:500\u2013503.","journal-title":"Nature"},{"key":"33_CR16","doi-asserted-by":"publisher","first-page":"4693","DOI":"10.1021\/bi00069a001","volume":"32","author":"JT Jarrett","year":"1993","unstructured":"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\u2019s disease. Biochemistry 1993;32:4693\u20134697.","journal-title":"Biochemistry"},{"key":"33_CR17","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1016\/0304-3940(94)90519-3","volume":"180","author":"TG Jensen","year":"1994","unstructured":"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\u2013196.","journal-title":"Neurosci. Lett."},{"key":"33_CR18","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1016\/0304-3940(91)90751-E","volume":"128","author":"S Kwak","year":"1991","unstructured":"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\u201324.","journal-title":"Neurosci. Lett"},{"key":"33_CR19","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1002\/path.1711660404","volume":"166","author":"L Laszlo","year":"1992","unstructured":"Laszlo L, Lowe J, Self T, et al. Lysosomes are key organelles in the pathogensis of prion encephalopathies. J. Pathol. 1992;166:333\u2013341.","journal-title":"J. Pathol"},{"key":"33_CR20","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1002\/path.1711640305","volume":"164","author":"L Laszlo","year":"1991","unstructured":"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\u2013214.","journal-title":"J. Pathol"},{"key":"33_CR21","doi-asserted-by":"publisher","first-page":"1236","DOI":"10.1136\/jnnp.52.11.1236","volume":"52","author":"G Lennox","year":"1989","unstructured":"Lennox G, Lowe J, Landon M, Byrne EJ, Mayer RJ, Godwin-Austen RB. Diffuse Lewy body disease: correlative neuropathology using anti-ubiquitin immunocytochemistry. J. Neurol. Neurosurg. Psychiatr. 1989a;52:1236\u20131247.","journal-title":"J. Neurol. Neurosurg. Psychiatr"},{"key":"33_CR22","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1136\/jnnp.52.1.67","volume":"52","author":"G Lennox","year":"1989","unstructured":"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\u201371.","journal-title":"J. Neurol. Neurosurg. Psychiatr"},{"key":"33_CR23","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1016\/0014-5793(93)81205-E","volume":"316","author":"P Low","year":"1993","unstructured":"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\u2013156.","journal-title":"FEBS Lett"},{"key":"33_CR24","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1111\/j.1750-3639.1993.tb00726.x","volume":"3","author":"J Lowe","year":"1993","unstructured":"Lowe J, Mayer RJ, Landon M. Ubiquitin in neurodegenerative diseases. Brain Pathol. 1993;3:55\u201365.","journal-title":"Brain Pathol"},{"key":"33_CR25","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1002\/path.1711680204","volume":"168","author":"J Lowe","year":"1992","unstructured":"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\u2013177.","journal-title":"J. Pathol"},{"key":"33_CR26","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1111\/j.1365-2990.1990.tb01263.x","volume":"16","author":"J Lowe","year":"1990","unstructured":"Lowe J, Mayer RJ. Ubiquitin, cell stress and diseases of the nervous system. Neuropathol. Appl. Neurobiol. 1990;16:281\u2013291.","journal-title":"Neuropathol. Appl. Neurobiol"},{"key":"33_CR27","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1038\/372092a0","volume":"372","author":"J Ma","year":"1994","unstructured":"Ma J, Yee A, Brewer H.B Jnr, Das S and Potter H. Amyloid-associated proteins a1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer b- protein into filaments. Nature 1994;372:92\u201394.","journal-title":"Nature"},{"key":"33_CR28","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1016\/0140-6736(92)93224-B","volume":"340","author":"RJ Mayer","year":"1992","unstructured":"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\u2013159.","journal-title":"Lancet"},{"key":"33_CR29","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/0167-4781(91)90002-4","volume":"1089","author":"RJ Mayer","year":"1991","unstructured":"Mayer RJ, Arnold J, Laszlo L, Landon M, Lowe J. Ubiquitin in health and disease. Biochim. Biophys. Acta 1991;1089:141\u2013157.","journal-title":"Biochim. Biophys. Acta"},{"key":"33_CR30","first-page":"622","volume":"65","author":"MP McKinley","year":"1991","unstructured":"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\u2013630.","journal-title":"Lab. Invest"},{"key":"33_CR31","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1016\/0006-8993(91)91092-F","volume":"541","author":"Y Namba","year":"1991","unstructured":"Namba Y, Tomonaga M, Kawasaki H, Otomo E and Ikeda K. Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer\u2019s disease and Kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res. 1991;541:163\u2013166.","journal-title":"Brain Res"},{"key":"33_CR32","doi-asserted-by":"publisher","first-page":"12277","DOI":"10.1021\/bi00164a001","volume":"31","author":"SB Prusiner","year":"1992","unstructured":"Prusiner SB. Chemistry and biology of prions. Biochemistry 1992;31:12277\u201312288.","journal-title":"Biochemistry"},{"key":"33_CR33","doi-asserted-by":"publisher","first-page":"1515","DOI":"10.1126\/science.1675487","volume":"252","author":"SB Prusiner","year":"1991","unstructured":"Prusiner SB. Molecular biology of prion diseases. Science 1991;252:1515\u20131522.","journal-title":"Science"},{"key":"33_CR34","doi-asserted-by":"publisher","first-page":"260","DOI":"10.1038\/361260a0","volume":"361","author":"P Seubert","year":"1993","unstructured":"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\u2013263.","journal-title":"Nature"},{"key":"33_CR35","doi-asserted-by":"publisher","first-page":"1239","DOI":"10.1083\/jcb.125.6.1239","volume":"125","author":"S-L Shyng","year":"1994","unstructured":"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\u20131250.","journal-title":"J. Cell Biol"},{"key":"33_CR36","doi-asserted-by":"crossref","first-page":"16602","DOI":"10.1016\/S0021-9258(19)85462-5","volume":"268","author":"R Siman","year":"1993","unstructured":"Siman R, Mistretta S, Durkin JT, et al. Processing of the b-amyloid precursor. J. Biol. Chem. 1993;268:16602\u201316609.","journal-title":"J. Biol. Chem"}],"container-title":["Advances in Experimental Medicine and Biology","Intracellular Protein Catabolism"],"original-title":[],"link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-4613-0335-0_33.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,5]],"date-time":"2021-12-05T11:48:21Z","timestamp":1638704901000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/978-1-4613-0335-0_33"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996]]},"ISBN":["9781461380030","9781461303350"],"references-count":36,"URL":"https:\/\/doi.org\/10.1007\/978-1-4613-0335-0_33","relation":{},"ISSN":["0065-2598"],"issn-type":[{"value":"0065-2598","type":"print"}],"subject":[],"published":{"date-parts":[[1996]]}}}