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Cataldo, A. M., Paskevich, P. A., Kominami, E., Nixon, R. A. (1991) Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proceedings of the National Academy of Sciences, 88 (24) 10998-11002 doi:10.1073/pnas.88.24.10998

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Reference TypeJournal (article/letter/editorial)
TitleLysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease.
JournalProceedings of the National Academy of Sciences
AuthorsCataldo, A. M.Author
Paskevich, P. A.Author
Kominami, E.Author
Nixon, R. A.Author
Year1991 (December 15)Volume88
Issue24
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.88.24.10998Search in ResearchGate
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Mindat Ref. ID1504004Long-form Identifiermindat:1:5:1504004:2
GUID0
Full ReferenceCataldo, A. M., Paskevich, P. A., Kominami, E., Nixon, R. A. (1991) Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proceedings of the National Academy of Sciences, 88 (24) 10998-11002 doi:10.1073/pnas.88.24.10998
Plain TextCataldo, A. M., Paskevich, P. A., Kominami, E., Nixon, R. A. (1991) Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proceedings of the National Academy of Sciences, 88 (24) 10998-11002 doi:10.1073/pnas.88.24.10998
In(1991, December) Proceedings of the National Academy of Sciences Vol. 88 (24) Proceedings of the National Academy of Sciences

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(1992) Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proceedings of the National Academy of Sciences, 89 (6) 2509 doi:10.1073/pnas.89.6.2509-a
Cataldo, A. M., Nixon, R. A. (1990) Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proceedings of the National Academy of Sciences, 87 (10) 3861-3865 doi:10.1073/pnas.87.10.3861
Crowther, R. A. (1991) Straight and paired helical filaments in Alzheimer disease have a common structural unit. Proceedings of the National Academy of Sciences, 88 (6) 2288-2292 doi:10.1073/pnas.88.6.2288
Papasozomenos, S. C., Su, Y. (1991) Altered phosphorylation of tau protein in heat-shocked rats and patients with Alzheimer disease. Proceedings of the National Academy of Sciences, 88 (10) 4543-4547 doi:10.1073/pnas.88.10.4543
Saitoh, T., Dobkins, K. R. (1986) Increased in vitro phosphorylation of a Mr 60,000 protein in brain from patients with Alzheimer disease. Proceedings of the National Academy of Sciences, 83 (24) 9764-9767 doi:10.1073/pnas.83.24.9764
Flood, J. F., Morley, J. E., Roberts, E. (1991) Amnestic effects in mice of four synthetic peptides homologous to amyloid beta protein from patients with Alzheimer disease. Proceedings of the National Academy of Sciences, 88 (8) 3363-3366 doi:10.1073/pnas.88.8.3363
NIXON, RALPH A., CATALDO, ANNE M., PASKEVICH, PETER A., HAMILTON, DEBORAH J., WHEELOCK, TIMOTHY R., KANALEY-ANDREWS, LISA (1992) The Lysosomal System in Neurons. Annals of the New York Academy of Sciences, 674 (1) 65-88 doi:10.1111/j.1749-6632.1992.tb27478.x
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., Markesbery, W. R. (1991) Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proceedings of the National Academy of Sciences, 88 (23) 10540-10543 doi:10.1073/pnas.88.23.10540
(1995) Advanced Maillard reaction end products are associated with Alzheimer disease pathology. Proceedings of the National Academy of Sciences, 92 (5) 1794 doi:10.1073/pnas.92.5.1794e
Harrington, C. R., Mukaetova-Ladinska, E. B., Hills, R., Edwards, P. C., Montejo de Garcini, E., Novak, M., Wischik, C. M. (1991) Measurement of distinct immunochemical presentations of tau protein in Alzheimer disease. Proceedings of the National Academy of Sciences, 88 (13) 5842-5846 doi:10.1073/pnas.88.13.5842
Tate-Ostroff, B., Majocha, R. E., Marotta, C. A. (1989) Identification of cellular and extracellular sites of amyloid precursor protein extracytoplasmic domain in normal and Alzheimer disease brains. Proceedings of the National Academy of Sciences, 86 (2) 745-749 doi:10.1073/pnas.86.2.745
 
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