TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 270, No. 16, Issue of April 21, pp, 9564-9570, 1995 © 1995 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Aggregation of Secreted Amyloid I3-Protein into Sodium Dodecyl Sulfate-stable Oligomers in Cell Culture* (Received for publication, January 17, 1995) Marcia B. Podlisny, Beth L. Ostaszewski, Sharon L. Squazzo, Edward H. Koo, Russell E. Rydell:j:, David B. Teplow§, and Dennis J. Selkoe From the Department of Neurology and Program in Neuroscience, Harvard Medical School, the Center for Neurologic Diseases and §Biopolymer Laboratory, Brigham and Women's Hospital Boston, Massachusetts 02115, and :!Athena Neurosciences, Inc., South San Francisco, California 94080 Filamentous aggregates of the 40-42-residue amyloid chromosome 21 (2). Cerebral deposits of AJ3 can exist as dense, Il-protein (Am accumulate progressively in the limbic filamentous aggregates of the peptide surrounded by dystro­ and cerebral cortex in Alzheimer's disease, where they phic neurites and glial cells (classical or neuritic amyloid are intimately associated with neuronal and glial cyto­ plaques) and as loose, amorphous deposits associated with pathology. Attempts to model this cytotoxicity in vitro little or no local cellular alteration (diffuse or preamyloid using synthetic peptides have shown that monomeric All plaques). 
TI - Aggregation of Secreted Amyloid β-Protein into Sodium Dodecyl Sulfate-stable Oligomers in Cell Culture
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.270.16.9564
DA - 1995-04-01
UR - https://www.deepdyve.com/lp/unpaywall/aggregation-of-secreted-amyloid-protein-into-sodium-dodecyl-sulfate-ScBxOQN9FM
DP - DeepDyve
ER -