Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Science

Volumn 300, Issue 5618, 2003, Pages 486-489

  Kayed, Rakez ^a   Head, Elizabeth ^a   Thompson, Jennifer L ^a   McIntire, Theresa M ^a   Milton, Saskia C ^a   Cotman, Carl W ^a   Glabel, Charles G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BRAIN; CONFORMATIONS; TOXICITY;

ALZHEIMER'S DISEASE;

OLIGOMERS;

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; HUMAN INSULIN; IMMUNOGLOBULIN G; LACTATE DEHYDROGENASE; LYSOZYME; OLIGOMER; POLYCLONAL ANTIBODY; POLYGLUTAMINE; PRION PROTEIN;

PATHOGEN; TOXICITY;

ALZHEIMER DISEASE; ANTIBODY SPECIFICITY; ARTICLE; CONTROLLED STUDY; CYTOTOXICITY; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; HUMAN CELL; IMMUNOREACTIVITY; NEUROBLASTOMA CELL; NEUROLOGIC DISEASE; NEUROTOXICITY; PRIORITY JOURNAL;

AGED; AGED, 80 AND OVER; ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PROTEIN; ANIMALS; ANTIBODIES; ANTIBODY SPECIFICITY; BIOPOLYMERS; BRAIN; BRAIN CHEMISTRY; CELL SURVIVAL; HUMANS; MICROSCOPY, CONFOCAL; MICROSCOPY, ELECTRON; MOLECULAR MIMICRY; NEUROFIBRILLARY TANGLES; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RABBITS; SOLUBILITY; TUMOR CELLS, CULTURED;

EID: 0242668337     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1079469     Document Type: Article

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19. This work was supported by NIH grants NS31230, AG00538, and AG16573 and by a grant from the Larry L. Hillblom foundation. We are grateful to D. A. Brant, Department of Chemistry, University of California, Irvine, for his support; R. Wetzel for providing the polyglutamine peptide; F. Saroza for technical assistance; and R. Langen for providing α-synuclein. R.K. thanks K. Sweimeh and Y. Al-Abed for helpful discussions.