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Volumn 416, Issue 6880, 2002, Pages 507-511
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Author keywords
[No Author keywords available]
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Indexed keywords
AGGLOMERATION;
BIOLOGICAL MATERIALS PRESERVATION;
ESCHERICHIA COLI;
PROTEINS;
TOXICITY;
FIBRILS;
DISEASES;
PROTEIN;
ALZHEIMER DISEASE;
ARTICLE;
BRAIN SPONGIOSIS;
CELL FUNCTION;
CYTOTOXICITY;
DEGENERATIVE DISEASE;
ELECTRON MICROSCOPY;
NERVE DEGENERATION;
NONHUMAN;
PATHOGENICITY;
PRIORITY JOURNAL;
PROTEIN AGGREGATION;
PROTEIN FAMILY;
PROTEIN FOLDING;
TOXICITY TESTING;
1-PHOSPHATIDYLINOSITOL 3-KINASE;
3T3 CELLS;
ALZHEIMER DISEASE;
ANIMALS;
BACTERIAL PROTEINS;
CYTOTOXINS;
EVOLUTION;
HUMANS;
MICE;
NEURODEGENERATIVE DISEASES;
PC12 CELLS;
PROTEIN FOLDING;
RATS;
RECOMBINANT PROTEINS;
SENILE PLAQUES;
SRC HOMOLOGY DOMAINS;
BOVINAE;
ESCHERICHIA COLI;
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EID: 0037041420
PISSN: 00280836
EISSN: None
Source Type: Journal
DOI: 10.1038/416507a Document Type: Article |
Times cited : (2228)
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References (34)
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