Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 24, 2007, Pages 10252-10257

  Wang, Y P ^a   Biernat, J ^a   Pickhardt, M ^a   Mandelkow, E ^a   Mandelkow, E M ^a  

^a MAX PLANCK UNIT FOR STRUCTURAL MOLECULAR BIOLOGY   (Germany)

Author keywords

Alzheimer's disease; Frontotemporal dementia; Paired helical filaments; Tau protein

Indexed keywords

LACTATE DEHYDROGENASE; TAU PROTEIN; ISOPROTEIN; PEPTIDE FRAGMENT; PEPTIDE HYDROLASE; THROMBIN;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; CHROMOSOME 17; CYTOTOXICITY; DEMENTIA; ENZYME ASSAY; FRONTOTEMPORAL DEMENTIA; GENE MUTATION; MODEL; MOUSE; NERVE CELL; NEUROLOGIC DISEASE; NONHUMAN; PAIRED HELICAL FILAMENT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN PROCESSING; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL; BINDING SITE; BIOLOGICAL MODEL; CHEMICAL MODEL; CHEMISTRY; FLUORESCENCE MICROSCOPY; FLUORESCENT ANTIBODY TECHNIQUE; GENETICS; HUMAN; HYDROLYSIS; METABOLISM; NEUROBLASTOMA; PATHOLOGY; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SOLUBILITY; TUMOR CELL LINE;

ALZHEIMER DISEASE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CELL LINE, TUMOR; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; HUMANS; HYDROLYSIS; MICE; MICROSCOPY, FLUORESCENCE; MODELS, BIOLOGICAL; MODELS, CHEMICAL; NEUROBLASTOMA; NEURONS; PEPTIDE FRAGMENTS; PEPTIDE HYDROLASES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLUBILITY; TAU PROTEINS; THROMBIN;

EID: 34547203592     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0703676104     Document Type: Article

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