The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions

Journal of Biological Chemistry

Volumn 281, Issue 6, 2006, Pages 3268-3275

  Leliveld, Sirik Rutger ^a   Dame, Remus Thei ^b   Wuite, Gijs J L ^b   Stitz, Lothar ^c   Korth, Carsten ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b VU UNIVERSITY AMSTERDAM   (Netherlands)

^c FEDERAL RESEARCH INSTITUTE FOR ANIMAL HEALTH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; BINDING ENERGY; CONFORMATIONS; GENES; MATHEMATICAL MODELS; PATHOLOGY;

AUTOCATALYTIC MANNER.; CREUTZFELDT JAKOB DISEASE; PRION PROTEIN GENE; SELF-REPLICATING CONVERSION PROCESS;

PROTEINS;

BUFFER; COPPER ION; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MUTANT PROTEIN; POLYMER; PRION PROTEIN; COPPER; OLIGONUCLEOTIDE; PEPTIDE; RECOMBINANT PROTEIN;

ANIMAL TISSUE; ARTICLE; BIOCHEMISTRY; CLUSTER ANALYSIS; CREUTZFELDT JAKOB DISEASE; FAMILIAL DISEASE; GENE MUTATION; NONHUMAN; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; ANIMAL; ATOMIC FORCE MICROSCOPY; BINDING SITE; BIOLOGICAL MODEL; BRAIN; CATALYSIS; CHEMISTRY; CHROMATOGRAPHY; DIMERIZATION; ENZYME LINKED IMMUNOSORBENT ASSAY; HAMSTER; HUMAN; LIGHT; METABOLISM; MOLECULAR CLONING; MUTATION; PRION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; RADIATION SCATTERING; SYRIAN HAMSTER; WESTERN BLOTTING;

ANIMALS; BINDING SITES; BLOTTING, WESTERN; BRAIN; CATALYSIS; CHROMATOGRAPHY; CLONING, MOLECULAR; COPPER; CREUTZFELDT-JAKOB SYNDROME; CRICETINAE; DIMERIZATION; ENZYME-LINKED IMMUNOSORBENT ASSAY; GLUTATHIONE TRANSFERASE; HUMANS; LIGHT; MESOCRICETUS; MICROSCOPY, ATOMIC FORCE; MODELS, BIOLOGICAL; MUTATION; OLIGONUCLEOTIDES; PEPTIDES; PRIONS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SCATTERING, RADIATION;

EID: 33645639813     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M510606200     Document Type: Article

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