Amyloid peptides are toxic via a common oxidative mechanism

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

Volumn 92, Issue 6, 1995, Pages 1989-1993

  Schubert, D ^a   Behl, C ^a,c   Lesley, R ^a   Brack, A ^b   Dargusch, R ^a   Sagara, Y ^a   Kimura, H ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^b CENTRE DE BIOPHYSIQUE MOLÉCULAIRE   (France)

^c MAX PLANCK INSTITUTE OF PSYCHIATRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CELL SURFACE RECEPTOR;

AEROBIC METABOLISM; AMYLOIDOSIS; ANIMAL CELL; ARTICLE; CELL DEATH; ENZYME ACTIVATION; FLOW CYTOMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; RAT;

AMINO ACID SEQUENCE; AMYLOID; AMYLOID BETA-PROTEIN; ANIMAL; ATRIAL NATRIURETIC FACTOR; BRAIN NEOPLASMS; CALCITONIN; CELL LINE; CELL SURVIVAL; COMPARATIVE STUDY; FLOW CYTOMETRY; HUMAN; HYDROGEN PEROXIDE; LACTATE DEHYDROGENASE; MELITTEN; MOLECULAR SEQUENCE DATA; NADH, NADPH OXIDOREDUCTASES; OLIGOPEPTIDES; ONIUM COMPOUNDS; P-METHOXY-N-METHYLPHENETHYLAMINE; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; RATS; STRUCTURE-ACTIVITY RELATIONSHIP; SUPPORT, U.S. GOV'T, P.H.S.; TUMOR CELLS, CULTURED; WASP VENOMS;

ANIMALIA;

EID: 0028957882     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.92.6.1989     Document Type: Article

References (39)