Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans

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

Volumn 104, Issue 18, 2007, Pages 7546-7551

  Yin, Shaoman ^a   Pham, Nancy ^b   Yu, Shuiliang ^a   Li, Chaoyang ^a   Wong, Poki ^a   Chang, Binggong ^a   Kang, Shin Chung ^a   Biasini, Emiliano ^c   Tien, Po ^d   Harris, David A ^c   Sy, Man Sun ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b CASE WESTERN RESERVE UNIVERSITY   (United States)

^c WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d INSTITUTE OF MICROBIOLOGY   (China)

Author keywords

Genetics; Structure

Indexed keywords

GLYCOSAMINOGLYCAN; MONOCLONAL ANTIBODY; MUTANT PROTEIN; OCTAPEPTIDE; PRION PROTEIN; RECOMBINANT PROTEIN; EPITOPE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; DEGENERATIVE DISEASE; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; GENE MUTATION; IMMUNOBLOTTING; MALE; MOUSE; NEUROLOGIC DISEASE; NONHUMAN; PATHOGENESIS; POINT MUTATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRION DISEASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN MOTIF; TRANSGENIC MOUSE; ANIMAL; BINDING SITE; GENETICS; HUMAN; IMMUNOLOGY; METABOLISM; MUTATION; PATHOGENICITY; PRION; PROTEIN BINDING;

MUS MUSCULUS;

ANIMALS; BINDING SITES; EPITOPES; GLYCOSAMINOGLYCANS; HUMANS; MICE; MICE, TRANSGENIC; MUTATION; PRIONS; PROTEIN BINDING;

EID: 34250644988     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0610827104     Document Type: Article

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