An amyloid-forming segment of β2-microglobulin suggests a molecular model for the fibril

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

Volumn 101, Issue 29, 2004, Pages 10584-10589

  Ivanova, Magdalena I ^a   Sawaya, Michael R ^a   Gingery, Mari ^a   Attinger, Antoine ^b   Eisenberg, David ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LA JOLLA INSTITUTE FOR ALLERGY AND IMMUNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN;

AMYLOIDOSIS; ANIMAL CELL; ARTICLE; BETA SHEET; DIALYSIS; FIBER; HUMAN; HUMAN CELL; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RESIDUE ANALYSIS; SEQUENCE ANALYSIS; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; BETA 2-MICROGLOBULIN; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; X-RAY DIFFRACTION;

ANIMALIA;

EID: 3242735504     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0403756101     Document Type: Article

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