Amyloid ion channels: A common structural link for protein-misfolding disease

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

Volumn 102, Issue 30, 2005, Pages 10427-10432

  Quist, Arjan ^a   Doudevski, Ivo ^a   Lin, Hai ^b   Azimova, Rushana ^c   Ng, Douglas ^d   Frangione, Blas ^d   Kagan, Bruce ^c   Ghiso, Jorge ^d   Lal, Ratnesh ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF PITTSBURGH   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d NEW YORK UNIVERSITY   (United States)

Author keywords

3D structure; Atomic force microscopy; Misfolding protein; Peptide ion channel; Protein conformational disease

Indexed keywords

ABRI PROTEIN; ADAN PROTEIN; ALPHA SYNUCLEIN; AMYLIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID PROTEIN; ION CHANNEL; SERUM AMYLOID A; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ELECTROPHYSIOLOGY; GEL ELECTROPHORESIS; HUNTINGTON CHOREA; PARKINSON DISEASE; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING;

AMYLOID; AMYLOIDOSIS; CIRCULAR DICHROISM; ELECTROPHORESIS; ELECTROPHYSIOLOGY; ION CHANNELS; MICROSCOPY, ATOMIC FORCE; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 23044449398     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0502066102     Document Type: Article

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