Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis

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

Volumn 114, Issue 32, 2017, Pages E6507-E6515

  Jayaraman, Shobini ^a   Gantz, Donald L ^a   Haupt, Christian ^b   Gursky, Olga ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ULM   (Germany)

Author keywords

Acute phase reactant; Hydrophobic cavities; Intrinsically disordered proteins; pH induced conformational changes; Prefibrillar amyloid oligomers

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; DIMER; GLUTARALDEHYDE; MONOMER; OLIGOMER; POLYMER; SERUM AMYLOID A; THIOFLAVINE; TRIMER; UNCLASSIFIED DRUG;

AA AMYLOIDOSIS; ALPHA HELIX; ANTIGEN BINDING; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CROSS LINKING; ENERGY TRANSFER; HYSTERESIS; LIPID BILAYER; LIPID MEMBRANE; LIPID VESICLE; LYSOSOMAL PH; LYSOSOME; NATIVE POLYACRYLAMIDE GEL ELECTROPHORESIS; NONHUMAN; PATHOGENESIS; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE; TEMPERATURE DEPENDENCE; THERMOSTABILITY; AMYLOIDOSIS; ANIMAL; CHEMISTRY; INTRACELLULAR MEMBRANE; METABOLISM; MOUSE; PATHOLOGY; PROTEIN MULTIMERIZATION;

AMYLOIDOSIS; ANIMALS; HYDROGEN-ION CONCENTRATION; INTRACELLULAR MEMBRANES; LYSOSOMES; MICE; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SERUM AMYLOID A PROTEIN;

EID: 85026881634     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1707120114     Document Type: Article

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