Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature

Biochemistry

Volumn 50, Issue 43, 2011, Pages 9184-9191

  Ye, Zhuqiu ^a   Bayron Poueymiroy, Diane ^b   Aguilera, J Javier ^a   Srinivasan, Saipraveen ^a   Wang, Yun ^a   Serpell, Louise C ^c   Colòn, Wilfredo ^a  

^a Rensselaer Polytechnic Institute   (United States)

^b UNIVERSITY OF PUERTO RICO   (Puerto Rico)

^c UNIVERSITY OF SUSSEX   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOIDOGENICITY; CHEMICAL DENATURATION; GLOBULAR PROTEINS; GLUTARALDEHYDE CROSS-LINKING; HIGH STABILITY; IN-VITRO; IN-VIVO; INFLAMMATORY RESPONSE; PHYSIOLOGICAL TEMPERATURE; SERUM AMYLOID A; THIOFLAVIN T;

ALDEHYDES; CHEMICAL STABILITY; GLYCOPROTEINS; METABOLISM; PATHOLOGY; PHYSIOLOGICAL MODELS; PHYSIOLOGY; UREA;

PROTEINS;

AMYLOID; AMYLOID PROTEIN; GLOBULAR PROTEIN; PLASMA PROTEIN; PROTEIN SERUM AMYLOID A 2.2; THIOFLAVINE; UNCLASSIFIED DRUG; UREA;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; IN VITRO STUDY; INFLAMMATION; MOUSE; NONHUMAN; PHYSIOLOGICAL PROCESS; PLASMA; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STRUCTURE;

AMYLOID; AMYLOIDOSIS; ANIMALS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MICE; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; SERUM AMYLOID A PROTEIN; TEMPERATURE; THIAZOLES;

MURINAE;

EID: 80054969302     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200856v     Document Type: Article

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