Protein Folding Symposium #9. From hexamer to amyloid: Marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature

Amyloid

Volumn 12, Issue 3, 2005, Pages 139-148

  Wang, Limin ^c   Lashuel, Hilal A ^b   Colón, Wilfredo ^a,d  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^b BRIGHAM AND WOMEN S HOSPITAL   (United States)

^c MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^d Research Rensselaer Polytechnic Institute   (United States)

Author keywords

Aggregation; Amyloidosis; Apolipoprotein; Inflammation; Misfolding; Serum amyloid A

Indexed keywords

AMYLOID; APOLIPOPROTEIN; SERUM AMYLOID A; PEPTIDE HYDROLASE; SAA2 PROTEIN, MOUSE;

AMINO TERMINAL SEQUENCE; CONFERENCE PAPER; FIBER; INCUBATION TIME; LIGAND BINDING; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; SEDIMENTATION; STATISTICAL SIGNIFICANCE; TEMPERATURE; ULTRACENTRIFUGATION; AMINO ACID SEQUENCE; AMYLOIDOSIS; ANIMAL; ARTICLE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN QUATERNARY STRUCTURE; THERMODYNAMICS;

AMINO ACID SEQUENCE; AMYLOIDOSIS; ANIMALS; APOLIPOPROTEINS; MICE; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; SERUM AMYLOID A PROTEIN; TEMPERATURE; THERMODYNAMICS;

EID: 27144480726     PISSN: 13506129     EISSN: 17442818     Source Type: Journal    
DOI: 10.1080/13506120500223084     Document Type: Conference Paper

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