High-throughput analysis of ultrasonication-forced amyloid fibrillation reveals the mechanism underlying the large fluctuation in the lag time

Journal of Biological Chemistry

Volumn 289, Issue 39, 2014, Pages 27290-27299

  Umemoto, Ayaka ^a   Yagi, Hisashi ^a,b   So, Masatomo ^a   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b Dept of Chemistry and Biotechnology Graduate School of Engineering Center for Research on Green Sustainable Chemistry   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEINS; SUPERSATURATION;

COEFFICIENT OF VARIATION; HIGH-THROUGHPUT ANALYSIS; LAG-TIME; ULTRA-SONICATION;

PROTEINS;

AMYLOID; IODIDE; LYSOZYME;

ANALYTICAL EQUIPMENT; ARTICLE; CHEMICAL PARAMETERS; CHEMICAL PROCEDURES; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTALLIZATION; HIGH THROUGHPUT SEQUENCING; LAG TIME; PHASE TRANSITION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FIBRILLATION; PROTEIN MODIFICATION; ULTRASONICATION; ANIMAL; CHEMICAL MODEL; CHEMISTRY; CHICKEN; HUMAN; OXIDATION REDUCTION REACTION; PH; SOUND;

AMYLOID; ANIMALS; CHICKENS; HUMANS; HYDROGEN-ION CONCENTRATION; IODIDES; MODELS, CHEMICAL; MURAMIDASE; OXIDATION-REDUCTION; SOUND;

EID: 84907452402     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.569814     Document Type: Article

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