Mechanism of lysophosphatidic acid-induced amyloid fibril formation of β2-microglobulin in vitro under physiological conditions

Biochemistry

Volumn 48, Issue 24, 2009, Pages 5689-5699

  Pál Gábor, Henriett ^a,b   Gombos, Linda ^a   Micsonai, András ^a   Kovács, Erika ^b   Petrik, Éva ^a   Kovács, János ^a   Gráf, László ^a   Fidy, Judit ^c   Naiki, Hironobu ^d   Goto, Yuji ^e   Liliom, Károly ^b   Kardos, József ^a  

^a EÖTVÖS LORÁND UNIVERSITY   (Hungary)

^b INSTITUTE OF ENZYMOLOGY   (Hungary)

^c SEMMELWEIS UNIVERSITY OF MEDICINE   (Hungary)

^d UNIVERSITY OF FUKUI   (Japan)

^e OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; AMYLOID FORMATION; COMPLEX MECHANISMS; CONFORMATIONAL FLEXIBILITY; DIALYSIS-RELATED AMYLOIDOSIS; ELEVATED CONCENTRATIONS; FLUORESCENCE AND CD SPECTROSCOPY; HIGH AFFINITY; IN-VITRO; IN-VIVO; ISOTHERMAL TITRATION CALORIMETRY; LYSOPHOSPHATIDIC ACID; MOLECULAR ORGANIZATION; NEUTRAL PH; PHYSIOLOGICAL CONDITION; PROTEOLYTIC DIGESTION; STABILIZING EFFECTS;

ACIDS; CALORIMETRY; CRITICAL MICELLE CONCENTRATION; DIALYSIS; GLYCOPROTEINS; PHOSPHOLIPIDS;

MICELLES;

AMYLOID BETA PROTEIN; BETA 2 MICROGLOBULIN; LYSOPHOSPHATIDIC ACID; PHOSPHOLIPID DERIVATIVE;

ACIDITY; ARTICLE; BINDING AFFINITY; CELL NUCLEUS; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; DEPOLYMERIZATION; FLUORESCENCE SPECTROSCOPY; ISOTHERMAL TITRATION CALORIMETRY; MICELLE; MOLECULAR MECHANICS; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STRUCTURE;

AMYLOID; BETA 2-MICROGLOBULIN; BINDING SITES; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; LYSOPHOSPHOLIPIDS; MODELS, MOLECULAR; OSMOLAR CONCENTRATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE;

EID: 67649213707     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900356r     Document Type: Article

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