Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin roles of shear flow, hydrophobic surfaces, and α-crystallin

Journal of Biological Chemistry

Volumn 288, Issue 43, 2013, Pages 30917-30930

  Mangione, P Patrizia ^a,b   Esposito, Gennaro ^c   Relini, Annalisa ^d   Raimondi, Sara ^b   Porcari, Riccardo ^a   Giorgetti, Sofia ^b   Corazza, Alessandra ^c   Fogolari, Federico ^c   Penco, Amanda ^d   Goto, Yuji ^e   Lee, Young Ho ^e   Yagi, Hisashi ^e   Cecconi, Ciro ^f   Naqvi, Mohsin M ^g   Gillmore, Julian D ^a   Hawkins, Philip N ^a   Chiti, Fabrizio ^h   Rolandi, Ranieri ^d   Taylor, Graham W ^a   Pepys, Mark B ^a   Stoppini, Monica ^b   Bellotti, Vittorio ^a,b   more..

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF PAVIA   (Italy)

^c UNIVERSITY OF UDINE   (Italy)

^d UNIVERSITY OF GENOA   (Italy)

^e OSAKA UNIVERSITY   (Japan)

^f CNR   (Italy)

^g UNIVERSITY OF MODENA AND REGGIO EMILIA   (Italy)

^h UNIVERSITY OF FLORENCE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID DEPOSITION; CHAPERONE ACTIVITY; EXTRACELLULAR CONDITIONS; HYDROPHOBIC SURFACES; HYDROPHOBIC-HYDROPHILIC; INSOLUBLE FIBRILS; NATURALLY OCCURRING; SYSTEMIC AMYLOIDOSIS;

DISEASES; GLYCOPROTEINS; HYDROPHOBICITY; INTERFACE STATES; PHYSIOLOGY; SHEAR FLOW; SURFACE CHEMISTRY;

PROTEINS;

ALPHA CRYSTALLIN; AMYLOID; BETA 2 MICROGLOBULIN;

AMYLOIDOGENESIS; ARTICLE; CONTROLLED STUDY; FLUID FLOW; HYDROPHILICITY; HYDROPHOBICITY; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN STRUCTURE; SHEAR FLOW; SURFACE PROPERTY; WILD TYPE;

AMYLOID; CHAPERONES; D76N Β2-MICROGLOBULIN; PROTEIN AGGREGATION; PROTEIN MISFOLDING; PROTEIN STABILITY; SHEAR STRESS; SYSTEMIC AMYLOIDOSIS;

ALPHA-CRYSTALLINS; AMINO ACID SUBSTITUTION; AMYLOID; AMYLOIDOSIS, FAMILIAL; BETA 2-MICROGLOBULIN; HUMANS; MUTATION, MISSENSE; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY;

EID: 84886655678     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.498857     Document Type: Article

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