A recurrent D-strand association interface is observed in β-2 microglobulin oligomers

FEBS Journal

Volumn 279, Issue 6, 2012, Pages 1131-1143

  Colombo, Matteo ^a   De Rosa, Matteo ^a   Bellotti, Vittorio ^b,c   Ricagno, Stefano ^a   Bolognesi, Martino ^a,d  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF PAVIA   (Italy)

^c FONDAZIONE IRCCS POLICLINICO SAN MATTEO   (Italy)

^d CNR   (Italy)

Author keywords

2 microglobulin; 2 microglobulin mutants; amyloid fibrils; amyloidogenic oligomers; dialysis related amyloidosis

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; CYSTEINE; DISULFIDE; HOMODIMER; OLIGOMER;

CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DISULFIDE BOND; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DETERMINATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW; STRUCTURE ANALYSIS; WILD TYPE; X RAY ANALYSIS;

AMYLOID; BETA 2-MICROGLOBULIN; CYSTEINE; DISULFIDES; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 84858446912     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08510.x     Document Type: Review

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