DE loop mutations affect β2-microglobulin stability and amyloid aggregation

Biochemical and Biophysical Research Communications

Volumn 377, Issue 1, 2008, Pages 146-150

  Ricagno, Stefano ^a   Colombo, Matteo ^a   Rosa, Matteo de ^a   Sangiovanni, Enrico ^a   Giorgetti, Sofia ^b,c   Raimondi, Sara ^b,c   Bellotti, Vittorio ^b,c   Bolognesi, Martino ^a  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF PAVIA   (Italy)

^c FONDAZIONE IRCCS POLICLINICO SAN MATTEO   (Italy)

Author keywords

2 Microglobulin; Amyloid fibrils; Dialysis related amyloidosis; Protein thermal stability; Protein X ray structure

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; AMYLOID; BETA 2-MICROGLOBULIN; HISTOCOMPATIBILITY ANTIGENS CLASS I; HUMANS; MUTATION; PROTEIN STRUCTURE, SECONDARY; X-RAY DIFFRACTION;

EID: 54449101429     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.09.108     Document Type: Article

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