A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface

Structure

Volumn 18, Issue 5, 2010, Pages 563-570

  Peterson, Francis C ^a   Baden, Elizabeth M ^b   Owen, Barbara A L ^c   Volkman, Brian F ^a   Ramirez Alvarado, Marina ^b  

^a MEDICAL COLLEGE OF WISCONSIN   (United States)

^b MAYO GRADUATE SCHOOL   (United States)

^c MAYO CLINIC   (United States)

Author keywords

PROTEINS

Indexed keywords

DIMER; IMMUNOGLOBULIN LIGHT CHAIN; LIGHT CHAIN AMYLOIDOSIS PROTEIN; MUTANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLIZATION; FIBER; IMMUNOGENICITY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

AMYLOID; AMYLOIDOSIS; HUMANS; MUTATION; PROTEOSTASIS DEFICIENCIES;

EID: 77952604860     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2010.02.012     Document Type: Article

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