Mutant protein A30P α-synuclein adopts wild-type fibril structure, despite slower fibrillation kinetics

Journal of Biological Chemistry

Volumn 287, Issue 14, 2012, Pages 11526-11532

  Lemkau, Luisel R ^a   Comellas, Gemma ^a   Kloepper, Kathryn D ^a,c   Woods, Wendy S ^b   George, Julia M ^b   Rienstra, Chad M ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c MERCER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AUTOSOMAL DOMINANTS; CLINICAL FEATURES; DOPAMINERGIC NEURONS; FIBRIL STRUCTURE; IN-VITRO; LEWY BODIES; MUTANT PROTEINS; PARKINSON DISEASE; PATHOGENIC MECHANISMS; SECONDARY STRUCTURES; SUBSTANTIA NIGRA; SYNUCLEIN; WILD TYPES;

NEURONS;

CHEMICAL SHIFT;

ALANINE; ALPHA SYNUCLEIN; PROLINE;

ARTICLE; CONTROLLED STUDY; IN VITRO STUDY; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; WILD TYPE;

ALPHA-SYNUCLEIN; HUMANS; KINETICS; MUTANT PROTEINS; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY;

EID: 84859514070     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.306902     Document Type: Article

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