The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein

Journal of Biological Chemistry

Volumn 290, Issue 4, 2015, Pages 2395-2404

  Porcari, Riccardo ^a   Proukakis, Christos ^b   Waudby, Christopher A ^a   Bolognesi, Benedetta ^c   Mangione, P Patrizia ^a,d   Paton, Jack F S ^a   Mullin, Stephen ^a   Cabrita, Lisa D ^a   Penco, Amanda ^f   Relini, Annalisa ^f   Verona, Guglielmo ^a,d   Vendruscolo, Michele ^e   Stoppini, Monica ^d   Tartaglia, Gian Gaetano ^c   Camilloni, Carlo ^e   Christodoulou, John ^a   Schapira, Anthony H V ^b   Bellotti, Vittorio ^a,d  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

^c UNIVERSITAT POMPEU FABRA   (Spain)

^d UNIVERSITY OF PAVIA   (Italy)

^e UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^f UNIVERSITY OF GENOA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ANALYSIS; CHEMICAL SHIFT; CHEMICAL STABILITY; GENES; THERMODYNAMIC STABILITY;

AGGREGATE FORMATION; AGGREGATION KINETICS; AGGREGATION PROCESS; AGGREGATION PROPENSITY; DOSE-DEPENDENT MANNER; PATHOGENIC MUTATION; PREDICTION ALGORITHMS; SECONDARY STRUCTURES;

AGGREGATES;

ALPHA SYNUCLEIN; GLUTAMINE; HISTIDINE; ISOPROTEIN; AMYLOID; PEPTIDE; POLYPROLINE; PROTEIN BINDING; RECOMBINANT PROTEIN;

ARTICLE; CONTROLLED STUDY; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SOLUBILITY; THERMODYNAMICS; WILD TYPE; ATOMIC FORCE MICROSCOPY; BINDING SITE; CHEMISTRY; GENETICS; HUMAN; LEWY BODY; METABOLISM; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARKINSON DISEASE; PHENOTYPE;

ALPHA-SYNUCLEIN; AMYLOID; BINDING SITES; HUMANS; LEWY BODIES; MAGNETIC RESONANCE SPECTROSCOPY; MICROSCOPY, ATOMIC FORCE; MUTATION; PARKINSON DISEASE; PEPTIDES; PHENOTYPE; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SOLUBILITY; THERMODYNAMICS;

EID: 84961289040     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.610527     Document Type: Article

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