The parkinson's disease-associated H50Q mutation accelerates α-synuclein aggregation in vitro

Biochemistry

Volumn 52, Issue 40, 2013, Pages 6925-6927

  Ghosh, Dhiman ^a   Mondal, Mrityunjoy ^a   Mohite, Ganesh M ^a   Singh, Pradeep K ^a   Ranjan, Priyatosh ^a   Anoop, A ^a   Ghosh, Saikat ^a   Jha, Narendra Nath ^a   Kumar, Ashutosh ^a   Maji, Samir K ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION MECHANISM; AMYLOID FORMATION; CHROMATOGRAPHIC TECHNIQUES; MISSENSE MUTANTS; PARKINSON'S DISEASE; SECONDARY STRUCTURES; TWO-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE; WILD TYPES;

CIRCULAR DICHROISM SPECTROSCOPY; OLIGOMERS;

NEURODEGENERATIVE DISEASES;

ALPHA SYNUCLEIN; AMYLOID;

ARTICLE; CIRCULAR DICHROISM; IN VITRO STUDY; MISSENSE MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PARKINSON DISEASE; PHENOTYPE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN POLYMERIZATION; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ALPHA-SYNUCLEIN; AMYLOID; HUMANS; MUTATION, MISSENSE; PARKINSON DISEASE; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY;

EID: 84885439148     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400999d     Document Type: Article

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