Structural Characteristics of α-Synuclein Oligomers

International Review of Cell and Molecular Biology

Volumn 329, Issue , 2017, Pages 79-143

  Cremades, N ^a   Chen, S W ^b   Dobson, C M ^b  

^a UNIVERSITY OF ZARAGOZA   (Spain)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Alpha synuclein; Amyloid aggregation; Fibril; Interconversion of states; Multiplicity; Oligomer; Protein misfolding pathways; Relationships between amyloid species; Structure

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; AMYLOID PROTEIN; DOPAMINE; INTRINSICALLY DISORDERED PROTEIN; METAL ION; OLIGOMER; POLYPEPTIDE; POLYPHENOL DERIVATIVE; PROTEIN AGGREGATE;

AMINO ACID SEQUENCE; ANTIBODY DETECTION; BETA SHEET; CELL LYSATE; CHANNEL GATING; DEGENERATIVE DISEASE; ENERGY TRANSFER; FREEZE DRYING; HUMAN; HYDROGEN BOND; LIPID MEMBRANE; NERVE CELL; NERVE DEGENERATION; NITRATION; NONHUMAN; OXIDATION; PARKINSON DISEASE; POLYMERIZATION; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN HOMEOSTASIS; PROTEIN MISFOLDING; PROTEIN MODIFICATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; CHEMISTRY; DISEASES; MOLECULAR MODEL; PROTEIN MULTIMERIZATION;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; AMYLOID; DISEASE; HUMANS; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION;

EID: 85006049725     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.ircmb.2016.08.010     Document Type: Chapter

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