Capturing a reactive state of amyloid aggregates: Nmr-based characterization of copper-bound alzheimer disease amyloid β-fibrils in a redox cycle

Journal of Biological Chemistry

Volumn 289, Issue 14, 2014, Pages 9998-10010

  Parthasarathy, Sudhakar ^a   Yoo, Brian ^a   McElheny, Dan ^a   Tay, William ^a   Ishii, Yoshitaka ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; GLYCOPROTEINS; METAL IONS; NEURODEGENERATIVE DISEASES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; REDOX REACTIONS; SPECTROSCOPIC ANALYSIS;

ALZHEIMER DISEASE; CHEMICAL SHIFT ANALYSIS; CONTINUOUS PRODUCTION; NEURONAL DAMAGE; PHYSIOLOGICAL CONCENTRATIONS; REACTIVE OXYGEN SPECIES; SOLID STATE NMR; SPECTROSCOPIC METHOD;

COPPER COMPOUNDS;

AMYLOID; AMYLOID BETA PROTEIN[1-40]; CUPRIC ION;

ALZHEIMER DISEASE; AMYLOID PLAQUE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; OXIDATION; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON TRANSPORT;

ALZHEIMER DISEASE; AMYLOID; AMYLOID Β; ASCORBIC ACID; COPPER BINDING; FIBRIL; HYDROGEN PEROXIDE; REACTIVE OXYGEN SPECIES (ROS); REDOX REACTION; SOLID-STATE NMR;

AMYLOID BETA-PEPTIDES; CARBON ISOTOPES; CATALYTIC DOMAIN; COPPER; HUMANS; HYDROGEN PEROXIDE; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS;

EID: 84898059809     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.511345     Document Type: Article

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