Structural mechanism of the interaction of Alzheimer disease Aβ fibrils with the non-steroidal anti-inflammatory drug (NSAID) sulindac sulfide

Journal of Biological Chemistry

Volumn 290, Issue 48, 2015, Pages 28737-28745

  Prade, Elke ^a   Bittner, Heiko J ^b   Sarkar, Riddhiman ^a   Del Amo, Juan Miguel Lopez ^c   Althoff Ospelt, Gerhard ^d   Multhaup, Gerd ^e   Hildebrand, Peter W ^b   Reif, Bernd ^a,f  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^c CIC ENERGIGUNE   (Spain)

^d BRUKER BIOSPIN GMBH   (Germany)

^e MCGILL UNIVERSITY   (Canada)

^f INSTITUTE OF EPIDEMIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BINS; GLYCOPROTEINS; HYDROPHOBICITY; MAGIC ANGLE SPINNING; MOLECULES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SPINNING (FIBERS); SULFUR COMPOUNDS;

ACTIVE MOLECULES; ALZHEIMER DISEASE; ARCHITECTURAL CHANGES; FIBRILLAR STRUCTURES; HYDROPHOBIC CAVITIES; NON-STEROIDAL ANTI-INFLAMMATORY DRUGS; PRIMARY BINDING SITES; STRUCTURAL MECHANISMS;

NEURODEGENERATIVE DISEASES;

AMYLOID BETA PROTEIN; SULINDAC SULFIDE; NONSTEROID ANTIINFLAMMATORY AGENT; PROTEIN BINDING; SULINDAC;

ALZHEIMER DISEASE; ARTICLE; BINDING SITE; DRUG PROTEIN BINDING; HYDROPHOBICITY; MOLECULAR DOCKING; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; ANALOGS AND DERIVATIVES; CHEMICAL PHENOMENA; CHEMISTRY; HUMAN; METABOLISM; PROTEIN SECONDARY STRUCTURE;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANTI-INFLAMMATORY AGENTS, NON-STEROIDAL; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SULINDAC;

EID: 84948685052     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.675215     Document Type: Article

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