Morin inhibits the early stages of amyloid β-peptide aggregation by altering tertiary and quaternary interactions to produce "off-pathway" structures

Biochemistry

Volumn 51, Issue 30, 2012, Pages 5990-6009

  Lemkul, Justin A ^a   Bevan, David R ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; IN-VITRO; LOW CONCENTRATIONS; MOLAR EXCESS; MOLECULAR DYNAMICS SIMULATIONS; NATURAL PRODUCTS; NEURAL TISSUE; NEURODEGENERATIVE DISORDERS; PEPTIDE AGGREGATION; QUATERNARY INTERACTIONS; QUATERNARY STRUCTURE; SECONDARY STRUCTURES; THERAPEUTIC AGENTS;

GLYCOPROTEINS; MOLECULAR DYNAMICS; MONOMERS; PEPTIDES; TISSUE;

DIMERS;

AMYLOID BETA PROTEIN; DIMER; MONOMER; MORIN;

ARTICLE; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMYLOID BETA-PEPTIDES; ANTIOXIDANTS; FLAVONOIDS; HUMANS; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION;

EID: 84864482811     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300113x     Document Type: Article

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