Nanoprobing of the effect of Cu2+ cations on misfolding, interaction and aggregation of amyloid β peptide

Journal of Neuroimmune Pharmacology

Volumn 8, Issue 1, 2013, Pages 262-273

  Lv, Zhengjian ^a   Condron, Margaret M ^b   Teplow, David B ^b   Lyubchenko, Yuri L ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Alzheimer's disease; Amyloid protein, A 42; Atomic force microscopy imaging; Cu2+ cations; Single molecule force spectroscopy

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; COLLAGEN FIBRIL; CUPROUS ION;

ACIDITY; ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; DIMERIZATION; DRUG DESIGN; NANOPROBE; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN IMMOBILIZATION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; PROTEIN UNFOLDING; PROTON TRANSPORT; STOICHIOMETRY;

ALGORITHMS; ALUMINUM SILICATES; AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; BUFFERS; CATIONS; COPPER; DATA INTERPRETATION, STATISTICAL; HUMANS; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ATOMIC FORCE; MOLECULAR SEQUENCE DATA; NEUROFIBRILLARY TANGLES; PEPTIDE FRAGMENTS; PROTEOSTASIS DEFICIENCIES;

EID: 84874652160     PISSN: 15571890     EISSN: 15571904     Source Type: Journal    
DOI: 10.1007/s11481-012-9416-6     Document Type: Article

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