Disease-modifying anti-Alzheimer's drugs: Inhibitors of human cholinesterases interfering with β-amyloid aggregation

CNS Neuroscience and Therapeutics

Volumn 20, Issue 7, 2014, Pages 624-632

  Brogi, Simone ^a   Butini, Stefania ^a   Maramai, Samuele ^a   Colombo, Raffaella ^b   Verga, Laura ^c   Lanni, Cristina ^b   De Lorenzi, Ersilia ^b   Lamponi, Stefania ^a   Andreassi, Marco ^a   Bartolini, Manuela ^d   Andrisano, Vincenza ^d   Novellino, Ettore ^a,e   Campiani, Giuseppe ^a   Brindisi, Margherita ^a   Gemma, Sandra ^a  

^a UNIVERSITY OF SIENA   (Italy)

^b UNIVERSITY OF PAVIA   (Italy)

^c FONDAZIONE IRCCS POLICLINICO SAN MATTEO   (Italy)

^d UNIVERSITY OF BOLOGNA   (Italy)

^e UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Alzheimer's disease; Amyloid beta oligomers; Amyloid beta peptides; Cholinesterase inhibitors; Molecular dynamics; Multifunctional ligands

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; CHOLINESTERASE INHIBITOR; OLIGOMER; TACRINE; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

ANIMAL CELL; ARTICLE; CAPILLARY ELECTROPHORESIS; CELL VIABILITY; COMPUTATIONAL FLUID DYNAMICS; COMPUTER MODEL; CONTROLLED STUDY; CYTOTOXICITY; DRUG INHIBITION; DRUG MECHANISM; DRUG POTENCY; FIBER; FIBROBLAST; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; IN VITRO STUDY; LIVER CELL; MOLECULAR BIOLOGY; MOLECULAR DOCKING; MOLECULAR DYNAMICS; NEUROBLASTOMA CELL; NEUROMODULATION; NONHUMAN; OLIGOMERIZATION; PLURIPOTENT STEM CELL; PROTEIN AGGREGATION; TRANSMISSION ELECTRON MICROSCOPY; 3T3 CELL LINE; ALZHEIMER DISEASE; ANIMAL; ANTAGONISTS AND INHIBITORS; CHEMISTRY; ENZYMOLOGY; METABOLISM; MOUSE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; TUMOR CELL LINE;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANIMALS; CELL LINE, TUMOR; CHOLINESTERASE INHIBITORS; HUMANS; MICE; NIH 3T3 CELLS; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84902481986     PISSN: 17555930     EISSN: 17555949     Source Type: Journal    
DOI: 10.1111/cns.12290     Document Type: Article

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