Ginsenoside Rb1 inhibits fibrillation and toxicity of alpha-synuclein and disaggregates preformed fibrils

Neurobiology of Disease

Volumn 74, Issue , 2015, Pages 89-101

  Ardah, Mustafa T ^a   Paleologou, Katerina E ^b   Lv, Guohua ^c   Menon, Sindhu A ^a   Abul Khair, Salema B ^a   Lu, Jia Hong ^d   Safieh Garabedian, Bared ^e   Al Hayani, Abdulmonem A ^f   Eliezer, David ^c   Li, Min ^g   El Agnaf, Omar M A ^a,f  

^a UNITED ARAB EMIRATES UNIVERSITY   (United Arab Emirates)

^b DEMOCRITUS UNIVERSITY OF THRACE   (Greece)

^c WEILL CORNELL MEDICAL COLLEGE   (United States)

^d UNIVERSITY OF MACAU   (Macao)

^e Qatar University   (Qatar)

^f King Abdulaziz University   (Saudi Arabia)

^g HONG KONG BAPTIST UNIVERSITY   (Hong Kong)

Author keywords

Aggregation; Amyloid fibrils; Drug discovery; Ginsenosides; Parkinson's disease; Synuclein

Indexed keywords

ALPHA SYNUCLEIN; GINSENOSIDE RB 1; GINSENOSIDE RG 1; GINSENOSIDE RG 3; THROMBIN; AMYLOID; GINSENOSIDE; NEUROPROTECTIVE AGENT; PROTEINASE K; RECOMBINANT PROTEIN; SNCA PROTEIN, HUMAN;

AMYLOIDOSIS; ARTICLE; CELL VIABILITY; CONTROLLED STUDY; CYTOTOXICITY; DRUG STRUCTURE; FLUORESCENCE MICROSCOPY; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; IMMUNOBLOTTING; IMMUNOCYTOCHEMISTRY; IN VITRO STUDY; NEUROBLASTOMA CELL; OLIGOMERIZATION; PARKINSON DISEASE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN AGGREGATION; PROTEIN CLEAVAGE; PROTEIN EXPRESSION; PROTEIN PURIFICATION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SUPERNATANT; TISSUE CULTURE; TRANSMISSION ELECTRON MICROSCOPY; CELL SURVIVAL; CHEMICAL STRUCTURE; COMPARATIVE STUDY; DRUG EFFECTS; ESCHERICHIA COLI; METABOLISM; PHYSIOLOGY; POLYMERIZATION; PROTEIN SECONDARY STRUCTURE; TUMOR CELL LINE;

ALPHA-SYNUCLEIN; AMYLOID; CELL LINE, TUMOR; CELL SURVIVAL; ENDOPEPTIDASE K; ESCHERICHIA COLI; GINSENOSIDES; HUMANS; MOLECULAR STRUCTURE; NEUROPROTECTIVE AGENTS; POLYMERIZATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 84913553701     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2014.11.007     Document Type: Article

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