Cystatin C reduces the in vitro formation of soluble Aβ1-42 oligomers and protofibrils

Scandinavian Journal of Clinical and Laboratory Investigation

Volumn 67, Issue 2, 2007, Pages 179-190

  Selenica, M L ^a   Wang, X ^b   Ostergaard Pedersen, L ^a   Westlind Danielsson, A ^a   Grubb, A ^b  

^a H LUNDBECK A S   (Denmark)

^b LUND UNIVERSITY HOSPITAL   (Sweden)

Author keywords

ADDLs; Alzheimer's disease; Beta amyloid protein; Cysteine protease inhibitor

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; CYSTATIN C; OLIGOMER;

ARTICLE; BINDING AFFINITY; ELECTRON MICROSCOPY; GEL CHROMATOGRAPHY; IMMUNOBLOTTING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SPECTROFLUOROMETRY;

AMYLOID BETA-PROTEIN; ANIMALS; CHROMATOGRAPHY, GEL; CYSTATINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; IMMUNOBLOTTING; MICROSCOPY, ELECTRON, TRANSMISSION; PEPTIDE FRAGMENTS; PROTEASE INHIBITORS; PROTEIN BINDING; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THIAZOLES;

EID: 33947133671     PISSN: 00365513     EISSN: 15027686     Source Type: Journal    
DOI: 10.1080/00365510601009738     Document Type: Article

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