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P1‐231: The Kunitz protease inhibitor domain controls homodimerization of the amyloid precursor protein
Author(s) -
Ben Khalifa Naouel,
Renauld Jean-Christophe,
Courtoy Pierre J.,
Tyteca Donatienne,
Collet Jean-François,
Depuydt Matthieu,
Octave Jean-Noël,
Constantinescu Stefan N.,
Kienlen-Campard Pascal
Publication year - 2010
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2010.05.782
Subject(s) - gene isoform , subcellular localization , protease , microbiology and biotechnology , chemistry , serine protease , confocal microscopy , endosome , biochemistry , amino acid , golgi apparatus , green fluorescent protein , protease inhibitor (pharmacology) , amyloid precursor protein , biophysics , intracellular , biology , cell , enzyme , gene , medicine , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load , immunology , disease , pathology , alzheimer's disease
a polypropylene disc were rotated without AWI, amyloid fibril formation was also considerably accelerated, where fine ThT-reactive aggregates were first found attached at the edge of the disc. Conclusions: These results indicate the critical roles of interfaces and agitation for amyloid fibril formation. Furthermore, elimination of AWI may be essential for proper evaluation of the roles of various biological molecules in the amyloid formation studies in vitro.