%0 Journal Article
%T NPT088 reduces both amyloid-¦Â and tau pathologies in transgenic mice
%A Beka Solomon
%A Charlotte H.-Y. Chung
%A Elliott J. Mufson
%A Eva Asp
%A Haim Tsubery
%A Hemraj B. Dodiya
%A Jason Wright
%A Jenna C. Carroll
%A Kimberley S. Gannon
%A Ming Proschitsky
%A Muhammad Nadeem
%A Rajaraman Krishnan
%A Richard Fisher
%A Sally Schroeter
%A Shadiyat Shoaga
%A Sharon Gilead
%A Valerie Cullen
%J Archive of "Alzheimer's & Dementia : Translational Research & Clinical Interventions".
%D 2016
%R 10.1016/j.trci.2016.06.004
%X Alzheimer's disease (AD) is characterized by appearance of both extracellular senile plaques and intracellular neurofibrillary tangles, comprised of aggregates of misfolded amyloid-¦Â (A¦Â) and hyper-phosphorylated tau, respectively. In a previous study, we demonstrated that g3p, a capsid protein from bacteriophage M13, binds to and remodels misfolded aggregates of proteins that assume an amyloid conformation. We engineered a fusion protein (¡°NPT088¡±) consisting of the active fragment of g3p and human-IgG1-Fc
%K GAIM
%K General amyloid interaction motif
%K Novel object recognition
%K Spontaneous alternation
%K Limb clasping
%K Thioflavin S
%K Brain weight
%K Cerebrospinal fluid
%K Phospho-tau
%U https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5651359/