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GAIM fusions are therapeutic candidates for peripheral amyloidosis.
Amyloid
January 2020
a Proclara Biosciences , Cambridge , MA , USA.
The M13 tip protein, g3p, binds the C-terminal domain of the bacterial membrane protein TolA via β-sheet augmentation, facilitating viral entry into Escherichia coli. G3p binding leads to rearrangement of the β strands and partial unfolding of TolA. G3p also binds multiple amyloid assemblies with high affinity, and it can remodel them into amorphous aggregates.
View Article and Find Full Text PDFConformation as the Therapeutic Target for Neurodegenerative Diseases.
Curr Alzheimer Res
October 2017
Proclara Biosciences, 222 Third Street, Cambridge, MA 02142, United States.
Therapeutic strategies that target pathways of protein misfolding and the toxicity of intermediates along these pathways are mainly at discovery and early development stages, with the exception of monoclonal antibodies that have mainly failed to produce convincing clinical benefits in late stage trials. The clinical failures represent potentially critical lessons for future neurodegenerative disease drug development. More effective drugs may be achieved by pursuing the following two strategies.
View Article and Find Full Text PDFNPT088 reduces both amyloid-β and tau pathologies in transgenic mice.
Alzheimers Dement (N Y)
September 2016
NeuroPhage Pharmaceuticals, Inc., Cambridge, MA, USA.
Introduction: Alzheimer's disease (AD) is characterized by appearance of both extracellular senile plaques and intracellular neurofibrillary tangles, comprised of aggregates of misfolded amyloid-β (Aβ) 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-IgG-Fc.
View Article and Find Full Text PDFA bacteriophage capsid protein provides a general amyloid interaction motif (GAIM) that binds and remodels misfolded protein assemblies.
J Mol Biol
June 2014
Neurophage Pharmaceuticals, 222 Third Street, Suite 3120, Cambridge, MA 02142, USA. Electronic address:
Misfolded protein aggregates, characterized by a canonical amyloid fold, play a central role in the pathobiology of neurodegenerative diseases. Agents that bind and sequester neurotoxic intermediates of amyloid assembly, inhibit the assembly or promote the destabilization of such protein aggregates are in clinical testing. Here, we show that the gene 3 protein (g3p) of filamentous bacteriophage mediates potent generic binding to the amyloid fold.
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