In: Neurochemical Research, 2015, vol. 40, no. 12, p. 2639-2646
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In: Cerebral Cortex, 2017, vol. 27, no. 8, p. 4048-4059
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In: Cerebral Cortex, 2017, vol. 27, no. 7, p. 3618-3629
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In: Magnetic Resonance Materials in Physics, Biology and Medicine, 2015, vol. 28, no. 5, p. 485-492
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In: Plos one, 2011, vol. 6, no. 4, p. e18268
Background: Monoclonal antibodies and antibody fragments are powerful biotherapeutics for various debilitating diseases. However, high production costs, functional limitations such as inadequate pharmacokinetics and tissue accessibility are the current principal disadvantages for broadening their use in clinic. Methodology and Principal Findings: We report a novel method for the long-term ...
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In: Plos pathogens, 2018, vol. 14, no. 10, p. e1007335
Antibodies to the prion protein, PrP, represent a promising therapeutic approach against prion diseases but the neurotoxicity of certain anti-PrP antibodies has caused concern. Here we describe scPOM-bi, a bispecific antibody designed to function as a molecular prion tweezer. scPOM-bi combines the complementarity-determining regions of the neurotoxic antibody POM1 and the neuroprotective...
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In: Cognitive, Affective, & Behavioral Neuroscience, 2014, vol. 14, no. 3, p. 996-1008
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In: Acta Neuropathologica, 2014, vol. 127, no. 2, p. 299-301
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In: Neurological Sciences, 2014, vol. 35, p. 215-224
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In: The journal of biological chemistry, 2015, vol. 290, no. 39, p. 23631-23645
Although the accumulation of a misfolded and protease-resistant form of the prion protein (PrP) is a key event in Prion pathogenesis, the cellular factors involved in its folding and quality control are poorly understood. PrP is a glycosylated and disulfide-bonded protein synthesized at the endoplasmic reticulum (ER). The ER foldase ERp57 (also known as Grp58) is highly expressed in the brain...
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