In: Neurochemical Research, 2015, vol. 40, no. 12, p. 2639-2646
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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: 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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In: npj Aging and Mechanisms of Disease, 2017, vol. 3, no. 1, p. 5
Mechanisms that ensure and maintain the stability of genetic information are fundamentally important for organismal function and can have a large impact on disease, aging, and life span. While a multi-layered cellular apparatus exists to detect and respond to DNA damage, various insults from environmental and endogenous sources continuously affect DNA integrity. Over time this can lead to the...
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In: European Journal of Plastic Surgery, 2013, vol. 36, no. 12, p. 777-782
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In: Journal of Biomolecular NMR, 1998, vol. 12, no. 2, p. 345-348
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In: Journal of Biomolecular NMR, 2006, vol. 34, no. 2, p. 75-87
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In: Journal of Biomolecular NMR, 2011, vol. 49, no. 1, p. 1-2
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In: Journal of Biomolecular NMR, 2008, vol. 42, no. 1, p. 23-33
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In: BIOspektrum, 2013, vol. 19, no. 5, p. 492-495
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