Search Results - "Altmeppen, Hermann C"
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Diverse functions of the prion protein – Does proteolytic processing hold the key?
Published in Biochimica et biophysica acta. Molecular cell research (01-11-2017)“…Proteolytic processing of the cellular and disease-associated form of the prion protein leads to generation of bioactive soluble prion protein fragments and…”
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GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice
Published in PLoS pathogens (01-01-2019)“…The cellular prion protein (PrPC) is a cell surface glycoprotein attached to the membrane by a glycosylphosphatidylinositol (GPI)-anchor and plays a critical…”
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Prion protein alters viral control and enhances pathology after perinatal cytomegalovirus infection
Published in Nature communications (05-09-2024)“…Cytomegalovirus (CMV) infection poses risks to newborns, necessitating effective therapies. Given that the damage includes both viral infection of brain cells…”
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Characterization of brain-derived extracellular vesicles reveals changes in cellular origin after stroke and enrichment of the prion protein with a potential role in cellular uptake
Published in Journal of extracellular vesicles (01-01-2020)“…Extracellular vesicles (EVs) are important means of intercellular communication and a potent tool for regenerative therapy. In ischaemic stroke, transient…”
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Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein
Published in Molecular neurodegeneration (06-04-2018)“…Keywords: ADAM10, Antibody, Exosomes, Glycosylation, Membrane anchor, Neurodegeneration, Prion protein, Proteolytic cleavage, Shedding…”
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The sheddase ADAM10 is a potent modulator of prion disease
Published in eLife (05-02-2015)“…The prion protein (PrP(C)) is highly expressed in the nervous system and critically involved in prion diseases where it misfolds into pathogenic PrP(Sc)…”
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α-Synuclein conformers reveal link to clinical heterogeneity of α-synucleinopathies
Published in Translational neurodegeneration (14-03-2023)“…α-Synucleinopathies, such as Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy, are a class of neurodegenerative diseases…”
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Inducing prion protein shedding as a neuroprotective and regenerative approach in pathological conditions of the brain: from theory to facts
Published in Neural regeneration research (01-09-2023)“…In the last decades, the role of the prion protein (PrP) in neurodegenerative diseases has been intensively investigated, initially in prion diseases of humans…”
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Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice
Published in Scientific reports (27-04-2016)“…Misfolding of proteins in the biosynthetic pathway in neurons may cause disturbed protein homeostasis and neurodegeneration. The prion protein (PrP C ) is a…”
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Lack of a-disintegrin-and-metalloproteinase ADAM10 leads to intracellular accumulation and loss of shedding of the cellular prion protein in vivo
Published in Molecular neurodegeneration (27-05-2011)“…The cellular prion protein (PrPC) fulfils several yet not completely understood physiological functions. Apart from these functions, it has the ability to…”
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Misfolding leads the way to unraveling signaling pathways in the pathophysiology of prion diseases
Published in Prion (01-11-2016)“…A misfolded version of the prion protein represents an essential component in the pathophysiology of fatal neurodegenerative prion diseases, which affect…”
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N-Glycans and Glycosylphosphatidylinositol-Anchor Act on Polarized Sorting of Mouse PrPC in Madin-Darby Canine Kidney Cells
Published in PloS one (08-09-2011)“…The cellular prion protein (PrPC) plays a fundamental role in prion disease. PrPC is a glycosylphosphatidylinositol (GPI)-anchored protein with two variably…”
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N-glycans and glycosylphosphatidylinositol-anchor act on polarized sorting of mouse PrP(C) in Madin-Darby canine kidney cells
Published in PloS one (2011)“…The cellular prion protein (PrP(C)) plays a fundamental role in prion disease. PrP(C) is a glycosylphosphatidylinositol (GPI)-anchored protein with two…”
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The SARS-CoV-2 main protease M pro causes microvascular brain pathology by cleaving NEMO in brain endothelial cells
Published in Nature neuroscience (01-11-2021)“…Coronavirus disease 2019 (COVID-19) can damage cerebral small vessels and cause neurological symptoms. Here we describe structural changes in cerebral small…”
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The prion protein and its ligands: Insights into structure-function relationships
Published in Biochimica et biophysica acta. Molecular cell research (01-06-2022)“…The prion protein is a multifunctional protein that exists in at least two different folding states. It is subject to diverse proteolytic processing steps that…”
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Muskelin Coordinates PrPC Lysosome versus Exosome Targeting and Impacts Prion Disease Progression
Published in Neuron (Cambridge, Mass.) (19-09-2018)“…Cellular prion protein (PrPC) modulates cell adhesion and signaling in the brain. Conversion to its infectious isoform causes neurodegeneration, including…”
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Cystatin C loaded in brain-derived extracellular vesicles rescues synapses after ischemic insult in vitro and in vivo
Published in Cellular and molecular life sciences : CMLS (01-12-2024)“…Synaptic loss is an early event in the penumbra area after an ischemic stroke. Promoting synaptic preservation in this area would likely improve functional…”
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Influence of Methanol on Prion Reduction during High Temperature and High Pressure Oleochemical Processes
Published in European journal of lipid science and technology (01-09-2020)“…Prion‐reduction in standard biodiesel processes is caused by acidic and alkaline conditions. In the alternative RepCat biodiesel process, efficient…”
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Roles of endoproteolytic α‐cleavage and shedding of the prion protein in neurodegeneration
Published in The FEBS journal (01-09-2013)“…The cellular prion protein (PrPC) plays important roles in neurodegenerative diseases. First, it is the well‐established substrate for the conformational…”
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Shortening heparan sulfate chains prolongs survival and reduces parenchymal plaques in prion disease caused by mobile, ADAM10-cleaved prions
Published in Acta neuropathologica (01-03-2020)“…Cofactors are essential for driving recombinant prion protein into pathogenic conformers. Polyanions promote prion aggregation in vitro, yet the cofactors that…”
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