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Manganese Binding to the Prion Protein*
There is considerable evidence that the prion protein binds copper. However, there have also been suggestions that prion protein (PrP) binds manganese. We used isothermal titration calorimetry toExpand
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Stress at the intestinal surface: catecholamines and mucosa–bacteria interactions
Psychological stress has profound effects on gastrointestinal function, and investigations over the past few decades have examined the mechanisms by which neural and hormonal stress mediators act toExpand
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Localization of CB1-cannabinoid receptor immunoreactivity in the porcine enteric nervous system
Abstract. Cannabis has been used for centuries in the medicinal treatment of gastrointestinal disorders. Endogenous cannabinimimetic substances such as 2-arachidonylglycerol have been isolated fromExpand
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Prion protein does not redox-silence Cu2+, but is a sacrificial quencher of hydroxyl radicals.
Oxidative stress is believed to play a central role in the pathogenesis of prion diseases, a group of fatal neurodegenerative disorders associated with a conformational change in the prion proteinExpand
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Preferential Cu2+ Coordination by His96 and His111 Induces β-Sheet Formation in the Unstructured Amyloidogenic Region of the Prion Protein*
The prion protein (PrP) is a Cu2+ binding cell surface glycoprotein that can misfold into a β-sheet-rich conformation to cause prion diseases. The majority of copper binding studies have concentratedExpand
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High Affinity Binding between Copper and Full-length Prion Protein Identified by Two Different Techniques*
The cellular prion protein is known to be a copper-binding protein. Despite the wide range of studies on the copper binding of PrP, there have been no studies to determine the affinity of the proteinExpand
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Neuromodulation of enteropathogen internalization in Peyer's patches from porcine jejunum
Jejunal Peyer's patches (JPP) are innervated sites of immune induction and enteropathogen infection. We investigated the role of enteric nerves in modulating pathogen entry into porcine JPP.Expand
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Prion protein fate governed by metal binding.
The conversion of the normal cellular prion protein to an abnormal isoform is considered to be causal to the prion diseases or transmissible spongiform encephalopathies. The prion protein is a copperExpand
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Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner.
Prion diseases are associated with the conversion of the normal prion protein, PrP(C), to the infectious disease form PrP(Sc). Discrimination between these isoforms would significantly enhanceExpand
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High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation
We show that human stefin B, a protease inhibitor from the family of cystatins, is a copper binding protein, unlike stefin A. We have used isothermal titration calorimetry to directly monitor theExpand
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