The interaction between the single hexarepeat unit of chicken prion protein [ChPrP(54–59)] and Cu(II) was investigated by NMR, finding different coordination modes for the trans/trans and cis/trans isomers
Copper(II) complexes of the neurotoxic peptide fragments of human and chicken prion proteins were st...
ABSTRACT: Prion-linked diseases, such as mad cow disease, scrapie, and the human genetic disorder Cr...
While the Cu(II) binding sites of the prion protein have been well studied under Cu-saturation condi...
Prion protein (PrP) misfolding is one of the pivotal issues in understanding the rudiments of neurod...
The prion protein (PrPc) is a copper-binding glycoprotein that can misfold into a beta-sheet-rich an...
Combined potentiometric, calorimetric and spectroscopic methods were used to investigate the Cu2+ bi...
Combined potentiometric, calorimetric and spectroscopic methods were used to investigate the Cu2+ bi...
In this paper, we report the characterization of copper(II) complexes with two prion (PrP) protein p...
Transmissible spongiform encephalopathies (TSEs) in mammals are neurodegenerative diseases caused by...
Recent experimental evidence supports the hypothe-sis that prion proteins (PrPs) are involved in the...
The unique biology of prion proteins (PrPs) allied with the public-health risks posed by prion zoono...
Prions are pathological isoforms of the cellular prion protein that is responsible for transmissible...
Prion proteins (PrPs) from different species have the enormous ability to anchor copper ions. The N-...
Cu(II) binding to the alpha prion protein (alphaPrP) can be both intramolecular and intermolecular. ...
Cu(II) binding to the α prion protein (αPrP) can be both intramolecular and intermolecular. X-ray ab...
Copper(II) complexes of the neurotoxic peptide fragments of human and chicken prion proteins were st...
ABSTRACT: Prion-linked diseases, such as mad cow disease, scrapie, and the human genetic disorder Cr...
While the Cu(II) binding sites of the prion protein have been well studied under Cu-saturation condi...
Prion protein (PrP) misfolding is one of the pivotal issues in understanding the rudiments of neurod...
The prion protein (PrPc) is a copper-binding glycoprotein that can misfold into a beta-sheet-rich an...
Combined potentiometric, calorimetric and spectroscopic methods were used to investigate the Cu2+ bi...
Combined potentiometric, calorimetric and spectroscopic methods were used to investigate the Cu2+ bi...
In this paper, we report the characterization of copper(II) complexes with two prion (PrP) protein p...
Transmissible spongiform encephalopathies (TSEs) in mammals are neurodegenerative diseases caused by...
Recent experimental evidence supports the hypothe-sis that prion proteins (PrPs) are involved in the...
The unique biology of prion proteins (PrPs) allied with the public-health risks posed by prion zoono...
Prions are pathological isoforms of the cellular prion protein that is responsible for transmissible...
Prion proteins (PrPs) from different species have the enormous ability to anchor copper ions. The N-...
Cu(II) binding to the alpha prion protein (alphaPrP) can be both intramolecular and intermolecular. ...
Cu(II) binding to the α prion protein (αPrP) can be both intramolecular and intermolecular. X-ray ab...
Copper(II) complexes of the neurotoxic peptide fragments of human and chicken prion proteins were st...
ABSTRACT: Prion-linked diseases, such as mad cow disease, scrapie, and the human genetic disorder Cr...
While the Cu(II) binding sites of the prion protein have been well studied under Cu-saturation condi...