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Two Misfolding Routes for the Prion Protein around pH 4.5

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Parkinson disease (PD) is characterized by dopaminergic neurodegeneration and intracellular inclusions of alpha-synuclein amyloid fibers, which are stable and difficult to dissolve. Whether inclusions are neuroprotective or pathological remains controversi ...

American Society for Clinical Investigation2008

On the structural stability of the free and metal-loaded c-terminal domain of the prion protein

Maria Carola Colombo

A misfolded conformer of the cellular prion protein, denoted as scrapie prion protein, is considered responsible for a variety of fatal neurodegenerative diseases. Both, the function of the protein in its native conformation as well as the factors that tri ...

EPFL2006

Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host

Peter Frey, Tristan Bolmont, Paolo Paganetti

Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo. Intracerebral injection of dilute, amyloid-beta (A beta)-containing brain extracts from humans with Alzheim ...

2006

The materials science of protein aggregation

Hilal Lashuel

Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer's, Parkinson's, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig's disease), Huntington's ...

Materials Research Society2005

Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro

Steinunn Baekkeskov Hanahan

While a b-sheet-rich form of the prion protein (PrPSc) causes neurodegeneration, the biological activity of its precursor, the cellular prion protein (PrPC), has been elusive. We have studied the effect of purified recombinant prion protein (recPrP) on rat ...

Wiley-Blackwell2005

Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis

Hilal Lashuel

Electron microscopy (EM) has played a central role in our current understanding of the mechanisms underlying the pathogenesis of several amyloid diseases, including Alzheimer's disease, Parkinson's disease, and prion diseases. In this chapter, we discuss t ...

Humana Press2005

Structure and stability of copper-prion protein

Ursula Röthlisberger, Maria Carola Colombo, Leonardo Guidoni

Recent EPR-measurements on the mouse prion protein (mPrP) have indicated that the structured C-terminal domain is capable of binding Cu(II) with high affinity. The structure of Cu(II) binding sites in PrPc are unravelled by exploiting mixed quantum-classic ...

2004

PrP-deficient mice are resistant to scrapie

Michel Aguet

Prusiner proposed that the infectious agent of scrapie, the prion, is PrPSc, a modified form of the normal host protein PrPC. Prn-p0/0 mice devoid of PrPC showed normal development and behavior. When inoculated with mouse scrapie prions they remained free ...

1994

Susceptibility to Scrapie in Mice Is Dependent on Prpc

Michel Aguet

Mice devoid of functional PrP genes (Prn-p(0/0) mice) showed normal development and behaviour. When inoculated with mouse scrapie prions they remained free of scrapie symptoms for at least 18 months whereas wild-type controls all died within 6 months. No p ...

1994

Mice devoid of PrP are resistant to scrapie

Michel Aguet

S.B. Prusiner proposed that the infectious agent of scraple, the prion, is PrPSc, a modified form of the normal host protein PrPC. Prn-p0/0 mice devoid of PrPC showed normal development and behavior. When inoculated with mouse scrapie prions, they remained ...

1993