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

Related publications (45)

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Antiprion prophylaxis by gene transfer of a soluble prion antagonist

Didier Trono

Prion diseases are untreatable neurodegenerative disorders characterized by accumulation of PrP(Sc), an aggregated isoform of the normal prion protein PrP(C). Here, we delivered the soluble prion antagonist PrP-Fc(2) to the brains of mice by lentiviral gen ...

American Society for Investigative Pathology2008

Bistability explains threshold phenomena in protein aggregation both in vitro and in vivo

Vassily Hatzimanikatis

Neurodegenerative disease can originate from the misfolding and aggregation of proteins, such as Amyloid-beta, SOD1, or Huntingtin. Fortunately, all cells possess protein quality control machinery that sequesters misfolded proteins, either refolding or deg ...

2006

Switch peptides

Incorrect folding of proteins, leading to aggregation and amyloid formation, is associated with a group of degenerative diseases including Alzheimer's disease and late onset diabetes. Amyloid forming proteins are believed to be mainly α-helical in their na ...

EPFL2006

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

Switch-peptides: from conformational studies to Alzheimer's disease

Hilal Lashuel, Richard Alan Mimna, Jacques Dubochet, Sonia Dos Santos, Karine Murat, Lydiane Jeanine Saucède, Marie-Stéphanie Camus, Jérémy Bérard

A review. Studies on designed peptides that exhibit high tendencies for medium-induced conformational transitions have recently attracted much attention because structural changes are considered as mol. key processes in degenerative diseases. The exptl. ac ...

2006

Le concept switch-peptides

Karine Murat

Conformational transitions have found broad interest due to their impact on protein misfolding and self-assembly as key events leading to the development of neurodegenerative diseases. However, investigation of these dynamic events has been limited so far ...

EPFL2006

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

Membrane permeabilization: a common mechanism in protein-misfolding diseases

Hilal Lashuel

Protein aggregation--and, more specifically, amyloid fibril formation--has been implicated as a primary cause of neurodegeneration in Alzheimer's disease, Parkinson's disease, and related disorders, but the mechanism by which this process triggers neuronal ...

2005

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

hA molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization

Hilal Lashuel, Sabrina Susan Vollers

Aberrant protein oligomerization is an important pathogenetic process in vivo. In Alzheimer's disease (AD), the amyloid beta-protein (Abeta) forms neurotoxic oligomers. The predominant in vivo Abeta alloforms, Abeta40 and Abeta42, have distinct oligomeriza ...

American Chemical Society2003