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Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding

• Gabriela P. Saborio, Bruno Permanne, Claudio Soto
• Nature
• 2001

Prions are the infectious agents responsible for transmissible spongiform encephalopathies. The principal component of prions is the glycoprotein PrPSc, which is a conformationally modified isoform… (More)

Unfolding the role of protein misfolding in neurodegenerative diseases

• Claudio Soto
• Nature Reviews Neuroscience
• 2003

Recent evidence indicates that diverse neurodegenerative diseases might have a common cause and pathological mechanism — the misfolding, aggregation and accumulation of proteins in the brain,… (More)

In Vitro Generation of Infectious Scrapie Prions

• Joaquín Castilla, Paula Saá, Claudio Hetz, Claudio Soto
• Cell
• 2005

Prions are unconventional infectious agents responsible for transmissible spongiform encephalopathy (TSE) diseases. They are thought to be composed exclusively of the protease-resistant prion protein… (More)

Acetylcholinesterase Accelerates Assembly of Amyloid-β-Peptides into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme

• Nibaldo C Inestrosa, Alejandra Moreno Álvarez, +6 authors Jorge Garrido
• Neuron
• 1996

Acetylcholinesterase (AChE), an important component of cholinergic synapses, colocalizes with amyloid-beta peptide (A beta) deposits of Alzheimer's brain. We report here that bovine brain AChE, as… (More)

Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein.

• Claudio Hetz, Milene Russelakis-Carneiro, Kinsey Maundrell, Joaquín Castilla, Claudio Soto
• The EMBO journal
• 2003

Prion diseases are characterized by accumulation of misfolded prion protein (PrP(Sc)), and neuronal death by apoptosis. Here we show that nanomolar concentrations of purified PrP(Sc) from mouse… (More)

Production of cattle lacking prion protein

• Juergen A. Richt, Poothappillai Kasinathan, +12 authors Yoshimi Kuroiwa
• Nature Biotechnology
• 2007

Prion diseases are caused by propagation of misfolded forms of the normal cellular prion protein PrPC, such as PrPBSE in bovine spongiform encephalopathy (BSE) in cattle and PrPCJD in… (More)

An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease

• Shirley ShiDu Yan, Jiamei Fu, +11 authors David Stern
• Nature
• 1997

Amyloid-β is a neurotoxic peptide which is implicated in the pathogenesis of Alzheimer's disease. It binds an intracellular polypeptide known as ERAB, thought to be a hydroxysteroid dehydrogenase… (More)

β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy

• Claudio Soto, Einar M. Sigurdsson, Laura Maria Morelli, R. Asok Kumar, Eduardo Miguel Castaño, Blas Frangione
• Nature Medicine
• 1998

Inhibition of cerebral amyloid β-protein deposition seems to be an important target for Alzheimer's disease therapy. Amyloidogenesis could be inhibited by short synthetic peptides designed as β-sheet… (More)

Converting a peptide into a drug: strategies to improve stability and bioavailability.

• Céline Adessi, Claudio Soto
• Current medicinal chemistry
• 2002

The discovery of peptide hormones, growth factors and neuropeptides implicated in vital biological functions of our organism has increased interest in therapeutic use of short peptides. However, the… (More)

Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification.

• Paula Saá, Joaquín Castilla, Claudio Soto
• The Journal of biological chemistry
• 2006

Prions are the unconventional infectious agents responsible for transmissible spongiform encephalopathies, which appear to be composed mainly or exclusively of the misfolded prion protein (PrPSc).… (More)

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