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Enhancing mitochondrial proteostasis reduces amyloid-beta proteotoxicity

Related publications (39)

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Self-Assembly of ß-Amyloid Peptides in Cells and on Solid Supports

Enrico Condemi

Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease and Huntington's disease share common mechanisms characterized by protein misfolding and aggregation, including formation of plaques or inclusion bodies. The rapid growing number o ...

EPFL2011

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

Giovanni Dietler, Paolo De Los Rios, Jérôme Flakowski, Raffaele Mezzenga

The aggregation of proteins is central to many aspects of daily life, including food processing, blood coagulation, eye cataract formation disease and prion-related neurodegenerative infections[1–5]. However, the physical mechanisms responsible for amyloid ...

Nature Publishing Group2010

Formation of amyloid-beta (A beta)(1-42) amyloid fibrils, a characteristic feature of Alzheimer's disease (AD), was monitored in situ through atomic force microscopy (AFM). Well-structured amyloid fibrils slowly formed in solution within 24 hours for which ...

2010

Fibrillar vs Crystalline Full-Length beta-2-Microglobulin Studied by High-Resolution Solid-State NMR Spectroscopy

David Lyndon Emsley

Elucidating the fine structure of amyloid fibrils as well as understanding their processes of nucleation and growth remains a difficult yet essential challenge, directly linked to our current poor insight into protein misfolding and aggregation diseases. H ...

AMER CHEMICAL SOC2010

Novel Pentameric Thiophene Derivatives for in Vitro and in Vivo Optical Imaging of a Plethora of Protein Aggregates in Cerebral Amyloidoses

Tristan Bolmont

Molecular probes for selective Identification of protein aggregates are important to advance our understanding of the molecular pathogenesis underlying cerebral amyloidoses. Here we report the chemical design of pentameric thiophene derivatives, denoted lu ...

American Chemical Society2009

The heat shock protein Hsp104 has been reported to possess the ability to modulate protein aggregation and toxicity and to "catalyze" the disaggregation and recovery of protein aggregates, including amyloid fibrils, in yeast, Escherichia coli, mammalian ce ...

Elsevier2008

Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation

Hilal Lashuel, David Viertl

The key pathogenic event in the onset of Alzheimer's disease (AD) is the aggregation of beta-amyloid (Abeta) peptides into toxic aggregates. Molecules that interfere with this process might act as therapeutic agents for the treatment of AD. The amino acid ...

Wiley-Blackwell2007

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

We have generated a novel transgenic mouse model on a C57BL/ 6J genetic background that coexpresses KM670/ 671NL mutated amyloid precursor protein and L166P mutated presenilin 1 under the control of a neuron- specific Thy1 promoter element ( APPPS1 mice). ...

Nature Publishing Group2006

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