Publication

Structure and function of the molecular chaperone Hsp104 from yeast

Related publications (63)

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

Hilal Lashuel, Bruno Claude Daniel Fauvet, Loay Awad, Mirva Hejjaoui

It has been more than a century since the first evidence linking the process of amyloid formation to the pathogenesis of Alzheimer's disease. During the last three decades in particular, increasing evidence from various sources (pathology, genetics, cell c ...

Elsevier2012

Enhanced Sampling Molecular Dynamics Identifies PrPSc Structures Harboring a C-Terminal beta-Core

Ursula Röthlisberger, Ivano Tavernelli, Maria Carola Colombo

We perform a replica exchange molecular dynamics simulation corresponding to a 2.8 mu s total time for the extensive enhanced sampling of the conformational space of the C-terminal part (residues 124-226) of the mouse prion protein (PrP); 1.3% of the confo ...

Amer Chemical Soc2012

Activation of the unfolded protein response pathway causes ceramide accumulation in yeast and INS-1E insulinoma cells

Howard Riezman

Sphingolipids are not only important components of membranes but also have functions in protein trafficking and intracellular signaling. The LCB1 gene encodes a subunit of the serine palmitoyltransferase, which is responsible for the first step of sphingol ...

2012

Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate

Paolo De Los Rios, Pierre Goloubinoff

During mild heat-stress, a native thermolabile polypeptide may partially unfold and transiently expose water-avoiding hydrophobic segments that readily tend to associate into a stable misfolded species, rich in intra-molecular non-native beta-sheet structu ...

2011

Characterisation of Living Matter Using Advanced Spectroscopy Techniques

Markus Bonda

In the context of an ageing society neurodegenerative disease have become more and more frequent among humans. Opposing the benefits of a longer life, these diseases have thus triggered research on neurons and how they interact with each other. In vitro as ...

EPFL2011

Investigation of protein aggregation dynamics with a Bloch surface wave sensor

Hans Peter Herzig, Vincent Paeder, Valeria Musi, Sara Santi

We present a study of the dynamics of protein aggregation using a common path heterodyne Bloch surface wave sensing scheme. We demonstrate the ability to detect, during thermal incubation, the early events linked to the aggregation of proteins related to c ...

SPIE2011

Redundancy and specificity of multiple Trigger Factor chaperones in Desulfitobacteria

Christof Holliger, Julien Maillard

The ribosome-bound Trigger Factor (TF) chaperone assists folding of newly synthesized polypeptides and participates in the assembly of macromolecular complexes. In the present study we showed that multiple distinct TF paralogues are present in genomes of D ...

2011

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

Detection of protein aggregation with a Bloch surface wave based sensor

Hans Peter Herzig, Vincent Paeder, Lubos Hvozdara, Valeria Musi, Sylvain Herminjard

We present the innovative application of a Bloch surface wave based sensor to the detection of protein aggregation. In Hen Egg White Lysozyme (HEWL) solutions, aggregates are discriminated from the monomeric forms in a label-free detection scheme. ...

Elsevier2011

Study of the dynamics of protein aggregation with a Bloch Surface Wave sensor

Hans Peter Herzig, Vincent Paeder, Valeria Musi

We present a study of the dynamics of protein aggregation using an interferometric Bloch surface wave sensing scheme. We demonstrate the ability to detect, during thermal incubation, the aggregation of proteins related to conformational diseases. ...

2011

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