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Publications associées (32)

The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins

Paolo De Los Rios

Proteins undergo both cold and heat denaturation, but often cold denaturation cannot be detected because it occurs at temperatures below water freezing. Proteins undergoing detectable cold as well as heat denaturation yield a reliable curve of protein stab ...

2018

Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins

Paolo De Los Rios, Alessandro Barducci, Pierre Goloubinoff, Bruno Claude Daniel Fauvet, Alberto Stefano Sassi

During and after protein translation, molecular chaperones require ATP hydrolysis to favor the native folding of their substrates and, under stress, to avoid aggregation and revert misfolding. Why do some chaperones need ATP, and what are the consequences ...

2018

Structural and functional analysis of host attachment proteins from contractile injection systems

Michel Plattner

Bacteriophages of the myoviridae family, R-type pyocin, Photorhabus virulence cassette (PVC), Serratia antifeeding prophage (Afp) and type 6 secretion system (T6SS) form a class of contractile injection systems that share common structural and functional c ...

EPFL2018

Quantifying and Localizing the Mitochondrial Proteome Across Five Tissues in A Mouse Population

Johan Auwerx, Jun Yong Kim, Dongryeol Ryu, Evan Graehl Williams, Pooja Jha, Jiayi Lan, Ruedi Aebersold, Moaraj Hasan

We have used SWATH mass spectrometry to quantify 3648 proteins across 76 proteomes collected from genetically diverse BXD mouse strains in two fractions (mitochondria and total cell) from five tissues: liver, quadriceps, heart, brain, and brown adipose (BA ...

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC2018

Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins

Paolo De Los Rios, Alessandro Barducci, Alberto Stefano Sassi, Pierre Goloubinoff, Bruno Claude Daniel Fauvet

Protein homeostasis, namely the ensemble of cellular mechanisms collectively controlling the activity, stability and conformational states of proteins, depends on energy-consuming processes. De novo protein synthesis requires ATP hydrolysis for peptide bon ...

2017

Polyglutamine expansion affects huntingtin conformation in multiple Huntington’s disease models

Hilal Lashuel, Lara Petricca, Sean Michael Deguire

Conformational changes in disease-associated or mutant proteins represent a key pathological aspect of Huntington's disease (HD) and other protein misfolding diseases. Using immunoassays and biophysical approaches, we and others have recently reported that ...

Springer Nature2017

Enhancing Structure Prediction and Design of Soluble and Membrane Proteins with Explicit Solvent-Protein Interactions

Patrick Daniel Barth

Solvent molecules interact intimately with proteins and can profoundly regulate their structure and function. However, accurately and efficiently modeling protein solvation effects at the molecular level has been challenging. Here, we present a method that ...

2017

Screening of structurally diverse bicyclic peptide libraries by phage display

Davide Bertoldo

Bicyclic peptides are an attractive molecule format for the development of therapeutics and research tools. Our laboratory is specialized on the development of bicyclic peptide ligands by phage display. In brief, libraries of randompeptides each containing ...

EPFL2016

Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process

Françoise Gisou van der Goot Grunberg, Matteo Dal Peraro, Mircea Ioan Iacovache, Nuria Cirauqui Diaz

Owing to their pathogenical role and unique ability to exist both as soluble proteins and transmembrane complexes, pore-forming toxins (PFTs) have been a focus of microbiologists and structural biologists for decades. PFTs are generally secreted as water-s ...

Nature Publishing Group2016

Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

Andrija Finka, Pierre Goloubinoff

Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989, groundbreaking experiments demonstrated that a purified chaperone can bind a ...

Annual Reviews2016

Elucidating the Role of Site-Specific Nitration of alpha-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis

Hilal Lashuel, Anass Chiki, Nadine Aït Bouziad, Ritwik Burai

Parkinsons disease (PD) is characterized by the loss of dopaminergic neurons in the substantia nigra and the presence of intraneuronal inclusions consisting of aggregated and post-translationally modified a-synuclein (a-syn). Despite advances in the chemic ...

Amer Chemical Soc2015

Hyperpolarized Water to Study Protein-Ligand Interactions

Geoffrey Bodenhausen, Aurélien Bornet, Sami Jannin, Jonas Milani, Basile Vuichoud, Quentin Chappuis

The affinity between a chosen target protein and small molecules is a key aspect of drug discovery. Screening by popular NMR methods such as Water-LOGSY suffers from low sensitivity and from false positives caused by aggregated or denatured proteins. This ...

2015

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