List of works - Joan Torrent

A Fluorescent Oligothiophene-Bis-Triazine ligand interacts with PrP fibrils and detects SDS-resistant oligomers in human prion diseases.

scientific article published on 26 January 2016

Alternative prion structural changes revealed by high pressure.

scientific article

Amyloid features and neuronal toxicity of mature prion fibrils are highly sensitive to high pressure

scientific article

Asymmetric kinetics of protein structural changes.

scientific article

Distinct unfolding and refolding pathways of ribonuclease a revealed by heating and cooling temperature jumps.

scientific article published on 30 January 2008

Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways.

scientific article

Fungicide Residues Exposure and β-amyloid Aggregation in a Mouse Model of Alzheimer's Disease

scientific article published on 15 January 2020

Getting to the core of prion superstructural variability.

scientific article published on 04 December 2015

Glucocorticoid receptors signaling impairment potentiates amyloid-β oligomers-induced pathology in an acute model of Alzheimer's disease

scientific article published on 29 November 2019

High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation.

scientific article

High pressure modulates amyloid formation.

scientific article

High pressure, a tool to switch between soluble and fibrillar prion protein structures.

scientific article

High-Pressure Response of Amyloid Folds

scientific article published on 28 February 2019

Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.

scientific article

Low doses of bioherbicide favour prion aggregation and propagation in vivo.

scientific article

Machine Learning to Improve the Sensing of Biomolecules by Conical Track-Etched Nanopore

scientific article published on 05 October 2020

Microcebus murinus retina: a new model to assess prion-related neurotoxicity in primates.

scientific article published on 23 April 2010

Modulation of prion protein structure by pressure and temperature.

scientific article

Oligomeric-induced activity by thienyl pyrimidine compounds traps prion infectivity

scientific article

Optimized overproduction, purification, characterization and high-pressure sensitivity of the prion protein in the native (PrP(C)-like) or amyloid (PrP(Sc)-like) conformation.

scientific article

Pressure Reveals Unique Conformational Features in Prion Protein Fibril Diversity

scientific article published on 26 February 2019

Pressure versus temperature unfolding of ribonuclease A: an FTIR spectroscopic characterization of 10 variants at the carboxy-terminal site

scientific article

Pressure- and temperature-induced unfolding studies: thermodynamics of core hydrophobicity and packing of ribonuclease A

scientific article published on 01 March 2006

Pressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease A

scientific article published on 23 June 2006

The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation.

scientific article

The powerful high pressure tool for protein conformational studies

scientific article published on 30 July 2005

The role of the 132-160 region in prion protein conformational transitions.

scientific article

Valine 108, a Chain-Folding Initiation Site-Belonging Residue, Crucial for the Ribonuclease A Stability

scientific article published on 01 November 1999

List of works by Joan Torrent

A Fluorescent Oligothiophene-Bis-Triazine ligand interacts with PrP fibrils and detects SDS-resistant oligomers in human prion diseases.

Alternative prion structural changes revealed by high pressure.

Amyloid features and neuronal toxicity of mature prion fibrils are highly sensitive to high pressure

Asymmetric kinetics of protein structural changes.

Distinct unfolding and refolding pathways of ribonuclease a revealed by heating and cooling temperature jumps.

Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways.

Fungicide Residues Exposure and β-amyloid Aggregation in a Mouse Model of Alzheimer's Disease

Getting to the core of prion superstructural variability.

Glucocorticoid receptors signaling impairment potentiates amyloid-β oligomers-induced pathology in an acute model of Alzheimer's disease

High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation.

High pressure modulates amyloid formation.

High pressure, a tool to switch between soluble and fibrillar prion protein structures.

High-Pressure Response of Amyloid Folds

Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.

Low doses of bioherbicide favour prion aggregation and propagation in vivo.

Machine Learning to Improve the Sensing of Biomolecules by Conical Track-Etched Nanopore

Microcebus murinus retina: a new model to assess prion-related neurotoxicity in primates.

Modulation of prion protein structure by pressure and temperature.

Oligomeric-induced activity by thienyl pyrimidine compounds traps prion infectivity

Optimized overproduction, purification, characterization and high-pressure sensitivity of the prion protein in the native (PrP(C)-like) or amyloid (PrP(Sc)-like) conformation.

Pressure Reveals Unique Conformational Features in Prion Protein Fibril Diversity

Pressure versus temperature unfolding of ribonuclease A: an FTIR spectroscopic characterization of 10 variants at the carboxy-terminal site

Pressure- and temperature-induced unfolding studies: thermodynamics of core hydrophobicity and packing of ribonuclease A

Pressure-jump-induced kinetics reveals a hydration dependent folding/unfolding mechanism of ribonuclease A

The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation.

The powerful high pressure tool for protein conformational studies

The role of the 132-160 region in prion protein conformational transitions.

Valine 108, a Chain-Folding Initiation Site-Belonging Residue, Crucial for the Ribonuclease A Stability