Salvador Ventura

Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.

Designing proteins from the inside out.

Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties.

Role of kinetic intermediates in the folding of leech carboxypeptidase inhibitor.

Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation.

Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin.

Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin.

Amyloid-like properties of bacterial inclusion bodies.

Sequence determinants of protein aggregation: tools to increase protein solubility.

NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.

Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond.

Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins.

Prediction of "hot spots" of aggregation in disease-linked polypeptides.

Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities.

Protein quality in bacterial inclusion bodies.

Folding of small disulfide-rich proteins: clarifying the puzzle.

Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates.

Characterizing the tick carboxypeptidase inhibitor: molecular basis for its two-domain nature.

The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.

Design and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains.

Effect of temperature on protein quality in bacterial inclusion bodies.

Ile-phe dipeptide self-assembly: clues to amyloid formation.

AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.

Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case.

Self-assembly of human latexin into amyloid-like oligomers.

Oxidative folding of leech-derived tryptase inhibitor via native disulfide-bonded intermediates.

Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry.

The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case.

Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid).

Inclusion bodies: specificity in their aggregation process and amyloid-like structure.

The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways.

Studies on bacterial inclusion bodies.

Monitoring the interference of protein-protein interactions in vivo by bimolecular fluorescence complementation: the DnaK case.

Kinetic and thermodynamic stability of bacterial intracellular aggregates.

Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease.

Detecting and interfering protein interactions: towards the control of biochemical pathways.

Protein complementation assays: approaches for the in vivo analysis of protein interactions.

Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function.

Amyloids in bacterial inclusion bodies.

Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.

Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.

Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion.

Protein aggregation profile of the bacterial cytosol.

Protein folding and aggregation in bacteria.

Protease inhibitors as models for the study of oxidative folding.

The role of protein sequence and amino acid composition in amyloid formation: scrambling and backward reading of IAPP amyloid fibrils.

Amyloid-like protein inclusions in tobacco transgenic plants.

Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria.

Does stoichiometry drive protein folding?

Linking amyloid protein aggregation and yeast survival.

The aggregation properties of Escherichia coli proteins associated with their cellular abundance.

Biological role of bacterial inclusion bodies: a model for amyloid aggregation.

Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case.

Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions.

AGGRESCAN: method, application, and perspectives for drug design.

The effect of amyloidogenic peptides on bacterial aging correlates with their intrinsic aggregation propensity.

Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide.

Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors.

Native structure protects SUMO proteins from aggregation into amyloid fibrils.

Protein oxidative folding in the intermembrane mitochondrial space: more than protein trafficking.

Yeast prions form infectious amyloid inclusion bodies in bacteria.

Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation.

Cross-β-sheet supersecondary structure in amyloid folds: techniques for detection and characterization.

Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone.

Protein aggregation profile of the human kinome.

Modeling amyloids in bacteria.

About targets and causes in protein folding.

The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.

Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains.

Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation.

Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy.

Selection against toxic aggregation-prone protein sequences in bacteria.

PrionScan: an online database of predicted prion domains in complete proteomes.

Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection.

N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case.

The mitochondrial intermembrane space oxireductase Mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein Cox19.

Association between foldability and aggregation propensity in small disulfide-rich proteins.

The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses.

The small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity.

Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli.

Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions.

Characterization of amyloid-like properties in bacterial intracellular aggregates.

What makes a protein sequence a prion?

Proteome response at the edge of protein aggregation.

AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures.

PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores.

The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.

Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor.

Computational analysis of candidate prion-like proteins in bacteria and their role.

Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.

In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time.

A fast and specific method to screen for intracellular amyloid inhibitors using bacterial model systems.

Curing bacterial infections with protein aggregates.

The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core.

Specific Hsp100 Chaperones Determine the Fate of the First Enzyme of the Plastidial Isoprenoid Pathway for Either Refolding or Degradation by the Stromal Clp Protease in Arabidopsis.

Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degeneration.

Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.

Mammalian prion amyloid formation in bacteria.

Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation.

Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.

Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria.

Understanding and predicting protein misfolding and aggregation: Insights from proteomics.

Editorial: Protein Solubility and Aggregation in Bacteria.

Characterization of Amyloid Cores in Prion Domains.

Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity.

Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure.

DisProt 7.0: a major update of the database of disordered proteins.

The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation.

DisProt 7.0: a major update of the database of disordered proteins.

Protein misfolding diseases.

Aggregation propensity of neuronal receptors: potential implications in neurodegenerative disorders.

Possible roles of amyloids in malaria pathophysiology.

High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors.

Prion-like proteins and their computational identification in proteomes.

Amyloid cores in prion domains: Key regulators for prion conformational conversion.

Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics.

Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation.

The Transcription Terminator Rho: A First Bacterial Prion.

Protein aggregation into insoluble deposits protects from oxidative stress.

Perfecting prediction of mutational impact on the aggregation propensity of the ALS-associated hnRNPA2 prion-like protein.

Advances in the prediction of protein aggregation propensity.

Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI).

Characterization of Soft Amyloid Cores in Human Prion-Like Proteins.

A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation.

Disulfide driven folding for a conditionally disordered protein.

Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases.

AGGRESCAN3D: Toward the Prediction of the Aggregation Propensities of Protein Structures.

The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region.

Minimalist Prion-Inspired Polar Self-Assembling Peptides.