Salvador Ventura

Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona

Affiliated withUniversitat Autònoma de Barcelona

Research Area

Biochemistry

Biography

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JoVE Journal Publications

ArticleTotal : 1	Year
Publication title	2018

Other Publications

Article	Year
Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proceedings of the National Academy of Sciences of the United States of America\| PubMed ID: 15123800	2004
Designing proteins from the inside out. Proteins\| PubMed ID: 15162481	2004
Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties. Biochemistry\| PubMed ID: 15196042	2004
Role of kinetic intermediates in the folding of leech carboxypeptidase inhibitor. The Journal of biological chemistry\| PubMed ID: 15226306	2004
Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation. Biological chemistry\| PubMed ID: 15255184	2004
Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin. Journal of molecular biology\| PubMed ID: 15313627	2004
Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin. Proceedings of the National Academy of Sciences of the United States of America\| PubMed ID: 15738388	2005
Amyloid-like properties of bacterial inclusion bodies. Journal of molecular biology\| PubMed ID: 15784261	2005
Sequence determinants of protein aggregation: tools to increase protein solubility. Microbial cell factories\| PubMed ID: 15847694	2005
NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor. Structure (London, England : 1993)\| PubMed ID: 16084391	2005
Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond. Journal of molecular biology\| PubMed ID: 16126224	2005
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microbial cell factories\| PubMed ID: 16156893	2005
Prediction of "hot spots" of aggregation in disease-linked polypeptides. BMC structural biology\| PubMed ID: 16197548	2005
Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. The FEBS journal\| PubMed ID: 16420488	2006
Protein quality in bacterial inclusion bodies. Trends in biotechnology\| PubMed ID: 16503059	2006
Folding of small disulfide-rich proteins: clarifying the puzzle. Trends in biochemical sciences\| PubMed ID: 16600598	2006
Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. Journal of biotechnology\| PubMed ID: 16621081	2006
Characterizing the tick carboxypeptidase inhibitor: molecular basis for its two-domain nature. The Journal of biological chemistry\| PubMed ID: 16760476	2006
The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. Microbial cell factories\| PubMed ID: 16893469	2006
Design and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains. Protein science : a publication of the Protein Society\| PubMed ID: 16963647	2006
Effect of temperature on protein quality in bacterial inclusion bodies. FEBS letters\| PubMed ID: 17101131	2006
Ile-phe dipeptide self-assembly: clues to amyloid formation. Biophysical journal\| PubMed ID: 17172307	2007
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC bioinformatics\| PubMed ID: 17324296	2007
Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics\| PubMed ID: 17352427	2007
Self-assembly of human latexin into amyloid-like oligomers. BMC structural biology\| PubMed ID: 17996039	2007
Oxidative folding of leech-derived tryptase inhibitor via native disulfide-bonded intermediates. Antioxidants & redox signaling\| PubMed ID: 18004973	2008
Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry. Nature protocols\| PubMed ID: 18193018	2008
The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case. Journal of molecular biology\| PubMed ID: 18423663	2008
Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid). Acta crystallographica. Section D, Biological crystallography\| PubMed ID: 18566513	2008
Inclusion bodies: specificity in their aggregation process and amyloid-like structure. Biochimica et biophysica acta\| PubMed ID: 18619498	2008
The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways. The Journal of biological chemistry\| PubMed ID: 18640980	2008
Studies on bacterial inclusion bodies. Future microbiology\| PubMed ID: 18651814	2008
Monitoring the interference of protein-protein interactions in vivo by bimolecular fluorescence complementation: the DnaK case. Proteomics\| PubMed ID: 18686297	2008
Kinetic and thermodynamic stability of bacterial intracellular aggregates. FEBS letters\| PubMed ID: 18840434	2008
Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease. Journal of the American Chemical Society\| PubMed ID: 19133767	2009
Detecting and interfering protein interactions: towards the control of biochemical pathways. Current medicinal chemistry\| PubMed ID: 19149583	2009
Protein complementation assays: approaches for the in vivo analysis of protein interactions. FEBS letters\| PubMed ID: 19269288	2009
Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function. Journal of molecular biology\| PubMed ID: 19559710	2009
Amyloids in bacterial inclusion bodies. Trends in biochemical sciences\| PubMed ID: 19647433	2009
Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases. PLoS computational biology\| PubMed ID: 19696882	2009
Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor. The Journal of biological chemistry\| PubMed ID: 19820233	2009
Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion. Microbial cell factories\| PubMed ID: 19863787	2009
Protein aggregation profile of the bacterial cytosol. PloS one\| PubMed ID: 20195530	2010
Protein folding and aggregation in bacteria. Cellular and molecular life sciences : CMLS\| PubMed ID: 20358253	2010
Protease inhibitors as models for the study of oxidative folding. Antioxidants & redox signaling\| PubMed ID: 20812859	2011
The role of protein sequence and amino acid composition in amyloid formation: scrambling and backward reading of IAPP amyloid fibrils. Journal of molecular biology\| PubMed ID: 20887731	2010
Amyloid-like protein inclusions in tobacco transgenic plants. PloS one\| PubMed ID: 21049018	2010
Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria. Proteomics\| PubMed ID: 21086517	2010
Does stoichiometry drive protein folding? Journal of biomolecular structure & dynamics\| PubMed ID: 21142251	2011
Linking amyloid protein aggregation and yeast survival. Molecular bioSystems\| PubMed ID: 21240401	2011
The aggregation properties of Escherichia coli proteins associated with their cellular abundance. Biotechnology journal\| PubMed ID: 21538899	2011
Biological role of bacterial inclusion bodies: a model for amyloid aggregation. The FEBS journal\| PubMed ID: 21569209	2011
Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case. Antioxidants & redox signaling\| PubMed ID: 21797671	2012
Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions. Biomacromolecules\| PubMed ID: 22176525	2012
AGGRESCAN: method, application, and perspectives for drug design. Methods in molecular biology (Clifton, N.J.)\| PubMed ID: 22183539	2012
The effect of amyloidogenic peptides on bacterial aging correlates with their intrinsic aggregation propensity. Journal of molecular biology\| PubMed ID: 22200483	2012
Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide. Biochimie\| PubMed ID: 22542639	2012
Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors. Microbial cell factories\| PubMed ID: 22553999	2012
Native structure protects SUMO proteins from aggregation into amyloid fibrils. Biomacromolecules\| PubMed ID: 22559198	2012
Protein oxidative folding in the intermembrane mitochondrial space: more than protein trafficking. Current protein & peptide science\| PubMed ID: 22612783	2012
Yeast prions form infectious amyloid inclusion bodies in bacteria. Microbial cell factories\| PubMed ID: 22731490	2012
Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation. Molecular bioSystems\| PubMed ID: 22868714	2012
Cross-β-sheet supersecondary structure in amyloid folds: techniques for detection and characterization. Methods in molecular biology (Clifton, N.J.)\| PubMed ID: 22987357	2013
Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone. Biochimica et biophysica acta\| PubMed ID: 23063975	2013
Protein aggregation profile of the human kinome. Frontiers in physiology\| PubMed ID: 23181023	2012
Modeling amyloids in bacteria. Microbial cell factories\| PubMed ID: 23272903	2012
About targets and causes in protein folding. Journal of biomolecular structure & dynamics\| PubMed ID: 23297814	2013
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain. PloS one\| PubMed ID: 23505482	2013
Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains. BMC genomics\| PubMed ID: 23663289	2013
Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation. Biochimica et biophysica acta\| PubMed ID: 23856334	2013
Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy. PloS one\| PubMed ID: 24358189	2013
Selection against toxic aggregation-prone protein sequences in bacteria. Biochimica et biophysica acta\| PubMed ID: 24472658	2014
PrionScan: an online database of predicted prion domains in complete proteomes. BMC genomics\| PubMed ID: 24498877	2014
Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection. Current protein & peptide science\| PubMed ID: 24555899	2014
N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case. Biomacromolecules\| PubMed ID: 24564702	2014
The mitochondrial intermembrane space oxireductase Mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein Cox19. The Journal of biological chemistry\| PubMed ID: 24569988	2014
Association between foldability and aggregation propensity in small disulfide-rich proteins. Antioxidants & redox signaling\| PubMed ID: 24635049	2014
The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses. The Journal of biological chemistry\| PubMed ID: 25086037	2014
The small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity. Human molecular genetics\| PubMed ID: 25092884	2014
Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli. Biotechnology journal\| PubMed ID: 25112199	2014
Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions. The Journal of biological chemistry\| PubMed ID: 25294878	2014
Characterization of amyloid-like properties in bacterial intracellular aggregates. Methods in molecular biology (Clifton, N.J.)\| PubMed ID: 25447861	2015
What makes a protein sequence a prion? PLoS computational biology\| PubMed ID: 25569335	2015
Proteome response at the edge of protein aggregation. Open biology\| PubMed ID: 25673330	2015
AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures. Nucleic acids research\| PubMed ID: 25883144	2015
PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores. Nucleic acids research\| PubMed ID: 25977297	2015
The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria. Microbial cell factories\| PubMed ID: 26160665	2015
Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor. PloS one\| PubMed ID: 26168158	2015
Computational analysis of candidate prion-like proteins in bacteria and their role. Frontiers in microbiology\| PubMed ID: 26528269	2015
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria. Microbial cell factories\| PubMed ID: 26536866	2015
In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time. Biotechnology journal\| PubMed ID: 26580000	2016
A fast and specific method to screen for intracellular amyloid inhibitors using bacterial model systems. European journal of medicinal chemistry\| PubMed ID: 26608003	2016
Curing bacterial infections with protein aggregates. Molecular microbiology\| PubMed ID: 26714186	2016
The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core. Frontiers in microbiology\| PubMed ID: 26779170	2015
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. PLoS genetics\| PubMed ID: 26815787	2016
Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degeneration. FEBS letters\| PubMed ID: 26865059	2016
Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity. Nature communications\| PubMed ID: 26902880	2016
Mammalian prion amyloid formation in bacteria. Prion\| PubMed ID: 26910379	2016
Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation. International journal of molecular sciences\| PubMed ID: 27322259	2016
Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals. PLoS pathogens\| PubMed ID: 27327765	2016
Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria. Data in brief\| PubMed ID: 27408907	2016
Understanding and predicting protein misfolding and aggregation: Insights from proteomics. Proteomics\| PubMed ID: 27479752	2016
Editorial: Protein Solubility and Aggregation in Bacteria. Frontiers in microbiology\| PubMed ID: 27524982	2016
Characterization of Amyloid Cores in Prion Domains. Scientific reports\| PubMed ID: 27686217	2016
Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity. Proceedings of the National Academy of Sciences of the United States of America\| PubMed ID: 27708160	2016
Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure. Scientific reports\| PubMed ID: 27708403	2016
DisProt 7.0: a major update of the database of disordered proteins. Nucleic acids research\| PubMed ID: 27899601	2017
The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation. Acta neuropathologica communications\| PubMed ID: 27938414	2016
DisProt 7.0: a major update of the database of disordered proteins. Nucleic acids research\| PubMed ID: 27965415	2017
Protein misfolding diseases. Future science OA\| PubMed ID: 28031867	2015
Aggregation propensity of neuronal receptors: potential implications in neurodegenerative disorders. Future science OA\| PubMed ID: 28031868	2015
Possible roles of amyloids in malaria pathophysiology. Future science OA\| PubMed ID: 28031872	2015
High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors. International journal of molecular sciences\| PubMed ID: 28257086	2017
Prion-like proteins and their computational identification in proteomes. Expert review of proteomics\| PubMed ID: 28271922	2017
Amyloid cores in prion domains: Key regulators for prion conformational conversion. Prion\| PubMed ID: 28281928	2017
Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics. Communicative & integrative biology\| PubMed ID: 28289488	2017
Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation. Scientific reports\| PubMed ID: 28338000	2017
The Transcription Terminator Rho: A First Bacterial Prion. Trends in microbiology\| PubMed ID: 28392113	2017
Protein aggregation into insoluble deposits protects from oxidative stress. Redox biology\| PubMed ID: 28410533	2017
Perfecting prediction of mutational impact on the aggregation propensity of the ALS-associated hnRNPA2 prion-like protein. FEBS letters\| PubMed ID: 28542905	2017
Advances in the prediction of protein aggregation propensity. Current medicinal chemistry\| PubMed ID: 28685682	2017
Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI). Scientific reports\| PubMed ID: 28710462	2017
Characterization of Soft Amyloid Cores in Human Prion-Like Proteins. Scientific reports\| PubMed ID: 28935930	2017
A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation. Redox biology\| PubMed ID: 29132128	2018
Disulfide driven folding for a conditionally disordered protein. Scientific reports\| PubMed ID: 29208936	2017
Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases. Molecular neurobiology\| PubMed ID: 29429052	2018
AGGRESCAN3D: Toward the Prediction of the Aggregation Propensities of Protein Structures. Methods in molecular biology (Clifton, N.J.)\| PubMed ID: 29594784	2018
The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region. International journal of molecular sciences\| PubMed ID: 29734798	2018
Minimalist Prion-Inspired Polar Self-Assembling Peptides. ACS nano\| PubMed ID: 29812908	2018