Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular
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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 May, 2004 | Pubmed ID: 15123800
Designing proteins from the inside out.
Proteins Jul, 2004 | Pubmed ID: 15162481
Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties.
Biochemistry Jun, 2004 | Pubmed ID: 15196042
Role of kinetic intermediates in the folding of leech carboxypeptidase inhibitor.
The Journal of biological chemistry Sep, 2004 | Pubmed ID: 15226306
Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation.
Biological chemistry Jun, 2004 | Pubmed ID: 15255184
Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin.
Journal of molecular biology Sep, 2004 | Pubmed ID: 15313627
Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin.
Proceedings of the National Academy of Sciences of the United States of America Mar, 2005 | Pubmed ID: 15738388
Amyloid-like properties of bacterial inclusion bodies.
Journal of molecular biology Apr, 2005 | Pubmed ID: 15784261
Sequence determinants of protein aggregation: tools to increase protein solubility.
Microbial cell factories Apr, 2005 | Pubmed ID: 15847694
NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
Structure (London, England : 1993) Aug, 2005 | Pubmed ID: 16084391
Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond.
Journal of molecular biology Sep, 2005 | Pubmed ID: 16126224
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins.
Microbial cell factories Sep, 2005 | Pubmed ID: 16156893
Prediction of "hot spots" of aggregation in disease-linked polypeptides.
BMC structural biology Sep, 2005 | Pubmed ID: 16197548
Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities.
The FEBS journal Feb, 2006 | Pubmed ID: 16420488
Protein quality in bacterial inclusion bodies.
Trends in biotechnology Apr, 2006 | Pubmed ID: 16503059
Folding of small disulfide-rich proteins: clarifying the puzzle.
Trends in biochemical sciences May, 2006 | Pubmed ID: 16600598
Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates.
Journal of biotechnology Aug, 2006 | Pubmed ID: 16621081
Characterizing the tick carboxypeptidase inhibitor: molecular basis for its two-domain nature.
The Journal of biological chemistry Aug, 2006 | Pubmed ID: 16760476
The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.
Microbial cell factories Aug, 2006 | Pubmed ID: 16893469
Design and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains.
Protein science : a publication of the Protein Society Oct, 2006 | Pubmed ID: 16963647
Effect of temperature on protein quality in bacterial inclusion bodies.
FEBS letters Nov, 2006 | Pubmed ID: 17101131
Ile-phe dipeptide self-assembly: clues to amyloid formation.
Biophysical journal Mar, 2007 | Pubmed ID: 17172307
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.
BMC bioinformatics Feb, 2007 | Pubmed ID: 17324296
Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case.
Proteomics Apr, 2007 | Pubmed ID: 17352427
Self-assembly of human latexin into amyloid-like oligomers.
BMC structural biology Nov, 2007 | Pubmed ID: 17996039
Oxidative folding of leech-derived tryptase inhibitor via native disulfide-bonded intermediates.
Antioxidants & redox signaling Jan, 2008 | Pubmed ID: 18004973
Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry.
Nature protocols , 2008 | Pubmed ID: 18193018
The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case.
Journal of molecular biology May, 2008 | Pubmed ID: 18423663
Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid).
Acta crystallographica. Section D, Biological crystallography Jul, 2008 | Pubmed ID: 18566513
Inclusion bodies: specificity in their aggregation process and amyloid-like structure.
Biochimica et biophysica acta Oct, 2008 | Pubmed ID: 18619498
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 Oct, 2008 | Pubmed ID: 18640980
Studies on bacterial inclusion bodies.
Future microbiology Aug, 2008 | Pubmed ID: 18651814
Monitoring the interference of protein-protein interactions in vivo by bimolecular fluorescence complementation: the DnaK case.
Proteomics Sep, 2008 | Pubmed ID: 18686297
Kinetic and thermodynamic stability of bacterial intracellular aggregates.
FEBS letters Oct, 2008 | Pubmed ID: 18840434
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 Feb, 2009 | Pubmed ID: 19133767
Detecting and interfering protein interactions: towards the control of biochemical pathways.
Current medicinal chemistry , 2009 | Pubmed ID: 19149583
Protein complementation assays: approaches for the in vivo analysis of protein interactions.
FEBS letters Jun, 2009 | Pubmed ID: 19269288
Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function.
Journal of molecular biology Sep, 2009 | Pubmed ID: 19559710
Amyloids in bacterial inclusion bodies.
Trends in biochemical sciences Aug, 2009 | Pubmed ID: 19647433
Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.
PLoS computational biology Aug, 2009 | Pubmed ID: 19696882
Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.
The Journal of biological chemistry Dec, 2009 | Pubmed ID: 19820233
Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion.
Microbial cell factories Oct, 2009 | Pubmed ID: 19863787
Protein aggregation profile of the bacterial cytosol.
PloS one Feb, 2010 | Pubmed ID: 20195530
Protein folding and aggregation in bacteria.
Cellular and molecular life sciences : CMLS Aug, 2010 | Pubmed ID: 20358253
Protease inhibitors as models for the study of oxidative folding.
Antioxidants & redox signaling Jan, 2011 | Pubmed ID: 20812859
The role of protein sequence and amino acid composition in amyloid formation: scrambling and backward reading of IAPP amyloid fibrils.
Journal of molecular biology Nov, 2010 | Pubmed ID: 20887731
Amyloid-like protein inclusions in tobacco transgenic plants.
PloS one Oct, 2010 | Pubmed ID: 21049018
Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria.
Proteomics Dec, 2010 | Pubmed ID: 21086517
Does stoichiometry drive protein folding?
Journal of biomolecular structure & dynamics Feb, 2011 | Pubmed ID: 21142251
Linking amyloid protein aggregation and yeast survival.
Molecular bioSystems Apr, 2011 | Pubmed ID: 21240401
The aggregation properties of Escherichia coli proteins associated with their cellular abundance.
Biotechnology journal Jun, 2011 | Pubmed ID: 21538899
Biological role of bacterial inclusion bodies: a model for amyloid aggregation.
The FEBS journal Jul, 2011 | Pubmed ID: 21569209
Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case.
Antioxidants & redox signaling Jan, 2012 | Pubmed ID: 21797671
Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions.
Biomacromolecules Feb, 2012 | Pubmed ID: 22176525
AGGRESCAN: method, application, and perspectives for drug design.
Methods in molecular biology (Clifton, N.J.) , 2012 | Pubmed ID: 22183539
The effect of amyloidogenic peptides on bacterial aging correlates with their intrinsic aggregation propensity.
Journal of molecular biology Aug, 2012 | Pubmed ID: 22200483
Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide.
Biochimie Aug, 2012 | Pubmed ID: 22542639
Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors.
Microbial cell factories May, 2012 | Pubmed ID: 22553999
Native structure protects SUMO proteins from aggregation into amyloid fibrils.
Biomacromolecules Jun, 2012 | Pubmed ID: 22559198
Protein oxidative folding in the intermembrane mitochondrial space: more than protein trafficking.
Current protein & peptide science May, 2012 | Pubmed ID: 22612783
Yeast prions form infectious amyloid inclusion bodies in bacteria.
Microbial cell factories Jun, 2012 | Pubmed ID: 22731490
Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation.
Molecular bioSystems Nov, 2012 | Pubmed ID: 22868714
Cross-β-sheet supersecondary structure in amyloid folds: techniques for detection and characterization.
Methods in molecular biology (Clifton, N.J.) , 2013 | Pubmed ID: 22987357
Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone.
Biochimica et biophysica acta Jan, 2013 | Pubmed ID: 23063975
Protein aggregation profile of the human kinome.
Frontiers in physiology , 2012 | Pubmed ID: 23181023
Modeling amyloids in bacteria.
Microbial cell factories Dec, 2012 | Pubmed ID: 23272903
About targets and causes in protein folding.
Journal of biomolecular structure & dynamics , 2013 | Pubmed ID: 23297814
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.
PloS one , 2013 | Pubmed ID: 23505482
Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains.
BMC genomics May, 2013 | Pubmed ID: 23663289
Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation.
Biochimica et biophysica acta Dec, 2013 | Pubmed ID: 23856334
Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy.
PloS one , 2013 | Pubmed ID: 24358189
Selection against toxic aggregation-prone protein sequences in bacteria.
Biochimica et biophysica acta May, 2014 | Pubmed ID: 24472658
PrionScan: an online database of predicted prion domains in complete proteomes.
BMC genomics Feb, 2014 | Pubmed ID: 24498877
Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection.
Current protein & peptide science , 2014 | Pubmed ID: 24555899
N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case.
Biomacromolecules Apr, 2014 | Pubmed ID: 24564702
The mitochondrial intermembrane space oxireductase Mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein Cox19.
The Journal of biological chemistry Apr, 2014 | Pubmed ID: 24569988
Association between foldability and aggregation propensity in small disulfide-rich proteins.
Antioxidants & redox signaling Jul, 2014 | Pubmed ID: 24635049
The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses.
The Journal of biological chemistry Oct, 2014 | Pubmed ID: 25086037
The small GTPase Rab11 co-localizes with α-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity.
Human molecular genetics Dec, 2014 | Pubmed ID: 25092884
Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli.
Biotechnology journal Oct, 2014 | Pubmed ID: 25112199
Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions.
The Journal of biological chemistry Dec, 2014 | Pubmed ID: 25294878
Characterization of amyloid-like properties in bacterial intracellular aggregates.
Methods in molecular biology (Clifton, N.J.) , 2015 | Pubmed ID: 25447861
What makes a protein sequence a prion?
PLoS computational biology Jan, 2015 | Pubmed ID: 25569335
Proteome response at the edge of protein aggregation.
Open biology Feb, 2015 | Pubmed ID: 25673330
AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures.
Nucleic acids research Jul, 2015 | Pubmed ID: 25883144
PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores.
Nucleic acids research Jul, 2015 | Pubmed ID: 25977297
The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.
Microbial cell factories Jul, 2015 | Pubmed ID: 26160665
Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor.
PloS one , 2015 | Pubmed ID: 26168158
Computational analysis of candidate prion-like proteins in bacteria and their role.
Frontiers in microbiology , 2015 | Pubmed ID: 26528269
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.
Microbial cell factories Nov, 2015 | Pubmed ID: 26536866
In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time.
Biotechnology journal Jan, 2016 | Pubmed ID: 26580000
A fast and specific method to screen for intracellular amyloid inhibitors using bacterial model systems.
European journal of medicinal chemistry Oct, 2016 | Pubmed ID: 26608003
Curing bacterial infections with protein aggregates.
Molecular microbiology Mar, 2016 | Pubmed ID: 26714186
The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core.
Frontiers in microbiology , 2015 | Pubmed ID: 26779170
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 Jan, 2016 | Pubmed ID: 26815787
Amyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degeneration.
FEBS letters Mar, 2016 | Pubmed ID: 26865059
Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.
Nature communications Feb, 2016 | Pubmed ID: 26902880
Mammalian prion amyloid formation in bacteria.
Prion 03, 2016 | Pubmed ID: 26910379
Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation.
International journal of molecular sciences Jun, 2016 | Pubmed ID: 27322259
Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.
PLoS pathogens Jun, 2016 | Pubmed ID: 27327765
Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria.
Data in brief Jun, 2016 | Pubmed ID: 27408907
Understanding and predicting protein misfolding and aggregation: Insights from proteomics.
Proteomics 10, 2016 | Pubmed ID: 27479752
Editorial: Protein Solubility and Aggregation in Bacteria.
Frontiers in microbiology , 2016 | Pubmed ID: 27524982
Characterization of Amyloid Cores in Prion Domains.
Scientific reports Sep, 2016 | Pubmed ID: 27686217
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 10, 2016 | Pubmed ID: 27708160
Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure.
Scientific reports 10, 2016 | Pubmed ID: 27708403
DisProt 7.0: a major update of the database of disordered proteins.
Nucleic acids research Jan, 2017 | Pubmed ID: 27899601
The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation.
Acta neuropathologica communications 12, 2016 | Pubmed ID: 27938414
DisProt 7.0: a major update of the database of disordered proteins.
Nucleic acids research Jan, 2017 | Pubmed ID: 27965415
Protein misfolding diseases.
Future science OA Sep, 2015 | Pubmed ID: 28031867
Aggregation propensity of neuronal receptors: potential implications in neurodegenerative disorders.
Future science OA Sep, 2015 | Pubmed ID: 28031868
Possible roles of amyloids in malaria pathophysiology.
Future science OA Sep, 2015 | Pubmed ID: 28031872
High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors.
International journal of molecular sciences Mar, 2017 | Pubmed ID: 28257086
Prion-like proteins and their computational identification in proteomes.
Expert review of proteomics 04, 2017 | Pubmed ID: 28271922
Amyloid cores in prion domains: Key regulators for prion conformational conversion.
Prion Jan, 2017 | Pubmed ID: 28281928
Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics.
Communicative & integrative biology , 2017 | Pubmed ID: 28289488
Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation.
Scientific reports Mar, 2017 | Pubmed ID: 28338000
The Transcription Terminator Rho: A First Bacterial Prion.
Trends in microbiology 06, 2017 | Pubmed ID: 28392113
Protein aggregation into insoluble deposits protects from oxidative stress.
Redox biology 08, 2017 | Pubmed ID: 28410533
Perfecting prediction of mutational impact on the aggregation propensity of the ALS-associated hnRNPA2 prion-like protein.
FEBS letters 07, 2017 | Pubmed ID: 28542905
Advances in the prediction of protein aggregation propensity.
Current medicinal chemistry Jul, 2017 | Pubmed ID: 28685682
Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI).
Scientific reports Jul, 2017 | Pubmed ID: 28710462
Characterization of Soft Amyloid Cores in Human Prion-Like Proteins.
Scientific reports Sep, 2017 | Pubmed ID: 28935930
A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation.
Redox biology Apr, 2018 | Pubmed ID: 29132128
Disulfide driven folding for a conditionally disordered protein.
Scientific reports Dec, 2017 | Pubmed ID: 29208936
Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases.
Molecular neurobiology Feb, 2018 | Pubmed ID: 29429052
AGGRESCAN3D: Toward the Prediction of the Aggregation Propensities of Protein Structures.
Methods in molecular biology (Clifton, N.J.) , 2018 | Pubmed ID: 29594784
The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region.
International journal of molecular sciences May, 2018 | Pubmed ID: 29734798
Minimalist Prion-Inspired Polar Self-Assembling Peptides.
ACS nano Jun, 2018 | Pubmed ID: 29812908
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