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Aggrescan4D: A comprehensive tool for pH‐dependent analysis and engineering of protein aggregation propensity.
- Published in:
- Protein Science: A Publication of the Protein Society, 2024, v. 33, n. 10, p. 1, doi. 10.1002/pro.5180
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- Article
Understanding and predicting protein misfolding and aggregation: Insights from proteomics.
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- Proteomics, 2016, v. 16, n. 19, p. 2570, doi. 10.1002/pmic.201500529
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- Publication type:
- Article
MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation.
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- Communications Biology, 2021, v. 4, n. 1, p. 1, doi. 10.1038/s42003-021-01930-8
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- Article
ZPD-2, a Small Compound That Inhibits α-Synuclein Amyloid Aggregation and Its Seeded Polymerization.
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- Frontiers in Molecular Neuroscience, 2019, v. 12, p. 1, doi. 10.3389/fnmol.2019.00306
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- Publication type:
- Article
In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time.
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- Biotechnology Journal, 2016, v. 11, n. 1, p. 172, doi. 10.1002/biot.201500252
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- Article
Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli.
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- Biotechnology Journal, 2014, v. 9, n. 10, p. 1259, doi. 10.1002/biot.201400291
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- Article
The aggregation properties of Escherichia coli proteins associated with their cellular abundance.
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- Biotechnology Journal, 2011, v. 6, n. 6, p. 752, doi. 10.1002/biot.201100014
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- Article
Prediction of the aggregation propensity of proteins from the primary sequence: Aggregation properties of proteomes.
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- Biotechnology Journal, 2011, v. 6, n. 6, p. 674, doi. 10.1002/biot.201000331
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- Publication type:
- Article
Secundum Regulam: cuidados y asistencia a enfermos y ancianos en las reglas monásticas hispano-visigodas.
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- Dynamis, 2019, v. 39, n. 2, p. 381, doi. 10.30827/dynamis.v39i2.9841
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- Article
PrionScan: an online database of predicted prion domains in complete proteomes.
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- BMC Genomics, 2014, v. 15, n. 1, p. 1, doi. 10.1186/1471-2164-15-102
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- Article
Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains.
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- BMC Genomics, 2013, v. 14, n. 1, p. 1, doi. 10.1186/1471-2164-14-316
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- Publication type:
- Article
A pyrene-inhibitor fluorescent probe with large Stokes shift for the staining of Aβ<sub>1-42</sub>, α-synuclein, and amylin amyloid fibrils as well as amyloid-containing Staphylococcus aureus biofilms.
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- Analytical & Bioanalytical Chemistry, 2019, v. 411, n. 1, p. 251, doi. 10.1007/s00216-018-1433-8
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- Article
Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria.
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- Proteomics, 2010, v. 10, n. 23, p. 4172, doi. 10.1002/pmic.201000260
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- Publication type:
- Article
Monitoring the interference of protein-protein interactions in vivo by bimolecular fluorescence complementation: the DnaK case.
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- Proteomics, 2008, v. 8, n. 17, p. 3433, doi. 10.1002/pmic.200700739
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- Article
Detection of transient protein-protein interactions by bimolecular fluorescence complementation: The Abl-SH3 case.
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- Proteomics, 2007, v. 7, n. 7, p. 1023, doi. 10.1002/pmic.200600966
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- Publication type:
- Article
In-Silico Analysis of pH-Dependent Liquid-Liquid Phase Separation in Intrinsically Disordered Proteins.
- Published in:
- Biomolecules (2218-273X), 2022, v. 12, n. 7, p. N.PAG, doi. 10.3390/biom12070974
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- Publication type:
- Article
DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH.
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- Biomolecules (2218-273X), 2021, v. 11, n. 11, p. 1596, doi. 10.3390/biom11111596
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- Publication type:
- Article
Prion‐like proteins: from computational approaches to proteome‐wide analysis.
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- FEBS Open Bio, 2021, v. 11, n. 9, p. 2400, doi. 10.1002/2211-5463.13213
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- Article
Aggrescan4D: structure-informed analysis of pH-dependent protein aggregation.
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- Nucleic Acids Research, 2024, v. 52, n. W1, p. W170, doi. 10.1093/nar/gkae382
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- Publication type:
- Article
A3D Model Organism Database (A3D-MODB): a database for proteome aggregation predictions in model organisms.
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- Nucleic Acids Research, 2024, v. 52, n. D1, p. D360, doi. 10.1093/nar/gkad942
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- Article
Aggrescan3D (A3D) 2.0: prediction and engineering of protein solubility.
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- Nucleic Acids Research, 2019, v. 47, n. W1, p. W300, doi. 10.1093/nar/gkz321
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- Publication type:
- Article
PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores.
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- Nucleic Acids Research, 2015, v. 43, n. W1, p. W331, doi. 10.1093/nar/gkv490
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- Publication type:
- Article
AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures.
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- Nucleic Acids Research, 2015, v. 43, n. W1, p. W306, doi. 10.1093/nar/gkv359
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- Publication type:
- Article
Modulation of AΒ<sub>42</sub> fibrillogenesis by glycosaminoglycan structure.
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- FASEB Journal, 2010, v. 24, n. 11, p. 4250, doi. 10.1096/fj.09-153551
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- Article
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.
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- Microbial Cell Factories, 2015, v. 14, p. 1, doi. 10.1186/s12934-015-0361-y
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- Publication type:
- Article
The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria.
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- Microbial Cell Factories, 2015, v. 14, n. 1, p. 1, doi. 10.1186/s12934-015-0284-7
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- Publication type:
- Article
Modeling amyloids in bacteria.
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- Microbial Cell Factories, 2012, v. 11, n. 1, p. 166, doi. 10.1186/1475-2859-11-166
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- Article
Yeast prions form infectious amyloid inclusion bodies in bacteria.
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- Microbial Cell Factories, 2012, v. 11, n. 1, p. 89, doi. 10.1186/1475-2859-11-89
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- Publication type:
- Article
Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors.
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- Microbial Cell Factories, 2012, v. 11, n. 1, p. 55, doi. 10.1186/1475-2859-11-55
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- Article
Comparative analysis of E. coli inclusion bodies and thermal protein aggregates.
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- 2006
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- Publication type:
- Abstract
The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.
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- Microbial Cell Factories, 2006, v. 5, p. 26, doi. 10.1186/1475-2859-5-26
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- Article
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins.
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- Microbial Cell Factories, 2005, v. 4, p. 27, doi. 10.1186/1475-2859-4-27
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- Publication type:
- Article
Sequence determinants of protein aggregation: tools to increase protein solubility.
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- Microbial Cell Factories, 2005, v. 4, p. 11, doi. 10.1186/1475-2859-4-11
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- Publication type:
- Article
Tolcapone, a potent aggregation inhibitor for the treatment of familial leptomeningeal amyloidosis.
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- FEBS Journal, 2021, v. 288, n. 1, p. 310, doi. 10.1111/febs.15339
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- Article
Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.
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- PLoS Pathogens, 2016, v. 12, n. 6, p. 1, doi. 10.1371/journal.ppat.1005711
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- Publication type:
- Article
Bacterial Inclusion Bodies of Alzheimer's Disease β-Amyloid Peptides Can Be Employed To Study Native-Like Aggregation Intermediate States.
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- ChemBioChem, 2011, v. 12, n. 3, p. 407, doi. 10.1002/cbic.201000602
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- Article
The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation.
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- Acta Neuropathologica Communications, 2016, v. 4, p. 1, doi. 10.1186/s40478-016-0402-8
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- Publication type:
- Article
Special Issue: "Inflammation, Oxidative Stress and Protein Aggregation; Any Links?".
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- 2020
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- Publication type:
- Editorial
pH-Dependent Aggregation in Intrinsically Disordered Proteins Is Determined by Charge and Lipophilicity.
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- Cells (2073-4409), 2020, v. 9, n. 1, p. 1, doi. 10.3390/cells9010145
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- Publication type:
- Article
Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation.
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- Cells (2073-4409), 2019, v. 8, n. 8, p. 856, doi. 10.3390/cells8080856
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- Article
Editorial: Protein Aggregation and Solubility in Microorganisms (Archaea, Bacteria and Unicellular Eukaryotes): Implications and Applications.
- Published in:
- 2020
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- Publication type:
- Editorial
Cryo-EM structure of hnRNPDL-2 fibrils, a functional amyloid associated with limb-girdle muscular dystrophy D3.
- Published in:
- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-35854-0
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- Publication type:
- Article
Amyloidogenic Regions and Interaction Surfaces Overlap in Globular Proteins Related to Conformational Diseases.
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- PLoS Computational Biology, 2009, v. 5, n. 8, p. 1, doi. 10.1371/journal.pcbi.1000476
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- Publication type:
- Article
Multiple β-sheet molecular dynamics of amyloid formation from two ABl-SH3 domain peptides.
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- Biopolymers, 2012, v. 98, n. 6, p. 557, doi. 10.1002/bip.22161
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- Publication type:
- Article
Aggregation of the neuroblastoma-associated mutant (S120G) of the human nucleoside diphosphate kinase-A/ NM23-H1 into amyloid fibrils.
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- Naunyn-Schmiedeberg's Archives of Pharmacology, 2011, v. 384, n. 4/5, p. 373, doi. 10.1007/s00210-011-0628-8
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- Publication type:
- Article
A3D database: structure-based predictions of protein aggregation for the human proteome.
- Published in:
- Bioinformatics, 2022, v. 38, n. 11, p. 3121, doi. 10.1093/bioinformatics/btac215
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- Publication type:
- Article
SolupHred: a server to predict the pH-dependent aggregation of intrinsically disordered proteins.
- Published in:
- Bioinformatics, 2021, v. 37, n. 11, p. 1602, doi. 10.1093/bioinformatics/btaa909
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- Publication type:
- Article
Aggrescan3D standalone package for structure-based prediction of protein aggregation properties.
- Published in:
- Bioinformatics, 2019, v. 35, n. 19, p. 3834, doi. 10.1093/bioinformatics/btz143
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- Publication type:
- Article
Editorial: Protein Solubility and Aggregation in Bacteria.
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- 2016
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- Publication type:
- Editorial
Curing bacterial infections with protein aggregates.
- Published in:
- Molecular Microbiology, 2016, v. 99, n. 5, p. 827, doi. 10.1111/mmi.13293
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- Article