about
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteinsRecombinant pharmaceuticals from microbial cells: a 2015 updateRecombinant protein quality evaluation: proposal for a minimal information standardDisulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditionsNeuroprotection from NMDA excitotoxic lesion by Cu/Zn superoxide dismutase gene delivery to the postnatal rat brain by a modular protein vector.Side effects of chaperone gene co-expression in recombinant protein production.Isolation of cell-free bacterial inclusion bodies.Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies.Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins.Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control.Protein aggregation in recombinant bacteria: biological role of inclusion bodies.Allosteric enzymes as biosensors for molecular diagnosis.Modular protein engineering for non-viral gene therapy.Biological activities of histidine-rich peptides; merging biotechnology and nanomedicine.Complex Particulate Biomaterials as Immunostimulant-Delivery Platforms.Intracellular CXCR4⁺ cell targeting with T22-empowered protein-only nanoparticles.Protein quality in bacterial inclusion bodies.Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview.Converging antigenic structure of a recombinant viral peptide displayed on different frameworks of carrier proteins.Membrane-active peptides for non-viral gene therapy: making the safest easier.Microbial factories for recombinant pharmaceuticalsPeptide-assisted traffic engineering for nonviral gene therapy.Functional inclusion bodies produced in the yeast Pichia pastoris.Peptide-mediated DNA condensation for non-viral gene therapy.Biomedical applications of distally controlled magnetic nanoparticles.Subcutaneous preconditioning increases invasion and metastatic dissemination in mouse colorectal cancer models.Nanostructured bacterial materials for innovative medicines.Biological role of bacterial inclusion bodies: a model for amyloid aggregation.Unconventional microbial systems for the cost-efficient production of high-quality protein therapeutics.Engineering protein self-assembling in protein-based nanomedicines for drug delivery and gene therapy.The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells.Post-production protein stability: trouble beyond the cell factory.Bacterial inclusion body purification.Recombinant protein materials for bioengineering and nanomedicine.BBB-targeting, protein-based nanomedicines for drug and nucleic acid delivery to the CNS.Integrating mechanical and biological control of cell proliferation through bioinspired multieffector materials.Functional protein aggregates: just the tip of the iceberg.Structural and functional features of self-assembling protein nanoparticles produced in endotoxin-free Escherichia coli.Intrinsic functional and architectonic heterogeneity of tumor-targeted protein nanoparticles.A novel bio-functional material based on mammalian cell aggresomes.
P50
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description
hulumtues
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researcher
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ricercatore
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wetenschapper
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հետազոտող
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name
Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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type
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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prefLabel
Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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Antonio Villaverde
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P214
P244
P950
P1053
N-3986-2018
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7005029873
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0000 0000 6021 6189
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n2003129591
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0000-0002-2615-4521
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