about
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteinsLactic acid bacteria: reviewing the potential of a promising delivery live vector for biomedical purposesDisulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditionsSide effects of chaperone gene co-expression in recombinant protein production.Isolation of cell-free bacterial inclusion bodies.Inclusion bodies: a new conceptCo-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control.Complex Particulate Biomaterials as Immunostimulant-Delivery Platforms.Functional inclusion bodies produced in the yeast Pichia pastoris.Trends in recombinant protein use in animal production.Biological role of bacterial inclusion bodies: a model for amyloid aggregation.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.Recombinant protein materials for bioengineering and nanomedicine.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.Divergent genetic control of protein solubility and conformational quality in Escherichia coli.Localization of functional polypeptides in bacterial inclusion bodies.A nanostructured bacterial bioscaffold for the sustained bottom-up delivery of protein drugs.Functional inclusion bodies produced in bacteria as naturally occurring nanopills for advanced cell therapies.Bioadhesiveness and efficient mechanotransduction stimuli synergistically provided by bacterial inclusion bodies as scaffolds for tissue engineering.CXCR4(+)-targeted protein nanoparticles produced in the food-grade bacterium Lactococcus lactis.The nanoscale properties of bacterial inclusion bodies and their effect on mammalian cell proliferation.Cellular uptake and intracellular fate of protein releasing bacterial amyloids in mammalian cells.Bottom-Up Instructive Quality Control in the Biofabrication of Smart Protein Materials.Nanostructured recombinant cytokines: A highly stable alternative to short-lived prophylactics.The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.Learning about protein solubility from bacterial inclusion bodies.Sheltering DNA in self-organizing, protein-only nano-shells as artificial viruses for gene delivery.Improved performance of protein-based recombinant gene therapy vehicles by tuning downstream procedures.Lactic Acid Bacteria: a promising alternative for recombinant protein production.Packaging protein drugs as bacterial inclusion bodies for therapeutic applicationsImproving protein delivery of fibroblast growth factor-2 from bacterial inclusion bodies used as cell culture substrates.Functionalization of 3D scaffolds with protein-releasing biomaterials for intracellular delivery.Two-dimensional microscale engineering of protein-based nanoparticles for cell guidance.Expanding the recombinant protein quality in Lactococcus lactis.In situ protein folding and activation in bacterial inclusion bodies.Nanoparticulate architecture of protein-based artificial viruses is supported by protein-DNA interactions.Functional protein-based nanomaterial produced in microorganisms recognized as safe: A new platform for biotechnology.
P50
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P50
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Elena García-Fruitós
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Elena García-Fruitós
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Elena García-Fruitós
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Elena García-Fruitós
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Elena García-Fruitós
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Elena García-Fruitós
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Elena García-Fruitós
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Elena García-Fruitós
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Elena García-Fruitós
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Elena García-Fruitós
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