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Biozol Diagnostica Vertrieb GmbH
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BioMimetic Therapeutics
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FUJIFILM
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Image Search Results
Journal: International Journal of Molecular Sciences
Article Title: Design of Gelatin-Capped Plasmonic-Diatomite Nanoparticles with Enhanced Galunisertib Loading Capacity for Drug Delivery Applications
doi: 10.3390/ijms221910755
Figure Lengend Snippet: Preparation and Characterization of the AuDNP-LY@Gel system. ( a ) Schematic representation of the functionalization procedure. The growth of AuNPs on the surface of the DNP is achieved by dispersing amino-modified DNPs in the HAuCl 4 solution and adding gelatin as a stabilizing agent. NaBH 4 is used as the reducing agent. Then, the small molecule Galunisertib is loaded into the system and the gelatin shell is performed by crosslinking of the polymer matrix. The scheme is not in scale and not intended to represent the full sample composition. ( b ) TEM investigations of the AuDNP (I), AuDNP-LY@Gel 0.125% (II) and AuDNP-LY@Gel 0.5% samples ( c ). Particle size analysis of AuNPs decorating the surface of the DNP fitted by a Gaussian curve. ( d ) Change in the size (black) and surface charge (blue) of the samples AuDNP-LY@Gel according to the different gelatin amounts in the outer shell. The vertical bars are representative of the standard deviation (SD) on a minimum of three independent measurements.
Article Snippet:
Techniques: Modification, Polymer, Particle Size Analysis, Standard Deviation
Journal: Polymers
Article Title: Recent Advancements and Strategies for Overcoming the Blood–Brain Barrier Using Albumin-Based Drug Delivery Systems to Treat Brain Cancer, with a Focus on Glioblastoma
doi: 10.3390/polym15193969
Figure Lengend Snippet: Methods used to overcome the BBB via controlled drug release systems. Nanoparticles based on biopolymers are transported via the cellular adsorption method by electrostatic forces using surface charges ( a ). Administration of small molecules of active substances encapsulated in nanoparticles using transport mediated by membrane proteins ( b ). Transport via endocytosis of natural inorganic nanoparticles into the cell ( c ). Mechanism of the efflux pump that causes drug resistance in the brain ( d ). Nanoparticle transport using surface receptors such as transferrin and LDL targeting receptors ( e ) .
Article Snippet:
Techniques: Adsorption, Membrane
Journal: Polymers
Article Title: Recent Advancements and Strategies for Overcoming the Blood–Brain Barrier Using Albumin-Based Drug Delivery Systems to Treat Brain Cancer, with a Focus on Glioblastoma
doi: 10.3390/polym15193969
Figure Lengend Snippet: Surface modification of albumin nanoparticles.
Article Snippet:
Techniques: Modification, Clinical Proteomics, Adsorption, In Vivo, Molecular Weight, Concentration Assay, Polymer, Conjugation Assay, Immunopeptidomics, Binding Assay, Marker, Inhibition, Ligand Binding Assay, Comparison, Injection, Bioprocessing, Activation Assay, Incubation, Expressing
Journal: Polymers
Article Title: Recent Advancements and Strategies for Overcoming the Blood–Brain Barrier Using Albumin-Based Drug Delivery Systems to Treat Brain Cancer, with a Focus on Glioblastoma
doi: 10.3390/polym15193969
Figure Lengend Snippet: The schematization of the process used to obtain nanoparticles through the electrohydrodynamic jet method .
Article Snippet:
Techniques:
Journal: Polymers
Article Title: Recent Advancements and Strategies for Overcoming the Blood–Brain Barrier Using Albumin-Based Drug Delivery Systems to Treat Brain Cancer, with a Focus on Glioblastoma
doi: 10.3390/polym15193969
Figure Lengend Snippet: Effect of albumin nanoparticles on U87 cells. ( A ) MTT test for nanoparticles with U87 cells for 48 h. ( B ) Cell apoptosis assay at a combined dose (2 μg/mL for each drug) .
Article Snippet:
Techniques: Apoptosis Assay
Journal: Polymers
Article Title: Recent Advancements and Strategies for Overcoming the Blood–Brain Barrier Using Albumin-Based Drug Delivery Systems to Treat Brain Cancer, with a Focus on Glioblastoma
doi: 10.3390/polym15193969
Figure Lengend Snippet: After intravenous administration, in vivo and ex vivo distribution of HSA-BODIPY nanoparticles and SP-HSA-BODIPY NPs. Images were taken 24 h after injection ( A ), and 3D images were taken 24 h after intravenous injection of SP-HSA-BODIPY nanoparticles ( B ). Representative ex vivo images of brains and organs from mice sacrificed at 24 h (C ) .
Article Snippet:
Techniques: In Vivo, Ex Vivo, Injection
Journal: Polymers
Article Title: Recent Advancements and Strategies for Overcoming the Blood–Brain Barrier Using Albumin-Based Drug Delivery Systems to Treat Brain Cancer, with a Focus on Glioblastoma
doi: 10.3390/polym15193969
Figure Lengend Snippet: Functionalized albumin-based nanoparticles that overcome the BBB.
Article Snippet:
Techniques: In Vitro, In Vivo, Drug discovery, Concentration Assay, Emulsion, Incubation, Conjugation Assay, Inhibition, Over Expression, Expressing, Modification, Homogenization, In Vivo Imaging, Ex Vivo, Gene Expression, Encapsulation, Labeling, Injection, Permeability, Zeta Potential Analyzer, In Situ, Disruption, Imaging, Binding Assay
Journal: bioRxiv
Article Title: miR-10b Deficiency Affords Atherosclerosis Resistance
doi: 10.1101/248641
Figure Lengend Snippet: A. Nucleotide sequences of miR-10b and those of its target in 3’ UTR in LTBP1. B. Western blotting for LTBP1 and β-tubulin (TUBB) using various human ECs that showed Type-I phenotypes (HUVEC, HAEC, HCAEC, HMVEC and ESdEC[P6]) and those with Type-II phenotypes (iPS(BJ)EC, iPS(HU)EC, ESdEC[P0] and ESdEC[P1]) as reported previously 1 . C . Type-II ECs that were transfected with an empty vector (CMV-vector (+), mock) or an miR-10b expression vector (CMV-vector (+), miR-10b), and Type-II ECs without transfection (CMV-vector (-)) were subjected to Western blotting for using an anti-LTBP1 body or an anti-β-tubulin (TUBB) antibody. D . Western blotting for LTBP1 and β-tubulin (TUBB) proteins using Type-I ECs that were transfected with a control HIV vector (control) or an miR-10b inhibitor-expressing HIV vector (miR-10bi) together with Western blotting using Type-II ECs without transfection were shown as indicated. E. Proliferation indexes of SMCs that were co-cultured with Type-II ECs in the absence or the presence of increasing concentrations of LY2157299, a TGF-β signaling inhibitor, as indicated. N=3. F and G . SMCs were co-cultured with Type-I or Type-II ECs and the percentages of phosphorylated SMAD2/3-positive cells in were calculated by flow cytometry (F) and nuclear localization of SMAD3 in PKH-26 (red)-stained SMCs was estimated by immunostaining studies with an anti-smad3 antibody (green) along with nuclear counterstaining with DAPI (blue) (G). Full-length blots are presented in Supplementary information. Abbreviations: ESdEC[P6], human ES cell-derived ECs at passage 6; ESdEC[P0], human ES cell-derived ECs at passage 0; ESdEC[P1], human ES cell-derived ECs at passage 1.
Article Snippet: A
Techniques: Western Blot, Transfection, Plasmid Preparation, Expressing, Cell Culture, Flow Cytometry, Staining, Immunostaining, Derivative Assay