0000000000431308

AUTHOR

Jeremy C. Simpson

0000-0002-7956-7805

showing 2 related works from this author

Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia.

2004

Cytoglobin is a recently discovered vertebrate globin distantly related to myoglobin, and its function is unknown. Here we present the first detailed analysis of the distribution and expression of cytoglobin. Northern and Western blotting experiments show the presence of cytoglobin mRNA and protein in a broad range of tissues. Quantitative PCR demonstrates an up-regulation of cytoglobin mRNA levels in rat heart and liver under hypoxic conditions (22 and 44 h of 9% oxygen). Immunofluorescence studies with three antibodies directed against different epitopes of the protein consistently show cytoglobin in connective tissue fibroblasts as well as in hepatic stellate cells. Cytoglobin is also pr…

CytoplasmRespiratory SystemFluorescent Antibody TechniqueBiochemistryMiceAntibody SpecificityChlorocebus aethiopsRespiratory functionHypoxiaNeuronsMice Inbred BALB CReverse Transcriptase Polymerase Chain ReactionCytoglobinNuclear ProteinsImmunohistochemistryGlobinsRespiratory proteinTracheamedicine.anatomical_structureLiverConnective TissueNeuroglobinRecombinant Fusion ProteinsGreen Fluorescent ProteinsMolecular Sequence DataConnective tissueBiologyTransfectionAntibodiesBone and BonesmedicineAnimalsHumansGlobinAmino Acid SequenceRNA MessengerMolecular BiologyVero CellsCell NucleusMessenger RNAMyocardiumCytoglobinCell BiologyFibroblastsMolecular biologyPeptide FragmentsRatsOxygenLuminescent ProteinsGene Expression RegulationHepatic stellate cellHeLa CellsThe Journal of biological chemistry
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Spectroscopic study of the loading of cationic porphyrins by carbon nanohorns as high capacity carriers of photoactive molecules to cells

2019

Carbon nanomaterials are attractive candidates for drug delivery due to their high surface area, ease of functionalisation and biocompatibility. This work describes the spectroscopic monitoring of the loading capacity of oxidised carbon nanohorns for two cationic porphyrins. Addition of the COOH functionalised carbon nanohorns to both meso-tetra(4-N-methylpyridyl) free base (H2TMPyP4) and platinum (PtTMPyP4) porphyrin in aqueous solution results in hypochromism of the Soret band and quenching of the porphyrin emission. These changes are used to monitor the non-covalent binding interactions with the nanohorn surface and determine the surface loading. The colloidal stability of the nanohorns …

BiocompatibilityNANOTUBESBiomedical Engineeringchemistry.chemical_element02 engineering and technology010402 general chemistryPhotochemistry01 natural scienceschemistry.chemical_compoundpolycyclic compoundsGeneral Materials ScienceDRUG-DELIVERYPHOTOTHERMAL THERAPYNANOMATERIALSQuenching (fluorescence)Aqueous solutionCationic polymerizationFree baseSettore CHIM/06 - Chimica OrganicaGeneral ChemistryGeneral Medicine021001 nanoscience & nanotechnologyPorphyrin0104 chemical scienceschemistry0210 nano-technologyPlatinumCarbonJournal of Materials Chemistry B
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