Please use this identifier to cite or link to this item:
https://doi.org/10.1039/c6cc00095a
DC Field | Value | |
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dc.title | A highly selective fluorogenic probe for the detection and: In vivo imaging of Cu/Zn superoxide dismutase | |
dc.contributor.author | Zhang, L | |
dc.contributor.author | Er, J.C | |
dc.contributor.author | Jiang, H | |
dc.contributor.author | Li, X | |
dc.contributor.author | Luo, Z | |
dc.contributor.author | Ramezani, T | |
dc.contributor.author | Feng, Y | |
dc.contributor.author | Tang, M.K | |
dc.contributor.author | Chang, Y.-T | |
dc.contributor.author | Vendrell, M | |
dc.date.accessioned | 2020-09-09T06:43:04Z | |
dc.date.available | 2020-09-09T06:43:04Z | |
dc.date.issued | 2016 | |
dc.identifier.citation | Zhang, L, Er, J.C, Jiang, H, Li, X, Luo, Z, Ramezani, T, Feng, Y, Tang, M.K, Chang, Y.-T, Vendrell, M (2016). A highly selective fluorogenic probe for the detection and: In vivo imaging of Cu/Zn superoxide dismutase. Chemical Communications 52 (58) : 9093-9096. ScholarBank@NUS Repository. https://doi.org/10.1039/c6cc00095a | |
dc.identifier.issn | 1359-7345 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/175270 | |
dc.description.abstract | Copper/zinc superoxide dismutase (Cu/Zn SOD) is an essential enzyme that protects tissue from oxidative damage. Herein we report the first fluorogenic probe (SODO) for the detection and in vivo imaging of Cu/Zn SOD. SODO represents a unique chemical probe for translational imaging studies of Cu/Zn SOD in inflammatory disorders. © 2016 The Royal Society of Chemistry. | |
dc.publisher | Royal Society of Chemistry | |
dc.source | Unpaywall 20200831 | |
dc.subject | aniline | |
dc.subject | benzylamine derivative | |
dc.subject | copper zinc superoxide dismutase | |
dc.subject | fluorine | |
dc.subject | triazole | |
dc.subject | copper zinc superoxide dismutase | |
dc.subject | fluorescent dye | |
dc.subject | animal experiment | |
dc.subject | animal model | |
dc.subject | Article | |
dc.subject | cell viability assay | |
dc.subject | chemical structure | |
dc.subject | controlled study | |
dc.subject | cytotoxicity | |
dc.subject | enzyme activity | |
dc.subject | fibroblast | |
dc.subject | fluorescence | |
dc.subject | human | |
dc.subject | hydrogen bond | |
dc.subject | hydrophobicity | |
dc.subject | imaging | |
dc.subject | in vitro study | |
dc.subject | in vivo study | |
dc.subject | inflammation | |
dc.subject | limit of detection | |
dc.subject | macromolecule | |
dc.subject | mechanical torsion | |
dc.subject | nonhuman | |
dc.subject | nucleophilicity | |
dc.subject | quantitative analysis | |
dc.subject | quantum yield | |
dc.subject | reverse transcription polymerase chain reaction | |
dc.subject | substitution reaction | |
dc.subject | synthesis | |
dc.subject | upregulation | |
dc.subject | viscosity | |
dc.subject | zebra fish | |
dc.subject | chemistry | |
dc.subject | metabolism | |
dc.subject | molecular imaging | |
dc.subject | Fluorescent Dyes | |
dc.subject | Molecular Imaging | |
dc.subject | Molecular Structure | |
dc.subject | Superoxide Dismutase-1 | |
dc.type | Article | |
dc.contributor.department | CHEMISTRY | |
dc.description.doi | 10.1039/c6cc00095a | |
dc.description.sourcetitle | Chemical Communications | |
dc.description.volume | 52 | |
dc.description.issue | 58 | |
dc.description.page | 9093-9096 | |
dc.published.state | Published | |
Appears in Collections: | Staff Publications Elements |
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