PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27956150-4 2017 Glucose oxidase (GOx) was immobilized on the PVA-Fe3O4 nanocomposite via physical adsorption. ferryl iron 49-54 hydroxyacid oxidase 1 Homo sapiens 0-15 31252482-5 2019 In this study, a novel curative strategy which combines glucose oxidase (GOx)-mediated Fe3O4-based Fenton reaction and multiwalled carbon nanotube (MWNT)-produced mild hyperthermia enhancer is proposed, achieving a mild hyperthermia-enhanced enzyme-mediated tumor cell CDT. ferryl iron 87-92 hydroxyacid oxidase 1 Homo sapiens 56-71 31252482-5 2019 In this study, a novel curative strategy which combines glucose oxidase (GOx)-mediated Fe3O4-based Fenton reaction and multiwalled carbon nanotube (MWNT)-produced mild hyperthermia enhancer is proposed, achieving a mild hyperthermia-enhanced enzyme-mediated tumor cell CDT. ferryl iron 87-92 hydroxyacid oxidase 1 Homo sapiens 73-76 31252482-6 2019 GOx can catalyze the conversion of glucose into gluconic acid and H2O2, which can elevate acidity in the tumor microenvironment and boost Fe3O4-based Fenton reaction, producing a myriad of OH to induce tumor cell death. ferryl iron 138-143 hydroxyacid oxidase 1 Homo sapiens 0-3 27956150-4 2017 Glucose oxidase (GOx) was immobilized on the PVA-Fe3O4 nanocomposite via physical adsorption. ferryl iron 49-54 hydroxyacid oxidase 1 Homo sapiens 17-20 27956150-9 2017 Presence of Fe3O4 nanoparticles in the PVA matrix enhanced the electron transfer between enzyme and electrode surface and the immobilized GOx showed excellent catalytic characteristic toward glucose. ferryl iron 12-17 hydroxyacid oxidase 1 Homo sapiens 138-141 27956150-10 2017 The GOx/PVA-Fe3O4/Sn bioelectrode could measure glucose in the range from 5 x 10-3 to 30 mM with a sensitivity of 9.36 muA mM-1 and exhibited a lower detection limit of 8 muM at a signal-to-noise ratio of 3. ferryl iron 12-17 hydroxyacid oxidase 1 Homo sapiens 4-7 20656467-4 2010 Moreover, glucose oxidase (GOx) and citrate-capped gold (Au) NPs, having negative charges, can be easily self-assembled at the surface of cationic PDDA-Fe3O4 NPs. ferryl iron 152-157 hydroxyacid oxidase 1 Homo sapiens 10-25 32261466-3 2014 Fe3O4@AuNP nanocomposites were used as labels of luminol, glucose oxidase (GOx) and signal aptamer which greatly enhanced the chemiluminescence emission and provided a simple magnetic separation approach to attain interference-free measurement for real detection. ferryl iron 0-5 hydroxyacid oxidase 1 Homo sapiens 58-73 32261466-3 2014 Fe3O4@AuNP nanocomposites were used as labels of luminol, glucose oxidase (GOx) and signal aptamer which greatly enhanced the chemiluminescence emission and provided a simple magnetic separation approach to attain interference-free measurement for real detection. ferryl iron 0-5 hydroxyacid oxidase 1 Homo sapiens 75-78 23208101-1 2013 In this study, a novel biomolecule immobilization approach has been proposed to the synthesis of multi-functional core-shell glucose oxidase-Au-polydopamine-Fe3O4 magnetic bionanoparticles (GOx-Au-PDA-Fe3O4 MBNPs) using the one-pot chemical polymerization method. ferryl iron 157-162 hydroxyacid oxidase 1 Homo sapiens 190-193 23208101-1 2013 In this study, a novel biomolecule immobilization approach has been proposed to the synthesis of multi-functional core-shell glucose oxidase-Au-polydopamine-Fe3O4 magnetic bionanoparticles (GOx-Au-PDA-Fe3O4 MBNPs) using the one-pot chemical polymerization method. ferryl iron 201-206 hydroxyacid oxidase 1 Homo sapiens 190-193 23208101-2 2013 Then, a high performance biosensor has been constructed by effectively attaching the proposed GOx-Au-PDA-Fe3O4 MBNPs to the surface of the magnetic glassy carbon electrode. ferryl iron 105-110 hydroxyacid oxidase 1 Homo sapiens 94-97 23208101-3 2013 Scanning electron microscope, energy dispersive x-ray spectrometer, UV-vis spectroscopy, and electrochemical methods were used to characterize the GOx-Au-PDA-Fe3O4 MBNPs. ferryl iron 158-163 hydroxyacid oxidase 1 Homo sapiens 147-150 23208101-4 2013 The resultant GOx-Au-PDA-Fe3O4 MBNPs not only have the magnetism of Fe3O4 nanoparticles which makes them easily manipulated by an external magnetic field, but also have the excellent biocompatibility of PDA to maintain the native structure of the GOx, and good conductivity of Au nanoparticles which can facilitate the direct electrochemistry of GOx in the biofilm. ferryl iron 25-30 hydroxyacid oxidase 1 Homo sapiens 14-17 23208101-4 2013 The resultant GOx-Au-PDA-Fe3O4 MBNPs not only have the magnetism of Fe3O4 nanoparticles which makes them easily manipulated by an external magnetic field, but also have the excellent biocompatibility of PDA to maintain the native structure of the GOx, and good conductivity of Au nanoparticles which can facilitate the direct electrochemistry of GOx in the biofilm. ferryl iron 25-30 hydroxyacid oxidase 1 Homo sapiens 247-250 23208101-4 2013 The resultant GOx-Au-PDA-Fe3O4 MBNPs not only have the magnetism of Fe3O4 nanoparticles which makes them easily manipulated by an external magnetic field, but also have the excellent biocompatibility of PDA to maintain the native structure of the GOx, and good conductivity of Au nanoparticles which can facilitate the direct electrochemistry of GOx in the biofilm. ferryl iron 25-30 hydroxyacid oxidase 1 Homo sapiens 247-250 23208101-4 2013 The resultant GOx-Au-PDA-Fe3O4 MBNPs not only have the magnetism of Fe3O4 nanoparticles which makes them easily manipulated by an external magnetic field, but also have the excellent biocompatibility of PDA to maintain the native structure of the GOx, and good conductivity of Au nanoparticles which can facilitate the direct electrochemistry of GOx in the biofilm. ferryl iron 68-73 hydroxyacid oxidase 1 Homo sapiens 14-17 23208101-5 2013 Hence, the present GOx-Au-PDA-Fe3O4 biofilm displays good linear amperometric response to glucose concentration ranging from 0.02 to 1.875 mM. ferryl iron 30-35 hydroxyacid oxidase 1 Homo sapiens 19-22 20656467-4 2010 Moreover, glucose oxidase (GOx) and citrate-capped gold (Au) NPs, having negative charges, can be easily self-assembled at the surface of cationic PDDA-Fe3O4 NPs. ferryl iron 152-157 hydroxyacid oxidase 1 Homo sapiens 27-30 20656467-5 2010 Without the requirement of a peroxidise enzyme, the composites of PDDA-Fe3O4 NPs and GOx effectively catalyzes the H2O2-mediated oxidation of 2,2"-azino-bis(3-ethylbenzothiazoline-6-sulfonate acid) (ABTS) in the presence of glucose. ferryl iron 71-76 hydroxyacid oxidase 1 Homo sapiens 85-88 34585187-0 2021 A multimodal strategy of Fe3O4@ZIF-8/GOx@MnO2 hybrid nanozyme via TME modulation for tumor therapy. ferryl iron 25-30 hydroxyacid oxidase 1 Homo sapiens 37-40 34585187-8 2021 At the same time, the intrinsic photothermal effect of Fe3O4 upon 808 nm laser irradiation promoted the activity of MnO2 and GOx as oxidase, and Fe(II) as catalase-like, and ablated the primary tumor. ferryl iron 55-60 hydroxyacid oxidase 1 Homo sapiens 125-128 35403639-3 2022 Natural glucose oxidase (GOx) and superparamagnetic Fe3O4 nanoparticles have been integrated into poly(lactic-co-glycolic acid) (PLGA) to fabricate a sequential nanocatalyst (designated as GOx@PLGA-Fe3O4). ferryl iron 52-57 hydroxyacid oxidase 1 Homo sapiens 189-192 35149425-4 2022 Herein, multifunctional bi-nanospheres (Fe3O4@Au NCs), which show both peroxidase-like and catalase-like catalytic activities in different working conditions, are successfully constructed and served as desirable platform with huge surface area for the immobilization of large amount of GOx probes. ferryl iron 40-45 hydroxyacid oxidase 1 Homo sapiens 286-289 35149425-5 2022 In acidic environment, hydroxyl radicals could be generated via the cascaded catalysis of beta-d-glucose by Fe3O4@Au-GOx, and then employed to initiate the polymerization of boric acid derivative to prepare molecularly imprinted polymers (MIPs) on the surface of GOx using beta-d-glucose as template. ferryl iron 108-113 hydroxyacid oxidase 1 Homo sapiens 117-120 35149425-5 2022 In acidic environment, hydroxyl radicals could be generated via the cascaded catalysis of beta-d-glucose by Fe3O4@Au-GOx, and then employed to initiate the polymerization of boric acid derivative to prepare molecularly imprinted polymers (MIPs) on the surface of GOx using beta-d-glucose as template. ferryl iron 108-113 hydroxyacid oxidase 1 Homo sapiens 263-266 35149425-6 2022 Then, the molecularly imprinted GOx are immobilized on the surface of highly oriented pyrolytic graphite (HOPG) electrode and an electrochemical biosensor (Fe3O4@Au-GOx-HOPG) for glucose sensing is successfully obtained. ferryl iron 156-161 hydroxyacid oxidase 1 Homo sapiens 32-35 35149425-6 2022 Then, the molecularly imprinted GOx are immobilized on the surface of highly oriented pyrolytic graphite (HOPG) electrode and an electrochemical biosensor (Fe3O4@Au-GOx-HOPG) for glucose sensing is successfully obtained. ferryl iron 156-161 hydroxyacid oxidase 1 Homo sapiens 165-168 34137418-3 2021 Herein, a cascade catalytic nanoplatform (GOx-NCs/Fe3O4) was designed by absorbing glucose oxidase (GOx) onto the surface of covalent-assembled polymer capsules (NCs) encapsulating Fe3O4 nanoparticles. ferryl iron 50-55 hydroxyacid oxidase 1 Homo sapiens 42-45 34137418-3 2021 Herein, a cascade catalytic nanoplatform (GOx-NCs/Fe3O4) was designed by absorbing glucose oxidase (GOx) onto the surface of covalent-assembled polymer capsules (NCs) encapsulating Fe3O4 nanoparticles. ferryl iron 50-55 hydroxyacid oxidase 1 Homo sapiens 83-98 34137418-3 2021 Herein, a cascade catalytic nanoplatform (GOx-NCs/Fe3O4) was designed by absorbing glucose oxidase (GOx) onto the surface of covalent-assembled polymer capsules (NCs) encapsulating Fe3O4 nanoparticles. ferryl iron 50-55 hydroxyacid oxidase 1 Homo sapiens 100-103 34137418-3 2021 Herein, a cascade catalytic nanoplatform (GOx-NCs/Fe3O4) was designed by absorbing glucose oxidase (GOx) onto the surface of covalent-assembled polymer capsules (NCs) encapsulating Fe3O4 nanoparticles. ferryl iron 181-186 hydroxyacid oxidase 1 Homo sapiens 42-45 34137418-3 2021 Herein, a cascade catalytic nanoplatform (GOx-NCs/Fe3O4) was designed by absorbing glucose oxidase (GOx) onto the surface of covalent-assembled polymer capsules (NCs) encapsulating Fe3O4 nanoparticles. ferryl iron 181-186 hydroxyacid oxidase 1 Homo sapiens 83-98 34137418-3 2021 Herein, a cascade catalytic nanoplatform (GOx-NCs/Fe3O4) was designed by absorbing glucose oxidase (GOx) onto the surface of covalent-assembled polymer capsules (NCs) encapsulating Fe3O4 nanoparticles. ferryl iron 181-186 hydroxyacid oxidase 1 Homo sapiens 100-103 35403639-3 2022 Natural glucose oxidase (GOx) and superparamagnetic Fe3O4 nanoparticles have been integrated into poly(lactic-co-glycolic acid) (PLGA) to fabricate a sequential nanocatalyst (designated as GOx@PLGA-Fe3O4). ferryl iron 198-203 hydroxyacid oxidase 1 Homo sapiens 8-23 35403639-3 2022 Natural glucose oxidase (GOx) and superparamagnetic Fe3O4 nanoparticles have been integrated into poly(lactic-co-glycolic acid) (PLGA) to fabricate a sequential nanocatalyst (designated as GOx@PLGA-Fe3O4). ferryl iron 198-203 hydroxyacid oxidase 1 Homo sapiens 25-28 35403639-3 2022 Natural glucose oxidase (GOx) and superparamagnetic Fe3O4 nanoparticles have been integrated into poly(lactic-co-glycolic acid) (PLGA) to fabricate a sequential nanocatalyst (designated as GOx@PLGA-Fe3O4). ferryl iron 198-203 hydroxyacid oxidase 1 Homo sapiens 189-192 32901482-9 2020 This indeed seen in the kcat obtained for Fe3O4@SHS (GOx added externally during assay), which is 18 times lower than that of GOx-Fe3O4@SHS. ferryl iron 130-135 hydroxyacid oxidase 1 Homo sapiens 126-129 33881052-3 2021 GOx on the surface of hollow mesoporous silica nanoparticles can catalyze the decomposition of intratumoral glucose to generate gluconic acid and H2O2, while Fe3O4 nanoparticles as a Fenton reaction catalyst can in situ catalyze H2O2 to produce highly toxic hydroxyl radicals ( OH). ferryl iron 158-163 hydroxyacid oxidase 1 Homo sapiens 0-3 32901482-4 2020 By tuning both shape and phase (vaterite/calcite and pure calcite) of CaCO3, it allows generation of GOx and Fe3O4-PEI encapsulated silica hollow microspheres (GOx-Fe3O4@SHS) and microcubes (GOx-Fe3O4@SHC). ferryl iron 109-114 hydroxyacid oxidase 1 Homo sapiens 160-163 32901482-4 2020 By tuning both shape and phase (vaterite/calcite and pure calcite) of CaCO3, it allows generation of GOx and Fe3O4-PEI encapsulated silica hollow microspheres (GOx-Fe3O4@SHS) and microcubes (GOx-Fe3O4@SHC). ferryl iron 109-114 hydroxyacid oxidase 1 Homo sapiens 160-163 32901482-4 2020 By tuning both shape and phase (vaterite/calcite and pure calcite) of CaCO3, it allows generation of GOx and Fe3O4-PEI encapsulated silica hollow microspheres (GOx-Fe3O4@SHS) and microcubes (GOx-Fe3O4@SHC). ferryl iron 164-169 hydroxyacid oxidase 1 Homo sapiens 160-163 32901482-4 2020 By tuning both shape and phase (vaterite/calcite and pure calcite) of CaCO3, it allows generation of GOx and Fe3O4-PEI encapsulated silica hollow microspheres (GOx-Fe3O4@SHS) and microcubes (GOx-Fe3O4@SHC). ferryl iron 164-169 hydroxyacid oxidase 1 Homo sapiens 160-163 32901482-6 2020 Comparison of the peroxidase like activity of the encapsulated Fe3O4-PEI shows that the hollow microspheres (GOx-Fe3O4@SHS) results in activity 14 times higher than that of the hollow microcubes (GOx-Fe3O4@SHC), which in turn is corroborated to the differential loading capacity of GOx in microspheres and microcubes. ferryl iron 63-68 hydroxyacid oxidase 1 Homo sapiens 109-112 32901482-6 2020 Comparison of the peroxidase like activity of the encapsulated Fe3O4-PEI shows that the hollow microspheres (GOx-Fe3O4@SHS) results in activity 14 times higher than that of the hollow microcubes (GOx-Fe3O4@SHC), which in turn is corroborated to the differential loading capacity of GOx in microspheres and microcubes. ferryl iron 63-68 hydroxyacid oxidase 1 Homo sapiens 196-199 32901482-6 2020 Comparison of the peroxidase like activity of the encapsulated Fe3O4-PEI shows that the hollow microspheres (GOx-Fe3O4@SHS) results in activity 14 times higher than that of the hollow microcubes (GOx-Fe3O4@SHC), which in turn is corroborated to the differential loading capacity of GOx in microspheres and microcubes. ferryl iron 63-68 hydroxyacid oxidase 1 Homo sapiens 196-199 32901482-6 2020 Comparison of the peroxidase like activity of the encapsulated Fe3O4-PEI shows that the hollow microspheres (GOx-Fe3O4@SHS) results in activity 14 times higher than that of the hollow microcubes (GOx-Fe3O4@SHC), which in turn is corroborated to the differential loading capacity of GOx in microspheres and microcubes. ferryl iron 113-118 hydroxyacid oxidase 1 Homo sapiens 109-112 32901482-6 2020 Comparison of the peroxidase like activity of the encapsulated Fe3O4-PEI shows that the hollow microspheres (GOx-Fe3O4@SHS) results in activity 14 times higher than that of the hollow microcubes (GOx-Fe3O4@SHC), which in turn is corroborated to the differential loading capacity of GOx in microspheres and microcubes. ferryl iron 113-118 hydroxyacid oxidase 1 Homo sapiens 196-199 32901482-6 2020 Comparison of the peroxidase like activity of the encapsulated Fe3O4-PEI shows that the hollow microspheres (GOx-Fe3O4@SHS) results in activity 14 times higher than that of the hollow microcubes (GOx-Fe3O4@SHC), which in turn is corroborated to the differential loading capacity of GOx in microspheres and microcubes. ferryl iron 113-118 hydroxyacid oxidase 1 Homo sapiens 196-199 32901482-7 2020 The evaluation of kinetic parameters indicates a 5 fold increase in the catalytic constant (kcat) of Fe3O4-PEI confined in hollow microspheres (GOx-Fe3O4@SHS) compared to the mixture comprising of free GOx and Fe3O4-PEI in solution. ferryl iron 101-106 hydroxyacid oxidase 1 Homo sapiens 144-147 32901482-7 2020 The evaluation of kinetic parameters indicates a 5 fold increase in the catalytic constant (kcat) of Fe3O4-PEI confined in hollow microspheres (GOx-Fe3O4@SHS) compared to the mixture comprising of free GOx and Fe3O4-PEI in solution. ferryl iron 101-106 hydroxyacid oxidase 1 Homo sapiens 202-205 32901482-9 2020 This indeed seen in the kcat obtained for Fe3O4@SHS (GOx added externally during assay), which is 18 times lower than that of GOx-Fe3O4@SHS. ferryl iron 42-47 hydroxyacid oxidase 1 Homo sapiens 53-56 32901482-9 2020 This indeed seen in the kcat obtained for Fe3O4@SHS (GOx added externally during assay), which is 18 times lower than that of GOx-Fe3O4@SHS. ferryl iron 42-47 hydroxyacid oxidase 1 Homo sapiens 126-129 32901482-9 2020 This indeed seen in the kcat obtained for Fe3O4@SHS (GOx added externally during assay), which is 18 times lower than that of GOx-Fe3O4@SHS. ferryl iron 130-135 hydroxyacid oxidase 1 Homo sapiens 53-56