PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 81-83 hydroxyacid oxidase 1 Homo sapiens 4-7 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 81-83 hydroxyacid oxidase 1 Homo sapiens 21-24 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 81-83 hydroxyacid oxidase 1 Homo sapiens 21-24 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 125-127 hydroxyacid oxidase 1 Homo sapiens 4-7 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 125-127 hydroxyacid oxidase 1 Homo sapiens 21-24 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 125-127 hydroxyacid oxidase 1 Homo sapiens 21-24 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 125-127 hydroxyacid oxidase 1 Homo sapiens 4-7 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 125-127 hydroxyacid oxidase 1 Homo sapiens 21-24 33161703-7 2020 The GOx on the Pd@Pt-GOx could catalyze the oxidation of intratumoral glucose by O2 for cancer starvation therapy, while the O2 produced from the decomposition of endogenous H2O2 by the Pd@Pt with the CAT-like activity could accelerate the O2-dependent depletion of glucose by GOx. Oxygen 125-127 hydroxyacid oxidase 1 Homo sapiens 21-24 33034314-5 2020 Once MONs-GOx@MnO2-Ce6 enter tumor cells, it catalyzes the oxidation of glucose using oxygen (O2) and generates hydrogen peroxide (H2O2) and gluconic acid, the former of which may accelerate the decomposition of MnO2 nanosheets. Oxygen 86-92 hydroxyacid oxidase 1 Homo sapiens 10-13 33034314-5 2020 Once MONs-GOx@MnO2-Ce6 enter tumor cells, it catalyzes the oxidation of glucose using oxygen (O2) and generates hydrogen peroxide (H2O2) and gluconic acid, the former of which may accelerate the decomposition of MnO2 nanosheets. Oxygen 16-18 hydroxyacid oxidase 1 Homo sapiens 10-13 34896831-5 2022 Once the bioreactor reached the desired region, GOx promptly consumed the intratumoral glucose and oxygen to starve cancer cells for robust starvation therapy. Oxygen 99-105 hydroxyacid oxidase 1 Homo sapiens 48-51 34798156-3 2022 In tumor microenvironment (TME), MnO2 nanosheets on the surface of mesoporous polydopamine (MPDA) could react with endogenous hydrogen peroxide (H2O2) and generate oxygen (O2) to relieve tumor hypoxia, thus enhancing the efficacy of PDT and GOx catalysis. Oxygen 164-170 hydroxyacid oxidase 1 Homo sapiens 241-244 34798156-3 2022 In tumor microenvironment (TME), MnO2 nanosheets on the surface of mesoporous polydopamine (MPDA) could react with endogenous hydrogen peroxide (H2O2) and generate oxygen (O2) to relieve tumor hypoxia, thus enhancing the efficacy of PDT and GOx catalysis. Oxygen 172-174 hydroxyacid oxidase 1 Homo sapiens 241-244 34798156-4 2022 Glucose consumption under the catalysis of GOx will enhance the acidity of TME and increase intracellular H2O2 concentration, which in turn promotes the production of O2 by MnO2 nanosheets, thus forming efficient cascade reaction and maximizing the efficacy of the functional agents. Oxygen 167-169 hydroxyacid oxidase 1 Homo sapiens 43-46 34757365-4 2021 In the case of off-targeting, when very few CeO2-GOx@CCM nanoparticles were accidentally delivered into normal tissue, its neutral pH environment (pH = 7.4) triggered a protective reaction, in which the H2O2 generated was catalyzed by CeO2 into non-toxic H2O and O2. Oxygen 263-265 hydroxyacid oxidase 1 Homo sapiens 49-52 34896860-4 2022 Herein, a biocompatible carbon nitride (C3N4)/nanozyme/GOx triple cascade nanocatalyst was designed with laser-activatable O2 self-supply via water splitting to relieve tumor hypoxia and thus improve the catalysis efficiency. Oxygen 123-125 hydroxyacid oxidase 1 Homo sapiens 55-58 34713523-2 2022 The composite (GOx&DhHP-6@ZIF-8) is then used to initiate oxygen-tolerant reversible addition-fragmentation chain-transfer (RAFT) polymerization for different methacrylate monomers, such as 2-diethylaminoethyl methacrylate, 2-hydroxyethyl methacrylate and poly (ethylene glycol) methyl ether methacrylate (Mn = 500 g mol-1 ). Oxygen 58-64 hydroxyacid oxidase 1 Homo sapiens 15-18 34517657-2 2021 Herein, an interrelated catalytic enzyme system has been developed, termed as CataFlower, which is composed of nanoflower MoS2 (peroxidase) decorated with GOx (glucose oxidase) and MnO2 (oxygen generator), and exhibits synergistic oxidative capability for sensitively monitoring sweat glucose. Oxygen 187-193 hydroxyacid oxidase 1 Homo sapiens 155-158 34517657-2 2021 Herein, an interrelated catalytic enzyme system has been developed, termed as CataFlower, which is composed of nanoflower MoS2 (peroxidase) decorated with GOx (glucose oxidase) and MnO2 (oxygen generator), and exhibits synergistic oxidative capability for sensitively monitoring sweat glucose. Oxygen 187-193 hydroxyacid oxidase 1 Homo sapiens 160-175 34517657-3 2021 CataFlower can not only generate oxygen in situ to maximize GOx activity, but promote peroxidase-triggered H2O2 oxidation of methylene blue, resulting in sensitive colorimetric detection of glucose. Oxygen 33-39 hydroxyacid oxidase 1 Homo sapiens 60-63 34606937-6 2021 Furthermore, the hydrogen peroxide generated by GOx as well as overexpressed in tumor can be decomposed by CAT and continuously generate oxygen, which further enhance the efficacy of oxygen-dependent starvation therapy and photodynamic therapy. Oxygen 137-143 hydroxyacid oxidase 1 Homo sapiens 48-51 34726226-4 2021 For synergistic cancer therapy, oxygen (O2) carried by PDA-PVAMBs@GOx was first released to promote starvation therapy by loaded GOx. Oxygen 32-38 hydroxyacid oxidase 1 Homo sapiens 66-69 34726226-4 2021 For synergistic cancer therapy, oxygen (O2) carried by PDA-PVAMBs@GOx was first released to promote starvation therapy by loaded GOx. Oxygen 32-38 hydroxyacid oxidase 1 Homo sapiens 129-132 34726226-4 2021 For synergistic cancer therapy, oxygen (O2) carried by PDA-PVAMBs@GOx was first released to promote starvation therapy by loaded GOx. Oxygen 40-42 hydroxyacid oxidase 1 Homo sapiens 66-69 34726226-4 2021 For synergistic cancer therapy, oxygen (O2) carried by PDA-PVAMBs@GOx was first released to promote starvation therapy by loaded GOx. Oxygen 40-42 hydroxyacid oxidase 1 Homo sapiens 129-132 34726226-5 2021 Then, moderate near-infrared (NIR) laser irradiation triggered PTT and improved enzymatic activity of GOx with its optimal activity around 47 C. Subsequently, GOx-mediated tumor starvation depleted O2 and exacerbated the hypoxia environment, thereby activating the toxicity of TPZ in the tumor site. Oxygen 199-201 hydroxyacid oxidase 1 Homo sapiens 102-105 34726226-5 2021 Then, moderate near-infrared (NIR) laser irradiation triggered PTT and improved enzymatic activity of GOx with its optimal activity around 47 C. Subsequently, GOx-mediated tumor starvation depleted O2 and exacerbated the hypoxia environment, thereby activating the toxicity of TPZ in the tumor site. Oxygen 199-201 hydroxyacid oxidase 1 Homo sapiens 160-163 34553729-0 2021 A flowerlike FePt/MnO2/GOx-based cascade nanoreactor with sustainable O2 supply for synergistic starvation-chemodynamic anticancer therapy. Oxygen 70-72 hydroxyacid oxidase 1 Homo sapiens 23-26 34553729-3 2021 In an acidic environment, intratumoral H2O2 could be decomposed to O2 to accelerate the consumption of glucose catalyzed by GOx to induce cancer starvation. Oxygen 67-69 hydroxyacid oxidase 1 Homo sapiens 124-127 34553729-6 2021 Therefore, BGMFP could catalyze a cascade of intracellular biochemical reactions and optimize the unique properties of MnO2, GOx and FePt via mutual promotion of each other to realize O2 supply, chemodynamic therapy (CDT) and starvation therapy. Oxygen 184-186 hydroxyacid oxidase 1 Homo sapiens 125-128 34153849-0 2021 Glucose oxidase loaded Cu2+ based metal-organic framework for glutathione depletion/reactive oxygen species elevation enhanced chemotherapy. Oxygen 93-99 hydroxyacid oxidase 1 Homo sapiens 0-15 34606937-6 2021 Furthermore, the hydrogen peroxide generated by GOx as well as overexpressed in tumor can be decomposed by CAT and continuously generate oxygen, which further enhance the efficacy of oxygen-dependent starvation therapy and photodynamic therapy. Oxygen 183-189 hydroxyacid oxidase 1 Homo sapiens 48-51 34577080-3 2021 Internalized by cancer cells, the GOx/CAT-NCs facilitate microenvironmental oxidation by catalyzing endogenous H2O2 to form O2, thereby accelerating intracellular glucose catabolism and enhancing cytotoxic singlet oxygen (1O2) production with infrared irradiation. Oxygen 124-126 hydroxyacid oxidase 1 Homo sapiens 34-37 34572575-2 2021 Glucose oxidase (GOx), which is considered as an attractive starvation reagent for cancer therapy, can effectively catalyze the conversion of glucose into gluconic acid and hydrogen peroxide (H2O2) in the presence of O2. Oxygen 217-219 hydroxyacid oxidase 1 Homo sapiens 0-15 34572575-2 2021 Glucose oxidase (GOx), which is considered as an attractive starvation reagent for cancer therapy, can effectively catalyze the conversion of glucose into gluconic acid and hydrogen peroxide (H2O2) in the presence of O2. Oxygen 217-219 hydroxyacid oxidase 1 Homo sapiens 17-20 34585187-6 2021 The generated O2 was utilized by GOx in starvation therapy to consume glucose and produce H2O2 and gluconic acid. Oxygen 14-16 hydroxyacid oxidase 1 Homo sapiens 33-36 34729313-5 2021 GOx maintains high enzymatic activity to catalyze glucose with assistant of oxygen to generate hydrogen peroxide (H2O2) as starvation therapy. Oxygen 76-82 hydroxyacid oxidase 1 Homo sapiens 0-3 34175561-3 2021 Based on Fenton reactions initiated by iron ions, CaO2-supplied H2O2 could not only generate OH for H2O2-sufficient CDT, but also produce O2 to promote the catalytic efficiency of GOx under hypoxia. Oxygen 139-141 hydroxyacid oxidase 1 Homo sapiens 181-184 34342219-3 2021 Herein, we constructed a self-sufficient hybrid enzyme-based silk fibroin hydrogel system, consisting of Pt-decorated hollow Ag-Au trimetallic nanocages (HGN@Pt) and glucose oxidase (GOx), to supply O2 continuously and consume glucose concurrently and, thereby, synergistically enhance the anti-cancer efficacy of a combined starvation and photothermal therapy operating in a hypoxic tumor microenvironment. Oxygen 199-201 hydroxyacid oxidase 1 Homo sapiens 166-181 34342219-3 2021 Herein, we constructed a self-sufficient hybrid enzyme-based silk fibroin hydrogel system, consisting of Pt-decorated hollow Ag-Au trimetallic nanocages (HGN@Pt) and glucose oxidase (GOx), to supply O2 continuously and consume glucose concurrently and, thereby, synergistically enhance the anti-cancer efficacy of a combined starvation and photothermal therapy operating in a hypoxic tumor microenvironment. Oxygen 199-201 hydroxyacid oxidase 1 Homo sapiens 183-186 34342219-9 2021 Finally, the O2 supplied by HGN@Pt overcame the hypoxia of the microenvironment and, thereby, promoted the starvation therapeutic effect of the GOx-mediated glucose consumption. Oxygen 13-15 hydroxyacid oxidase 1 Homo sapiens 144-147 34342219-10 2021 Meanwhile, the GOx-produced H2O2 from the oxidation of glucose could be used to regenerate O2 and, thereby, construct a complementary circulatory system. Oxygen 91-93 hydroxyacid oxidase 1 Homo sapiens 15-18 34436075-2 2021 Here, we studied the effect of DNA adsorption on electrochemical charge transfer at few-layered, oxygen-functionalized graphene (GOx) electrodes. Oxygen 97-103 hydroxyacid oxidase 1 Homo sapiens 129-132 34119887-5 2021 Herein, using glucose oxidase (GOx) as an O2-consuming agent to exacerbate hypoxia, a cascade strategy of GOx-induced overexpression of NTR and amplified NTR-catalyzed release was proposed for early antitumor therapy. Oxygen 42-44 hydroxyacid oxidase 1 Homo sapiens 14-29 34119887-5 2021 Herein, using glucose oxidase (GOx) as an O2-consuming agent to exacerbate hypoxia, a cascade strategy of GOx-induced overexpression of NTR and amplified NTR-catalyzed release was proposed for early antitumor therapy. Oxygen 42-44 hydroxyacid oxidase 1 Homo sapiens 31-34 34119887-5 2021 Herein, using glucose oxidase (GOx) as an O2-consuming agent to exacerbate hypoxia, a cascade strategy of GOx-induced overexpression of NTR and amplified NTR-catalyzed release was proposed for early antitumor therapy. Oxygen 42-44 hydroxyacid oxidase 1 Homo sapiens 106-109 34119887-8 2021 First, as a "key", tumor hypoxia triggers the initial release of GOx, which serves as the O2-consuming agent when catalyzing its reaction with glucose, which is accompanied by H2O2 production. Oxygen 90-92 hydroxyacid oxidase 1 Homo sapiens 65-68 35452214-8 2022 This antitumorigenic potential of FA-CD-(PTX-GOx) could be attributed to the enhanced intratumoral reactive oxygen species generation following glucose depletion by GOx that has been facilitated by the chemotherapeutic efficacy of PTX resulting in the efficient killing of cancer cells. Oxygen 108-114 hydroxyacid oxidase 1 Homo sapiens 45-48 34095615-3 2021 Taking advantage of the catalytic activity of Mn ions, the composite hydrogels could decompose hydrogen peroxide (H2O2) into oxygen (O2), which can alleviate the problem of tumor hypoxia microenvironment and endow GOx with an ability to consume glucose in the presence of O2 for tumor starvation. Oxygen 125-131 hydroxyacid oxidase 1 Homo sapiens 214-217 34095615-3 2021 Taking advantage of the catalytic activity of Mn ions, the composite hydrogels could decompose hydrogen peroxide (H2O2) into oxygen (O2), which can alleviate the problem of tumor hypoxia microenvironment and endow GOx with an ability to consume glucose in the presence of O2 for tumor starvation. Oxygen 133-135 hydroxyacid oxidase 1 Homo sapiens 214-217 34095615-3 2021 Taking advantage of the catalytic activity of Mn ions, the composite hydrogels could decompose hydrogen peroxide (H2O2) into oxygen (O2), which can alleviate the problem of tumor hypoxia microenvironment and endow GOx with an ability to consume glucose in the presence of O2 for tumor starvation. Oxygen 272-274 hydroxyacid oxidase 1 Homo sapiens 214-217 35580473-5 2022 The resultant GOx exposure initiates intratumoral glucose depletion, which is promoted by the O2 replenishment through Pt-catalyzed decomposition of H2O2. Oxygen 94-96 hydroxyacid oxidase 1 Homo sapiens 14-17 35452214-8 2022 This antitumorigenic potential of FA-CD-(PTX-GOx) could be attributed to the enhanced intratumoral reactive oxygen species generation following glucose depletion by GOx that has been facilitated by the chemotherapeutic efficacy of PTX resulting in the efficient killing of cancer cells. Oxygen 108-114 hydroxyacid oxidase 1 Homo sapiens 165-168 35383789-5 2022 When TPZ@FeMSN-GOX entered the tumor cells, GOX could not only exhaust glucose to starve cancer cells and concomitantly produce H2O2, but also consume O2 to aggravate the hypoxia environment and amplify TPZ-mediated chemotherapy. Oxygen 151-153 hydroxyacid oxidase 1 Homo sapiens 15-18 35383789-5 2022 When TPZ@FeMSN-GOX entered the tumor cells, GOX could not only exhaust glucose to starve cancer cells and concomitantly produce H2O2, but also consume O2 to aggravate the hypoxia environment and amplify TPZ-mediated chemotherapy. Oxygen 151-153 hydroxyacid oxidase 1 Homo sapiens 44-47 34008688-5 2021 Upon initial dissociation of the host-guest interactions and hence Au NVs by cancer-specific reactive oxygen species (ROS), GOx is released to consume glucose and oxygen, generate H2O2 and induce the hypoxic TME, which act as the two keys for triggering burst payload release and promoter activation, thus allowing synergistic starvation and gene therapy of cancer. Oxygen 102-108 hydroxyacid oxidase 1 Homo sapiens 124-127 35253953-8 2022 For membranes prepared with relatively higher GOx, oxygen-limited behavior is considered the source of diminished sensitivity at higher glucose levels. Oxygen 51-57 hydroxyacid oxidase 1 Homo sapiens 46-49 35348331-5 2022 GOx could effectively consume oxygen and catalyzed glucose into gluconic acid and hydrogen peroxide. Oxygen 30-36 hydroxyacid oxidase 1 Homo sapiens 0-3 35327664-3 2022 Glucose oxidase catalyzes the oxidation of beta-d-glucose to d-glucono-delta-lactone and hydrogen peroxide in the presence of molecular oxygen. Oxygen 136-142 hydroxyacid oxidase 1 Homo sapiens 0-15 32206911-4 2020 Using the photoelectrode of CoxOyHz@ZIF-67/TiO2 nanotubes (NTs), glucose was oxidized firstly by dissolved oxygen to generate H2O2 under the catalysis of CoxOyHz film as the mimics of GOx. Oxygen 107-113 hydroxyacid oxidase 1 Homo sapiens 184-187 33984636-6 2021 GOx would rapidly exhaust endogenous glucose and O2 to shut off the energy supply of tumor cells for starvation treatment. Oxygen 49-51 hydroxyacid oxidase 1 Homo sapiens 0-3 33720684-5 2021 Then, the conjugated GOx can utilize O2 production to catalyze intracellular glucose to generate H2O2, which not only starves the tumor cells but also promotes oxidation of l-Arg to NO. Oxygen 37-39 hydroxyacid oxidase 1 Homo sapiens 21-24 33656325-3 2021 CuCo(O) was characterized as the Cu0.3Co2.7O4 phase through X-ray diffraction analysis and it can react with H2O2 to generate O2 and alleviate tumor hypoxia, resulting in the recovered enzymatic activity of GOx and the enhanced starvation therapy. Oxygen 111-113 hydroxyacid oxidase 1 Homo sapiens 207-210 33656325-5 2021 The three-in-one functions of oxygen supply, glucose consumption, and photothermal conversion were realized in the ZIFs-derived CuCo(O)/GOx@PCNs nanozyme and the starvation therapy effect was improved by PTT and oxygen supplement. Oxygen 30-36 hydroxyacid oxidase 1 Homo sapiens 136-139 33656325-5 2021 The three-in-one functions of oxygen supply, glucose consumption, and photothermal conversion were realized in the ZIFs-derived CuCo(O)/GOx@PCNs nanozyme and the starvation therapy effect was improved by PTT and oxygen supplement. Oxygen 212-218 hydroxyacid oxidase 1 Homo sapiens 136-139 33465212-3 2021 In this nanosystem, the loaded Dex can not only expand the pores of the nucleus to promote GOx to enter the nucleus, addressing the shortcomings of short life of reactive oxygen species, but also inhibit the production of collagen to reshape the tumor microenvironment and inhibit lung metastasis. Oxygen 171-177 hydroxyacid oxidase 1 Homo sapiens 91-94 31838457-5 2020 To overcome the inherent drawback of GOx, namely, the use of oxygen as the electron acceptor, various glucose dehydrogenases (GDHs) have been utilized in second-generation principle-based sensors. Oxygen 61-67 hydroxyacid oxidase 1 Homo sapiens 37-40 33787203-4 2021 The GOx utilizes glucose to produce hydrogen peroxide, which is subsequently degraded by Cat, resulting in the generation of active radicals and/or oxygen bubbles that propel the particles. Oxygen 148-154 hydroxyacid oxidase 1 Homo sapiens 4-7 33964699-2 2021 Herein, an intelligent reactive oxygen species (ROS) nanogenerator Ce6/GOx@ZIF-8/PDA@MnO2 (denoted as CGZPM; Ce6, GOx, ZIF-8, PDA, MnO2 are chlorin e6, glucose oxidase, zeolitic imidazolate framework-8, polydopamine and manganese dioxide respectively) with O2-generating and GSH-/glucose-depleting abilities was constructed by a facile and green one-pot method. Oxygen 87-89 hydroxyacid oxidase 1 Homo sapiens 71-74 33964699-2 2021 Herein, an intelligent reactive oxygen species (ROS) nanogenerator Ce6/GOx@ZIF-8/PDA@MnO2 (denoted as CGZPM; Ce6, GOx, ZIF-8, PDA, MnO2 are chlorin e6, glucose oxidase, zeolitic imidazolate framework-8, polydopamine and manganese dioxide respectively) with O2-generating and GSH-/glucose-depleting abilities was constructed by a facile and green one-pot method. Oxygen 87-89 hydroxyacid oxidase 1 Homo sapiens 114-117 33964699-4 2021 The Mn2+ acted as an ideal Fenton-like agent and magnetic resonance (MR) imaging contrast agent, while the O2 promoted the PDT via hypoxia relief and facilitated the intratumoral glucose oxidation by GOx for starvation therapy (ST). Oxygen 107-109 hydroxyacid oxidase 1 Homo sapiens 200-203 33231593-5 2020 Initiated by the breakdown of glucose into gluconic acid and H2O2 by GOx, Fe-PDAP promotes reoxygenation by catalyzing the reaction-supplied and tumor cell-supplied H2O2 into O2, which then enhances the O2-dependent PDT. Oxygen 63-65 hydroxyacid oxidase 1 Homo sapiens 69-72 33231593-5 2020 Initiated by the breakdown of glucose into gluconic acid and H2O2 by GOx, Fe-PDAP promotes reoxygenation by catalyzing the reaction-supplied and tumor cell-supplied H2O2 into O2, which then enhances the O2-dependent PDT. Oxygen 167-169 hydroxyacid oxidase 1 Homo sapiens 69-72 32806277-4 2020 The nano-conjugate constitutes of the nano-carrier (AuNP-PEG-RGD) and glucose oxidase (GOx, activity equivalent), which not only can specifically target cancer cells with the help of the cancer-targeting peptide (RGD) laid on the surface, but also can deplete glucose and O2 with the simultaneous generation of H2O2. Oxygen 272-274 hydroxyacid oxidase 1 Homo sapiens 70-85 32806277-4 2020 The nano-conjugate constitutes of the nano-carrier (AuNP-PEG-RGD) and glucose oxidase (GOx, activity equivalent), which not only can specifically target cancer cells with the help of the cancer-targeting peptide (RGD) laid on the surface, but also can deplete glucose and O2 with the simultaneous generation of H2O2. Oxygen 272-274 hydroxyacid oxidase 1 Homo sapiens 87-90 33015023-2 2020 Glucose oxidase (GOx), an enzyme that catalyzes the conversion of glucose to glucolactone, producing oxygen and hydrogen peroxide in the process, has proved useful in this regard. Oxygen 101-107 hydroxyacid oxidase 1 Homo sapiens 0-15 33015023-2 2020 Glucose oxidase (GOx), an enzyme that catalyzes the conversion of glucose to glucolactone, producing oxygen and hydrogen peroxide in the process, has proved useful in this regard. Oxygen 101-107 hydroxyacid oxidase 1 Homo sapiens 17-20 33015023-7 2020 When oxygen is plentiful, GOx promotes glucose consumption, allowing amplification of its effects on tumor starvation. Oxygen 5-11 hydroxyacid oxidase 1 Homo sapiens 26-29 32995127-0 2020 Porous Pt Nanospheres Incorporated with GOx to Enable Synergistic Oxygen-Inductive Starvation/Electrodynamic Tumor Therapy. Oxygen 66-72 hydroxyacid oxidase 1 Homo sapiens 40-43 32995127-2 2020 However, this reaction of catalytic oxidation by GOx is highly dependent on the on-site oxygen content, and thus starvation therapy often suffers unexpected anticancer outcomes due to the intrinsic tumorous hypoxia. Oxygen 88-94 hydroxyacid oxidase 1 Homo sapiens 49-52 32995127-4 2020 In this system, GOx can effectively catalyze the oxidation of glucose to generate H2O2, while pPt triggers the decomposition of both endogenous and exogenous H2O2 to produce considerable content of O2 to facilitate the glucose consumption by GOx. Oxygen 84-86 hydroxyacid oxidase 1 Homo sapiens 16-19 32175544-3 2020 GOx reduces atmospheric O2 to H2O2, causing a cyclic change of cerium ion states, resulting in propagating free radicals in the carbon group in the amino functionalised nanoceria surface. Oxygen 24-26 hydroxyacid oxidase 1 Homo sapiens 0-3 32175544-6 2020 GOx held two major roles within the reaction: to provide an oxygen free system, without any other form of degassing, and to provide cyclical cerium ion states between Ce4+ and Ce3+, creating new free radicals for polymerisation. Oxygen 60-66 hydroxyacid oxidase 1 Homo sapiens 0-3 31282750-2 2020 However, the oxygen consumption induced by SDT and glucose oxidase (GOx) mediated starvation therapy would worsen the hypoxic tumor environment, which further impeded therapeutic efficacy. Oxygen 13-19 hydroxyacid oxidase 1 Homo sapiens 51-66 31282750-2 2020 However, the oxygen consumption induced by SDT and glucose oxidase (GOx) mediated starvation therapy would worsen the hypoxic tumor environment, which further impeded therapeutic efficacy. Oxygen 13-19 hydroxyacid oxidase 1 Homo sapiens 68-71 31747128-1 2019 Glucose oxidase (GOx) can react with intracellular glucose and oxygen (O2 ) to produce hydrogen peroxide (H2 O2 ) and gluconic acid, which can cut off the nutrition source of cancer cells and consequently inhibit their proliferation. Oxygen 63-69 hydroxyacid oxidase 1 Homo sapiens 0-15 31680346-5 2019 Moreover, under hypoxia TME, the catalase-like CMS could react with endogenous H2 O2 to generate O2 for activating the catalyzed oxidation of glucose by GOx for starvation therapy accompanied with the regeneration of H2 O2 . Oxygen 82-84 hydroxyacid oxidase 1 Homo sapiens 153-156 31769461-4 2020 Moreover, Azo achieved charge reversal in a hypoxia microenvironment caused by the sustained oxygen consumption by GOx, which resulted in selective and enhanced tumor accumulation based on the hypoxia-activated positive feedback cellular uptake. Oxygen 93-99 hydroxyacid oxidase 1 Homo sapiens 115-118 31747128-1 2019 Glucose oxidase (GOx) can react with intracellular glucose and oxygen (O2 ) to produce hydrogen peroxide (H2 O2 ) and gluconic acid, which can cut off the nutrition source of cancer cells and consequently inhibit their proliferation. Oxygen 63-69 hydroxyacid oxidase 1 Homo sapiens 17-20 31784833-4 2019 If glucose oxidase (GOx) catalyzes the oxidation of glucose, dissolved oxygen is consumed. Oxygen 71-77 hydroxyacid oxidase 1 Homo sapiens 3-18 31784833-4 2019 If glucose oxidase (GOx) catalyzes the oxidation of glucose, dissolved oxygen is consumed. Oxygen 71-77 hydroxyacid oxidase 1 Homo sapiens 20-23 31291092-5 2019 Once released, GOx can rapidly deplete glucose and molecular oxygen in tumor cells while the toxic side product, i.e., H2O2, can be readily decomposed by CAT for site-specific and low-toxicity tumor starvation. Oxygen 61-67 hydroxyacid oxidase 1 Homo sapiens 15-18 30841739-2 2019 For some BGMS using glucose oxidase (GOx)-based test strips, one of these factors is the oxygen partial pressure (pO2) of the applied blood sample. Oxygen 89-95 hydroxyacid oxidase 1 Homo sapiens 20-35 30841739-2 2019 For some BGMS using glucose oxidase (GOx)-based test strips, one of these factors is the oxygen partial pressure (pO2) of the applied blood sample. Oxygen 89-95 hydroxyacid oxidase 1 Homo sapiens 37-40 31720532-4 2019 The response of the SOI-GOx working electrode was significantly higher in the presence of oxygen than that without oxygen, indicating that a hydrogen peroxide pathway dominated in our SOI-GOx electrode. Oxygen 90-96 hydroxyacid oxidase 1 Homo sapiens 24-27 31720532-4 2019 The response of the SOI-GOx working electrode was significantly higher in the presence of oxygen than that without oxygen, indicating that a hydrogen peroxide pathway dominated in our SOI-GOx electrode. Oxygen 90-96 hydroxyacid oxidase 1 Homo sapiens 188-191 31720532-4 2019 The response of the SOI-GOx working electrode was significantly higher in the presence of oxygen than that without oxygen, indicating that a hydrogen peroxide pathway dominated in our SOI-GOx electrode. Oxygen 115-121 hydroxyacid oxidase 1 Homo sapiens 24-27 31720532-4 2019 The response of the SOI-GOx working electrode was significantly higher in the presence of oxygen than that without oxygen, indicating that a hydrogen peroxide pathway dominated in our SOI-GOx electrode. Oxygen 115-121 hydroxyacid oxidase 1 Homo sapiens 188-191 31498991-2 2019 For this purpose, a recently reported methodology that employs the enzyme glucose oxidase (GOx) to deplete oxygen in reaction media was utilized. Oxygen 107-113 hydroxyacid oxidase 1 Homo sapiens 74-89 31498991-2 2019 For this purpose, a recently reported methodology that employs the enzyme glucose oxidase (GOx) to deplete oxygen in reaction media was utilized. Oxygen 107-113 hydroxyacid oxidase 1 Homo sapiens 91-94 31374171-5 2019 In addition to efficient removal of H2O2 for self-protection of normal tissues via antioxidation, GOx/TPZ-coloaded HMBRN can also rapidly deplete intratumoral glucose/oxygen to promote a synergistic starvation-enhanced bioreductive chemotherapeutic effect for the substantial suppression of solid tumor growth. Oxygen 167-173 hydroxyacid oxidase 1 Homo sapiens 98-101 31374171-1 2019 A major concern about glucose oxidase (GOx)-mediated cancer starvation therapy is its ability to induce serious oxidative damage to normal tissues through the massive production of H2O2 byproducts in the oxygen-involved glucose decomposition reaction, which may be addressed by using a H2O2 scavenger, known as an antioxidation agent. Oxygen 204-210 hydroxyacid oxidase 1 Homo sapiens 22-37 31374171-1 2019 A major concern about glucose oxidase (GOx)-mediated cancer starvation therapy is its ability to induce serious oxidative damage to normal tissues through the massive production of H2O2 byproducts in the oxygen-involved glucose decomposition reaction, which may be addressed by using a H2O2 scavenger, known as an antioxidation agent. Oxygen 204-210 hydroxyacid oxidase 1 Homo sapiens 39-42 31078766-6 2019 After that, the GOx in GMP@RBC could effectively catalyze the conversion of endogenous glucose to hydrogen peroxide (H2O2) in the presence of oxygen. Oxygen 142-148 hydroxyacid oxidase 1 Homo sapiens 16-19 31048253-7 2019 In the INAzymes system, glucose is converted to gluconic acid by GOx in the presence of oxygen to produce H2O2 as an intermediate. Oxygen 88-94 hydroxyacid oxidase 1 Homo sapiens 65-68 31030174-3 2019 Among those glucose sensors, few have been thought and well-engineered and do not solve the problems associated with glucose oxidase; among which the O2 sensitivity of the enzyme or the competition between O2 and redox mediators for GOx"s electrons. Oxygen 150-152 hydroxyacid oxidase 1 Homo sapiens 233-236 31030174-3 2019 Among those glucose sensors, few have been thought and well-engineered and do not solve the problems associated with glucose oxidase; among which the O2 sensitivity of the enzyme or the competition between O2 and redox mediators for GOx"s electrons. Oxygen 206-208 hydroxyacid oxidase 1 Homo sapiens 233-236 31030174-4 2019 Enzyme engineering has been employed to solve those issues but screening GOx in homogeneous solution with O2 as an electron acceptor is not suitable. Oxygen 106-108 hydroxyacid oxidase 1 Homo sapiens 73-76 31179709-4 2019 Under hypoxia environment, we observed that MnO2 could react with endogenous H2O2 to produce O2 for enhancing the catalytic efficiency of GOx for starvation therapy. Oxygen 46-48 hydroxyacid oxidase 1 Homo sapiens 138-141 31179709-6 2019 The biochemical reaction cycle, consisting of MnO2, O2, GOx, and H+, was triggered by the tumor microenvironment and accelerated each other so as to achieve self-supplied H+ and accelerate O2 generation, enhancing the starvation therapy, alleviating tumor hypoxia and accelerating the reactive oxygen species generation in photodynamic therapy. Oxygen 48-50 hydroxyacid oxidase 1 Homo sapiens 56-59 31179709-6 2019 The biochemical reaction cycle, consisting of MnO2, O2, GOx, and H+, was triggered by the tumor microenvironment and accelerated each other so as to achieve self-supplied H+ and accelerate O2 generation, enhancing the starvation therapy, alleviating tumor hypoxia and accelerating the reactive oxygen species generation in photodynamic therapy. Oxygen 294-300 hydroxyacid oxidase 1 Homo sapiens 56-59 30870640-5 2019 3-fold compared with that of the plain electrode, while an in situ deoxygenation process, based on GOx-glucose enzyme reaction, depletes dissolved oxygen. Oxygen 69-75 hydroxyacid oxidase 1 Homo sapiens 99-102 30921734-3 2019 Here, we utilize GOx-CPO as integrated tandem enzymes to in situ generate singlet oxygen, which could be not only for oxidative cross-linking of injectable hydrogel carriers but also for continuous tumor treatment by adjustable bioconversion of blood oxygen, glucose, and chloride ion. Oxygen 82-88 hydroxyacid oxidase 1 Homo sapiens 17-20 29594588-0 2017 Glucose oxidase assisted visual detection of glucose using oxygen deficient alpha-MoO3-x nanoflakes. Oxygen 59-65 hydroxyacid oxidase 1 Homo sapiens 0-15 30865742-4 2019 In the slightly acidic environment of cancer cells, GOx is released and it consumes d-glucose and molecular oxygen, nutrients essential for the survival of cancer cells, and produces gluconic acid and hydrogen peroxide, respectively. Oxygen 108-114 hydroxyacid oxidase 1 Homo sapiens 52-55 32254161-3 2019 As a proof of concept, we study the kinetics of glucose oxidase (GOx) catalyzed reactions using a triphase system fabricated by layering GOx upon superhydrophobic mesoporous ZnO nanowire arrays through which oxygen, needed for the enzymatic reaction, is supplied directly from the atmosphere to the liquid-solid interface. Oxygen 208-214 hydroxyacid oxidase 1 Homo sapiens 48-63 32254161-3 2019 As a proof of concept, we study the kinetics of glucose oxidase (GOx) catalyzed reactions using a triphase system fabricated by layering GOx upon superhydrophobic mesoporous ZnO nanowire arrays through which oxygen, needed for the enzymatic reaction, is supplied directly from the atmosphere to the liquid-solid interface. Oxygen 208-214 hydroxyacid oxidase 1 Homo sapiens 65-68 30001103-0 2018 Fabrication of Activity-Reporting Glucose Oxidase Nanocapsules with Oxygen-Independent Fluorescence Variation. Oxygen 68-74 hydroxyacid oxidase 1 Homo sapiens 34-49 30001103-6 2018 The peripheral polymer shell confines the orientation of GOx and prevents it from denaturing, whereas incorporated DAA-flavin can replace the oxygen as an alternative electron acceptor to interact with the active centers of GOx in the presence of the substrate, thus giving the nanocapsules oxygen-independent characteristics. Oxygen 142-148 hydroxyacid oxidase 1 Homo sapiens 224-227 30001103-6 2018 The peripheral polymer shell confines the orientation of GOx and prevents it from denaturing, whereas incorporated DAA-flavin can replace the oxygen as an alternative electron acceptor to interact with the active centers of GOx in the presence of the substrate, thus giving the nanocapsules oxygen-independent characteristics. Oxygen 291-297 hydroxyacid oxidase 1 Homo sapiens 224-227 29765012-3 2018 The proposed fluorescence sensing mechanism for detection of glucose is related to the consumption of dissolved oxygen at the double layer of the electrode which is fluorescence quenching agent by glucose-GOx reaction. Oxygen 112-118 hydroxyacid oxidase 1 Homo sapiens 205-208 29510031-4 2018 The nanocarriers are designed to enhance the efficacy of the hypoxia-suppressed GOx-mediated starvation therapy by catalyzing the decomposition of intratumoral hydroperoxide into oxygen with PHPBNs, and the enhanced glucose depletion by the two complementary biocatalysts may consequently suppress the expression of heat shock proteins (HSPs) after photothermal treatment to reduce their resistance to the PHPBN-mediated low-temperature photothermal therapies. Oxygen 179-185 hydroxyacid oxidase 1 Homo sapiens 80-83 29240973-2 2018 This air-tolerant ATRP was enabled by the continuous conversion of oxygen to carbon dioxide catalyzed by glucose oxidase (GOx), in the presence of glucose and sodium pyruvate as sequential sacrificial substrates. Oxygen 67-73 hydroxyacid oxidase 1 Homo sapiens 105-120 29240973-2 2018 This air-tolerant ATRP was enabled by the continuous conversion of oxygen to carbon dioxide catalyzed by glucose oxidase (GOx), in the presence of glucose and sodium pyruvate as sequential sacrificial substrates. Oxygen 67-73 hydroxyacid oxidase 1 Homo sapiens 122-125 29240973-4 2018 Without added pyruvates, lower MWs were observed due to generation of new chains by H2 O2 formed by reaction of O2 with GOx. Oxygen 87-89 hydroxyacid oxidase 1 Homo sapiens 120-123 30719775-3 2019 As a proof-of-concept, glucose oxidase (GOx) was encapsulated in situ within an oxygen (O2 )-sensitive, noble-metal-free, luminescent CuI triazolate framework (MAF-2), denoted as GOx@MAF-2. Oxygen 80-86 hydroxyacid oxidase 1 Homo sapiens 23-38 30719775-3 2019 As a proof-of-concept, glucose oxidase (GOx) was encapsulated in situ within an oxygen (O2 )-sensitive, noble-metal-free, luminescent CuI triazolate framework (MAF-2), denoted as GOx@MAF-2. Oxygen 80-86 hydroxyacid oxidase 1 Homo sapiens 40-43 30719775-3 2019 As a proof-of-concept, glucose oxidase (GOx) was encapsulated in situ within an oxygen (O2 )-sensitive, noble-metal-free, luminescent CuI triazolate framework (MAF-2), denoted as GOx@MAF-2. Oxygen 88-90 hydroxyacid oxidase 1 Homo sapiens 23-38 30719775-3 2019 As a proof-of-concept, glucose oxidase (GOx) was encapsulated in situ within an oxygen (O2 )-sensitive, noble-metal-free, luminescent CuI triazolate framework (MAF-2), denoted as GOx@MAF-2. Oxygen 88-90 hydroxyacid oxidase 1 Homo sapiens 40-43 30719775-5 2019 More importantly, owing to the O2 sensitivity of MAF-2, the GOx@MAF-2 composite exhibited a rapid and reversible response towards dissolved O2 , thereby allowing direct and ratiometric sensing of glucose without the need for chromogenic substrates, cascade enzymatic reactions, or electrode systems. Oxygen 31-33 hydroxyacid oxidase 1 Homo sapiens 60-63 30719775-5 2019 More importantly, owing to the O2 sensitivity of MAF-2, the GOx@MAF-2 composite exhibited a rapid and reversible response towards dissolved O2 , thereby allowing direct and ratiometric sensing of glucose without the need for chromogenic substrates, cascade enzymatic reactions, or electrode systems. Oxygen 140-142 hydroxyacid oxidase 1 Homo sapiens 60-63 30674187-2 2019 Glucose oxidase (GOx) can inexpensively enable radical polymerization in solution by enzymatically consuming oxygen as it oxidizes glucose. Oxygen 109-115 hydroxyacid oxidase 1 Homo sapiens 0-15 30674187-2 2019 Glucose oxidase (GOx) can inexpensively enable radical polymerization in solution by enzymatically consuming oxygen as it oxidizes glucose. Oxygen 109-115 hydroxyacid oxidase 1 Homo sapiens 17-20 31815054-8 2018 GOx-assisted oxygen removal in the synthesis of hydrophobic polymers is reported for the first time. Oxygen 13-19 hydroxyacid oxidase 1 Homo sapiens 0-3 30265804-4 2018 The fabricated TGZ@eM nanoreactor can assist the delivery of GOx to tumor cells and then exhaust endogenous glucose and O2 to starve tumors efficiently. Oxygen 120-122 hydroxyacid oxidase 1 Homo sapiens 61-64 29959868-4 2018 To design optimized enzyme-mediator couples and to describe a mediator binding model, a joint experimental and computational study was performed based on an oxygen-independent GOx variant V7 and two quinone diimine based electron mediators (QDM-1 and QDM-2), which differ in polarity and size, and ferrocenemethanol (FM). Oxygen 157-163 hydroxyacid oxidase 1 Homo sapiens 176-179 29750865-5 2018 Amperometric measurements using the GOx biosensor were performed at -0.7 V by following the oxygen consumption due to the enzymatic reaction in different glucose concentrations. Oxygen 92-98 hydroxyacid oxidase 1 Homo sapiens 36-39 29702470-3 2018 As a result of the enzymatic reaction between GOx and glucose, the glucose amount was determined by monitoring the change in the oxygen level associated with substrate concentration via the amperometric detection technique. Oxygen 129-135 hydroxyacid oxidase 1 Homo sapiens 46-49 29427882-1 2018 In enzymatic fuel cells (EnFCs), hydrogen peroxide formation is one of the main problems when enzymes, such as, glucose oxidase (GOx) is used due to the conversion of oxygen to hydrogen peroxide in the catalytic reaction. Oxygen 167-173 hydroxyacid oxidase 1 Homo sapiens 112-127 29427882-1 2018 In enzymatic fuel cells (EnFCs), hydrogen peroxide formation is one of the main problems when enzymes, such as, glucose oxidase (GOx) is used due to the conversion of oxygen to hydrogen peroxide in the catalytic reaction. Oxygen 167-173 hydroxyacid oxidase 1 Homo sapiens 129-132 29119659-5 2017 Moreover, the GOx@ZIF-8(NiPd) modified electrode showed good bioactivity of GOx and high electrocatalytic activity for the oxygen reduction reaction (ORR), which could also be used for electrochemical detection of glucose. Oxygen 123-129 hydroxyacid oxidase 1 Homo sapiens 14-17 29119659-5 2017 Moreover, the GOx@ZIF-8(NiPd) modified electrode showed good bioactivity of GOx and high electrocatalytic activity for the oxygen reduction reaction (ORR), which could also be used for electrochemical detection of glucose. Oxygen 123-129 hydroxyacid oxidase 1 Homo sapiens 76-79 28665600-4 2017 Interestingly, it is observed that the O2 could participate in the enzymatic reaction directly from gas phase through the proposed nanochannels, and a hydrophobic interface is more favorable for the enzymatic reaction due to the rearrangement of GOx structure as well as the high gas adhesion. Oxygen 39-41 hydroxyacid oxidase 1 Homo sapiens 246-249 28284922-5 2017 We first evaluated the effect of soluble GOX on inducing solution hypoxia (O2<5%) and found that both unmodified and acrylated GOX could sustain hypoxia for at least 24h even under ambient air condition with constant oxygen diffusion from the air-liquid interface. Oxygen 220-226 hydroxyacid oxidase 1 Homo sapiens 130-133 27426264-0 2016 Fabrication of Mediatorless/Membraneless Glucose/Oxygen Based Biofuel Cell using Biocatalysts Including Glucose Oxidase and Laccase Enzymes. Oxygen 49-55 hydroxyacid oxidase 1 Homo sapiens 104-119 26937455-3 2016 Here we used a model of oxidative stress by employing glucose/glucose oxidase (GOx), which (based on the availability of glucose and oxygen) is known to produce H2O2. Oxygen 133-139 hydroxyacid oxidase 1 Homo sapiens 79-82 26785309-5 2016 Glucose oxidase (GOx) or glucose dehydrogenase (GDH) were immobilized on bioanode and oxidize glucose while oxygen reduced in biocathode using immobilized laccase or bilirubin oxidase in order to generate sufficient power. Oxygen 108-114 hydroxyacid oxidase 1 Homo sapiens 0-15 26785309-5 2016 Glucose oxidase (GOx) or glucose dehydrogenase (GDH) were immobilized on bioanode and oxidize glucose while oxygen reduced in biocathode using immobilized laccase or bilirubin oxidase in order to generate sufficient power. Oxygen 108-114 hydroxyacid oxidase 1 Homo sapiens 17-20 25522366-4 2015 For a biosensor with the glucose oxidase (GOx) enzyme in the presence of oxygen, the response of a metallic SWNT-GOx electrode was 2 times larger than that of a semiconducting SWNT-GOx electrode. Oxygen 73-79 hydroxyacid oxidase 1 Homo sapiens 25-40 31973283-1 2015 Benzoxazine-based redox polymers bearing Os complexes are synthesized and used as an immobilization matrix for glucose oxidase (GOx) as a model system for a reagentless biosensor. Oxygen 41-43 hydroxyacid oxidase 1 Homo sapiens 111-126 31973283-1 2015 Benzoxazine-based redox polymers bearing Os complexes are synthesized and used as an immobilization matrix for glucose oxidase (GOx) as a model system for a reagentless biosensor. Oxygen 41-43 hydroxyacid oxidase 1 Homo sapiens 128-131 26257458-2 2015 Oxygen sensitive phosphors with glucose oxidase (GOx) can be used to determine glucose levels indirectly by monitoring oxygen consumption. Oxygen 0-6 hydroxyacid oxidase 1 Homo sapiens 32-47 26257458-2 2015 Oxygen sensitive phosphors with glucose oxidase (GOx) can be used to determine glucose levels indirectly by monitoring oxygen consumption. Oxygen 0-6 hydroxyacid oxidase 1 Homo sapiens 49-52 26257458-2 2015 Oxygen sensitive phosphors with glucose oxidase (GOx) can be used to determine glucose levels indirectly by monitoring oxygen consumption. Oxygen 119-125 hydroxyacid oxidase 1 Homo sapiens 32-47 26257458-2 2015 Oxygen sensitive phosphors with glucose oxidase (GOx) can be used to determine glucose levels indirectly by monitoring oxygen consumption. Oxygen 119-125 hydroxyacid oxidase 1 Homo sapiens 49-52 25934105-2 2015 The biosensor (poly(TTP)/GOx/GCE) showed a pair of redox peaks in 0.1 M phosphate buffer (pH 7.4) solution in the absence of oxygen the co-substrate of GOx. Oxygen 125-131 hydroxyacid oxidase 1 Homo sapiens 25-28 25934105-3 2015 In here, Poly(TTP)/GOx/GCE biosensor acts as the co-substrate instead of oxygen. Oxygen 73-79 hydroxyacid oxidase 1 Homo sapiens 19-22 25943704-4 2015 The cyclic voltammetry of immobilized GOx showed a pair of well-defined redox peaks in O2-free solution, indicating the DET of GOx. Oxygen 87-89 hydroxyacid oxidase 1 Homo sapiens 38-41 25943704-4 2015 The cyclic voltammetry of immobilized GOx showed a pair of well-defined redox peaks in O2-free solution, indicating the DET of GOx. Oxygen 87-89 hydroxyacid oxidase 1 Homo sapiens 127-130 25280342-3 2015 As a certain amount of glucose was added into the detection cell, GOx rapidly catalyzed the oxidation of glucose, coupling with the local generation of H2O2 in the presence of dissolved O2. Oxygen 154-156 hydroxyacid oxidase 1 Homo sapiens 66-69 25522366-4 2015 For a biosensor with the glucose oxidase (GOx) enzyme in the presence of oxygen, the response of a metallic SWNT-GOx electrode was 2 times larger than that of a semiconducting SWNT-GOx electrode. Oxygen 73-79 hydroxyacid oxidase 1 Homo sapiens 42-45 25522366-4 2015 For a biosensor with the glucose oxidase (GOx) enzyme in the presence of oxygen, the response of a metallic SWNT-GOx electrode was 2 times larger than that of a semiconducting SWNT-GOx electrode. Oxygen 73-79 hydroxyacid oxidase 1 Homo sapiens 113-116 25522366-4 2015 For a biosensor with the glucose oxidase (GOx) enzyme in the presence of oxygen, the response of a metallic SWNT-GOx electrode was 2 times larger than that of a semiconducting SWNT-GOx electrode. Oxygen 73-79 hydroxyacid oxidase 1 Homo sapiens 113-116 25522366-5 2015 In contrast, in the absence of oxygen, the response of the semiconducting SWNT-GOx electrode was retained, whereas that of the metallic SWNT-GOx electrode was significantly reduced. Oxygen 31-37 hydroxyacid oxidase 1 Homo sapiens 79-82 24351177-1 2013 BACKGROUND: Partial pressure of oxygen (pO2) in blood samples can affect blood glucose (BG) measurements, particularly in systems that employ the glucose oxidase (GOx) enzyme reaction on test strips. Oxygen 32-38 hydroxyacid oxidase 1 Homo sapiens 146-161 24519466-3 2014 Based on the GOx-mimicking enzyme activity, Au nanoparticles on the surface of the Fe3O4-Au nanocomposites effectively catalyzed the oxidization of glucose in the presence of dissolved O2, accompanied by the production of H2O2. Oxygen 185-187 hydroxyacid oxidase 1 Homo sapiens 13-16 24491761-3 2014 The GOx assembled on the nanoprobe can catalyze glucose to generate H2O2 in the presence of O2 while the ECL reaction occurred in the luminol ECL biosensor. Oxygen 70-72 hydroxyacid oxidase 1 Homo sapiens 4-7 23835222-2 2013 Nevertheless, GOx activity is highly oxygen dependent which can lead to inaccuracies in amperometric beta-D-glucose determinations. Oxygen 37-43 hydroxyacid oxidase 1 Homo sapiens 14-17 23508863-7 2013 Glucose oxidase (GOx), which is a redox enzyme capable of oxidizing glucose as a renewable fuel using oxygen, was immobilized on the CL-CNT composite paper. Oxygen 102-108 hydroxyacid oxidase 1 Homo sapiens 0-15 23508863-7 2013 Glucose oxidase (GOx), which is a redox enzyme capable of oxidizing glucose as a renewable fuel using oxygen, was immobilized on the CL-CNT composite paper. Oxygen 102-108 hydroxyacid oxidase 1 Homo sapiens 17-20 24274759-2 2014 The voltammetric studies showed that, regardless of CHIT matrix, the GOx adsorbed on CNT yielding a pair of surface-confined current peaks at -0.48 V. The anodic peak did not increase in the presence of glucose in an O2-free solution indicating the lack of direct electron transfer (DET) between the enzymatically active GOx and CNT. Oxygen 217-219 hydroxyacid oxidase 1 Homo sapiens 69-72 24121716-0 2013 Hydrogen peroxide produced by glucose oxidase affects the performance of laccase cathodes in glucose/oxygen fuel cells: FAD-dependent glucose dehydrogenase as a replacement. Oxygen 101-107 hydroxyacid oxidase 1 Homo sapiens 30-45 24121716-3 2013 Experiments focused on determining the effect of the side reaction of GOx between its natural electron acceptor O2 (consumed) and hydrogen peroxide (produced) in the electrolyte. Oxygen 112-114 hydroxyacid oxidase 1 Homo sapiens 70-73 24121716-4 2013 Firstly, oxygen consumption was investigated by both GOx and FAD-GDH in the presence of substrate. Oxygen 9-15 hydroxyacid oxidase 1 Homo sapiens 53-56 24121716-6 2013 O2 consumption was observed with immobilized GOx only, whilst O2 concentration remained stable for the FAD-GDH. Oxygen 0-2 hydroxyacid oxidase 1 Homo sapiens 45-48 24121716-10 2013 24 h stability experiments suggest that the use of O2-insensitive FAD-GDH as to obviate in situ peroxide production by GOx is effective. Oxygen 51-53 hydroxyacid oxidase 1 Homo sapiens 119-122 24351177-1 2013 BACKGROUND: Partial pressure of oxygen (pO2) in blood samples can affect blood glucose (BG) measurements, particularly in systems that employ the glucose oxidase (GOx) enzyme reaction on test strips. Oxygen 32-38 hydroxyacid oxidase 1 Homo sapiens 163-166 24351177-3 2013 Two of the GOx systems are labeled by the manufacturers to be sensitive to increased blood oxygen content, while the other three GOx systems are not. Oxygen 91-97 hydroxyacid oxidase 1 Homo sapiens 11-14 22200380-0 2012 A comparison of glucose oxidase and aldose dehydrogenase as mediated anodes in printed glucose/oxygen enzymatic fuel cells using ABTS/laccase cathodes. Oxygen 95-101 hydroxyacid oxidase 1 Homo sapiens 16-31 24032474-6 2013 Introduction of apo-GOx, instead of GOx, can avoid the consumption of O2 and production of H2O2 during the interaction with glucose, which may exert effects on normal physiological events in living cells and even lead to cellular damage. Oxygen 70-72 hydroxyacid oxidase 1 Homo sapiens 20-23 23663141-6 2013 The reaction between reduced GOx and Ru(NH3)6(3+) is rapid even in air-saturated Tris buffer, where the faster competitive reaction between reduced GOx and dissolved oxygen also occurs. Oxygen 166-172 hydroxyacid oxidase 1 Homo sapiens 29-32 23663141-6 2013 The reaction between reduced GOx and Ru(NH3)6(3+) is rapid even in air-saturated Tris buffer, where the faster competitive reaction between reduced GOx and dissolved oxygen also occurs. Oxygen 166-172 hydroxyacid oxidase 1 Homo sapiens 148-151 23289639-5 2013 However, efficient mediated electron transfer (MET) occurs if an appropriate electron mediator is placed in solution, or the natural electron mediator oxygen is used, indicating that GOx is adsorbed and active on CNT/N-CNT electrodes. Oxygen 151-157 hydroxyacid oxidase 1 Homo sapiens 183-186 21728233-2 2011 For the GOx assay, the postulated fluorescence mechanism is based on the consumption of glucose by dissolved oxygen and GOx in the microwell plates covered with the PSU-Py membrane. Oxygen 109-115 hydroxyacid oxidase 1 Homo sapiens 8-11 22634106-1 2012 An online immobilized glucose oxidase (GOx) capillary microreactor was developed based on an enzymatic redox reaction with 1,4-benzoquinone as an acceptor of electrons, replacing the molecular oxygen typically used in a GOx reaction to achieve direct ultraviolet detection without derivation. Oxygen 193-199 hydroxyacid oxidase 1 Homo sapiens 22-37 22634106-1 2012 An online immobilized glucose oxidase (GOx) capillary microreactor was developed based on an enzymatic redox reaction with 1,4-benzoquinone as an acceptor of electrons, replacing the molecular oxygen typically used in a GOx reaction to achieve direct ultraviolet detection without derivation. Oxygen 193-199 hydroxyacid oxidase 1 Homo sapiens 39-42 22846293-2 2012 In this study, the GOX/CAT system was used to independently provide and control the amount of H2O2 and oxygen in cell culture. Oxygen 103-109 hydroxyacid oxidase 1 Homo sapiens 19-22 25214132-2 2011 Electrochemical measurements were carried out by following the consumed oxygen due to the enzymatic reaction of glucose oxidase (GOx) at -0.7V vs Ag/AgCl. Oxygen 72-78 hydroxyacid oxidase 1 Homo sapiens 112-127 25214132-2 2011 Electrochemical measurements were carried out by following the consumed oxygen due to the enzymatic reaction of glucose oxidase (GOx) at -0.7V vs Ag/AgCl. Oxygen 72-78 hydroxyacid oxidase 1 Homo sapiens 129-132 21568312-1 2011 A single basic residue above the si-face of the flavin ring is the site of oxygen activation in glucose oxidase (GOX) (His516) and monomeric sarcosine oxidase (MSOX) (Lys265). Oxygen 75-81 hydroxyacid oxidase 1 Homo sapiens 96-111 21568312-1 2011 A single basic residue above the si-face of the flavin ring is the site of oxygen activation in glucose oxidase (GOX) (His516) and monomeric sarcosine oxidase (MSOX) (Lys265). Oxygen 75-81 hydroxyacid oxidase 1 Homo sapiens 113-116 21568312-5 2011 The protonated form of His516 is required for tight binding of chloride to oxidized GOX and for rapid reaction of reduced GOX with oxygen. Oxygen 131-137 hydroxyacid oxidase 1 Homo sapiens 84-87 21568312-5 2011 The protonated form of His516 is required for tight binding of chloride to oxidized GOX and for rapid reaction of reduced GOX with oxygen. Oxygen 131-137 hydroxyacid oxidase 1 Homo sapiens 122-125 20541640-5 2010 When ferrocene monocarboxylic acid (FMCA) was introduced as diffusional electron mediator, the current responses toward glucose of the Nafion/GOx/SWCNT electrodes in glucose solution containing FMCA were dramatically improved, and the developed sensor was independent of oxygen. Oxygen 271-277 hydroxyacid oxidase 1 Homo sapiens 142-145 20605749-3 2010 As well as some parameters important in the optimization studies such as optimum pH, enzyme loading and AuNP amount, the analytical characteristics of the biosensor (AuNP/GOx) were examined by the monitoring of chronoamperometric response due to the oxygen consumption through the enzymatic reaction at -0.7 V under optimized conditions at sodium acetate buffer (50 mM, pH 4.0) and the linear graph was obtained in the range of 0.1-1.0 mM glucose. Oxygen 250-256 hydroxyacid oxidase 1 Homo sapiens 171-174 20586415-1 2010 Enzyme-mediated redox chain initiation involving glucose oxidase (GOX) was employed in an iterative solution dip-coating technique to polymerize multiple, three-dimensional hydrogel layers using mild aqueous conditions at ambient temperature and oxygen levels. Oxygen 246-252 hydroxyacid oxidase 1 Homo sapiens 49-64 20586415-1 2010 Enzyme-mediated redox chain initiation involving glucose oxidase (GOX) was employed in an iterative solution dip-coating technique to polymerize multiple, three-dimensional hydrogel layers using mild aqueous conditions at ambient temperature and oxygen levels. Oxygen 246-252 hydroxyacid oxidase 1 Homo sapiens 66-69 18792902-5 2008 The produced O2 can further participate in the catalyzed reaction of GOx, forming a cyclic electron-transfer mechanism of glucose oxidation, which is favorable for the whole reaction system. Oxygen 13-15 hydroxyacid oxidase 1 Homo sapiens 69-72 17935968-4 2008 To facilitate the electrochemical communication between the CNT layer and GOx, CNT was treated with nitrogen or oxygen plasma. Oxygen 112-118 hydroxyacid oxidase 1 Homo sapiens 74-77 19745547-2 2009 To fabricate a GOx layer by applying cross-linking chemistries, the PDMS layer was treated with oxygen plasma to replace silane groups with silanol groups. Oxygen 96-102 hydroxyacid oxidase 1 Homo sapiens 15-18 16430853-4 2006 Using GOx as a model enzyme, the assembled multilayer membranes showed some striking features such as the adsorbed form of GOx on individual MWCNT, uniformity, good stability, and electrocatalytic activity toward oxygen reduction. Oxygen 213-219 hydroxyacid oxidase 1 Homo sapiens 6-9 17321126-6 2007 A linear decrease of the reduction current of oxygen at the {GOx/CNT}-modified electrodes with the addition of glucose suggests that such multilayer films of GOx retain the bioactivity and can be used as reagentless glucose biosensors. Oxygen 46-52 hydroxyacid oxidase 1 Homo sapiens 61-64 17321126-6 2007 A linear decrease of the reduction current of oxygen at the {GOx/CNT}-modified electrodes with the addition of glucose suggests that such multilayer films of GOx retain the bioactivity and can be used as reagentless glucose biosensors. Oxygen 46-52 hydroxyacid oxidase 1 Homo sapiens 158-161 19071317-4 2007 In the presence of oxygen, GOx converts glucose to gluconic acid and hydrogen peroxide (H(2)O(2)). Oxygen 19-25 hydroxyacid oxidase 1 Homo sapiens 27-30 16430853-4 2006 Using GOx as a model enzyme, the assembled multilayer membranes showed some striking features such as the adsorbed form of GOx on individual MWCNT, uniformity, good stability, and electrocatalytic activity toward oxygen reduction. Oxygen 213-219 hydroxyacid oxidase 1 Homo sapiens 123-126 16430853-5 2006 Based on the consumption of dissolved oxygen during the oxidation process of glucose catalyzed by the immobilized GOx, a sensitive amperometric biosensor was developed for the detection of glucose up to 5.0 mM with a detection limit of 58 microM. Oxygen 38-44 hydroxyacid oxidase 1 Homo sapiens 114-117 15970532-5 2005 An intramolecular electron transfer rate constant of 1.0x10(5) s(-1) was obtained for the activated GOx, compared with the rate constant of 7.0x10(2) s(-1) of the natural GOx-oxygen system, making this an amenable system for biosensor applications. Oxygen 175-181 hydroxyacid oxidase 1 Homo sapiens 100-103 15970532-5 2005 An intramolecular electron transfer rate constant of 1.0x10(5) s(-1) was obtained for the activated GOx, compared with the rate constant of 7.0x10(2) s(-1) of the natural GOx-oxygen system, making this an amenable system for biosensor applications. Oxygen 175-181 hydroxyacid oxidase 1 Homo sapiens 171-174 15649080-7 2005 Even though the atmosphere over the drop was O2 at 1 atm pressure, the wired BOD disk scavenged the O2 so effectively that the glucose-reduced FADH2 of GOx was not oxidized by O2, the natural cosubstrate of the enzyme. Oxygen 45-47 hydroxyacid oxidase 1 Homo sapiens 152-155 15649080-7 2005 Even though the atmosphere over the drop was O2 at 1 atm pressure, the wired BOD disk scavenged the O2 so effectively that the glucose-reduced FADH2 of GOx was not oxidized by O2, the natural cosubstrate of the enzyme. Oxygen 100-102 hydroxyacid oxidase 1 Homo sapiens 152-155 15649080-7 2005 Even though the atmosphere over the drop was O2 at 1 atm pressure, the wired BOD disk scavenged the O2 so effectively that the glucose-reduced FADH2 of GOx was not oxidized by O2, the natural cosubstrate of the enzyme. Oxygen 100-102 hydroxyacid oxidase 1 Homo sapiens 152-155 10565290-1 1999 The response of first-generation glucose oxidase (GOx) amperometric glucose biosensors is strongly dependent on the concentration of the oxygen cosubstrate. Oxygen 137-143 hydroxyacid oxidase 1 Homo sapiens 33-48 10565290-1 1999 The response of first-generation glucose oxidase (GOx) amperometric glucose biosensors is strongly dependent on the concentration of the oxygen cosubstrate. Oxygen 137-143 hydroxyacid oxidase 1 Homo sapiens 50-53 10565290-2 1999 The incorporation of the natural oxygen binder myoglobin into a GOx-containing carbon-paste matrix is shown to satisfy the oxygen demand of the enzymatic reaction and to provide convenient biosensing of glucose in oxygen-free solutions. Oxygen 33-39 hydroxyacid oxidase 1 Homo sapiens 64-67 10565290-2 1999 The incorporation of the natural oxygen binder myoglobin into a GOx-containing carbon-paste matrix is shown to satisfy the oxygen demand of the enzymatic reaction and to provide convenient biosensing of glucose in oxygen-free solutions. Oxygen 123-129 hydroxyacid oxidase 1 Homo sapiens 64-67 10565290-2 1999 The incorporation of the natural oxygen binder myoglobin into a GOx-containing carbon-paste matrix is shown to satisfy the oxygen demand of the enzymatic reaction and to provide convenient biosensing of glucose in oxygen-free solutions. Oxygen 123-129 hydroxyacid oxidase 1 Homo sapiens 64-67 1660188-4 1991 Gox was purified and shown to augment the rate of O2- production in a cell-free oxidase activation system. Oxygen 50-52 hydroxyacid oxidase 1 Homo sapiens 0-3 15875368-3 2004 Here we sought to explore generation of the oxidative environment and induction of polymersome destabilization through production of hydrogen peroxide by the glucose-oxidase (GOx)/glucose/oxygen system. Oxygen 188-194 hydroxyacid oxidase 1 Homo sapiens 158-173 15875368-3 2004 Here we sought to explore generation of the oxidative environment and induction of polymersome destabilization through production of hydrogen peroxide by the glucose-oxidase (GOx)/glucose/oxygen system. Oxygen 188-194 hydroxyacid oxidase 1 Homo sapiens 175-178