PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 32029222-7 2020 RESULTS: We demonstrate that the "immunometabolite" itaconate slowed tricarboxylic acid (TCA) cycle metabolism and buffered redox imbalance via succinate dehydrogenase (SDH) inhibition and induction of anti-oxidative stress response in primary cultures of astrocytes and neurons. itaconic acid 52-61 aminoadipate-semialdehyde synthase Mus musculus 144-167 32046101-13 2020 However, inhibition of SDH can lead to the accumulation of succinate, an important signaling molecule associated with inflammation, fibrosis, and carcinogenesis. Succinic Acid 59-68 aminoadipate-semialdehyde synthase Mus musculus 23-26 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). Tricarboxylic Acids 68-71 aminoadipate-semialdehyde synthase Mus musculus 215-238 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). Tricarboxylic Acids 68-71 aminoadipate-semialdehyde synthase Mus musculus 240-243 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). citrate 83-90 aminoadipate-semialdehyde synthase Mus musculus 215-238 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). citrate 83-90 aminoadipate-semialdehyde synthase Mus musculus 240-243 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). alpha-methylaconitate 99-112 aminoadipate-semialdehyde synthase Mus musculus 215-238 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). itaconic acid 116-125 aminoadipate-semialdehyde synthase Mus musculus 215-238 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). itaconic acid 116-125 aminoadipate-semialdehyde synthase Mus musculus 240-243 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). Tricarboxylic Acids 187-190 aminoadipate-semialdehyde synthase Mus musculus 215-238 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). Tricarboxylic Acids 187-190 aminoadipate-semialdehyde synthase Mus musculus 240-243 31894617-3 2020 The transition from immune resistance to tolerance also diverts the TCA cycle from citrate-derived cis-aconitate to itaconate, a recently discovered catabolic mediator that separates the TCA cycle at isocitrate and succinate dehydrogenase (SDH). Isocitrates 200-210 aminoadipate-semialdehyde synthase Mus musculus 240-243 31894617-4 2020 Itaconate inhibits succinate dehydrogenase and its anabolic role in mitochondrial ATP generation. itaconic acid 0-9 aminoadipate-semialdehyde synthase Mus musculus 19-42 32029222-7 2020 RESULTS: We demonstrate that the "immunometabolite" itaconate slowed tricarboxylic acid (TCA) cycle metabolism and buffered redox imbalance via succinate dehydrogenase (SDH) inhibition and induction of anti-oxidative stress response in primary cultures of astrocytes and neurons. itaconic acid 52-61 aminoadipate-semialdehyde synthase Mus musculus 169-172 32029222-7 2020 RESULTS: We demonstrate that the "immunometabolite" itaconate slowed tricarboxylic acid (TCA) cycle metabolism and buffered redox imbalance via succinate dehydrogenase (SDH) inhibition and induction of anti-oxidative stress response in primary cultures of astrocytes and neurons. Tricarboxylic Acids 69-87 aminoadipate-semialdehyde synthase Mus musculus 169-172 32029222-7 2020 RESULTS: We demonstrate that the "immunometabolite" itaconate slowed tricarboxylic acid (TCA) cycle metabolism and buffered redox imbalance via succinate dehydrogenase (SDH) inhibition and induction of anti-oxidative stress response in primary cultures of astrocytes and neurons. Tricarboxylic Acids 89-92 aminoadipate-semialdehyde synthase Mus musculus 169-172 32029222-12 2020 CONCLUSIONS: We hypothesize that itaconate transiently inhibits SDH to gradually "awaken" mitochondrial function upon reperfusion that minimizes ROS and tissue damage. itaconic acid 33-42 aminoadipate-semialdehyde synthase Mus musculus 64-67 32879254-6 2020 It was found that the heart rate and SDH activity in serum of mice gradually decreased with the increase of TMT dose compared with the control group. trimethyltin chloride 108-111 aminoadipate-semialdehyde synthase Mus musculus 37-40 30573525-3 2019 In Caenorhbditis elegans, mutations in the saccharopine dehydrogenase (SDH) domain of the bi-functional enzyme alpha-aminoadipic semialdehyde synthase AASS-1 greatly elevate the lysine catabolic intermediate saccharopine, which causes mitochondrial damage by disrupting mitochondrial dynamics, leading to reduced adult animal growth. Lysine 178-184 aminoadipate-semialdehyde synthase Mus musculus 43-69 31313401-9 2019 YF476-treated mouse pancreas showed downregulation of Riks, Zpbp, Ntf3, Lrrn4, Aass, Skint3, Kcnb1, Dgkb, Ddx60, and Aspn gene expressions compared with untreated mouse pancreas. YF 476 0-5 aminoadipate-semialdehyde synthase Mus musculus 79-83 30794944-5 2019 Intriguingly, PDH, KGDH, and SDH comprised up to ~95% of the ROS generating capacity of permeabilized 6N liver mitochondria, with PRODH, G3PDH, and BCKDH making minor contributions. ros 61-64 aminoadipate-semialdehyde synthase Mus musculus 29-32 30573525-3 2019 In Caenorhbditis elegans, mutations in the saccharopine dehydrogenase (SDH) domain of the bi-functional enzyme alpha-aminoadipic semialdehyde synthase AASS-1 greatly elevate the lysine catabolic intermediate saccharopine, which causes mitochondrial damage by disrupting mitochondrial dynamics, leading to reduced adult animal growth. Lysine 178-184 aminoadipate-semialdehyde synthase Mus musculus 71-74 30573525-3 2019 In Caenorhbditis elegans, mutations in the saccharopine dehydrogenase (SDH) domain of the bi-functional enzyme alpha-aminoadipic semialdehyde synthase AASS-1 greatly elevate the lysine catabolic intermediate saccharopine, which causes mitochondrial damage by disrupting mitochondrial dynamics, leading to reduced adult animal growth. saccharopine 43-55 aminoadipate-semialdehyde synthase Mus musculus 71-74 30573525-5 2019 Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis. saccharopine 72-84 aminoadipate-semialdehyde synthase Mus musculus 147-150 30573525-5 2019 Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis. Lysine 96-102 aminoadipate-semialdehyde synthase Mus musculus 147-150 30573525-5 2019 Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis. Ketoglutaric Acids 107-126 aminoadipate-semialdehyde synthase Mus musculus 147-150 30573525-5 2019 Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis. saccharopine 168-180 aminoadipate-semialdehyde synthase Mus musculus 147-150 30573525-5 2019 Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis. saccharopine 168-180 aminoadipate-semialdehyde synthase Mus musculus 147-150 29746885-5 2018 RESULTS: Oral administration of curcumin and metformin combated mitochondrial fatty acid oxidation and reduced hepatic succinate accumulation due to the inhibition of succinate dehydrogenase (SDH) activity and demonstrated inhibitory effect on hepatic fibrosis. Curcumin 32-40 aminoadipate-semialdehyde synthase Mus musculus 167-190 30299210-0 2019 Application of a novel nanoemulsion adjuvant for rabies vaccine which stabilizes a Krebs cycle intermediate (SDH) in an animal model. krebs 83-88 aminoadipate-semialdehyde synthase Mus musculus 109-112 30299210-3 2019 In this study, we focused on the role of a Krebs cycle intermediate, succinate dehydrogenase (SDH), in the innate immune response to cytokine production. krebs 43-48 aminoadipate-semialdehyde synthase Mus musculus 69-92 30299210-3 2019 In this study, we focused on the role of a Krebs cycle intermediate, succinate dehydrogenase (SDH), in the innate immune response to cytokine production. krebs 43-48 aminoadipate-semialdehyde synthase Mus musculus 94-97 30159755-1 2018 Pheochromocytomas and paragangliomas (PGLs) due to mutations of succinate dehydrogenase (SDH) B, a subunit of the SDH complex with a role in the Krebs cycle and the respiratory chain, tend to be larger at diagnosis and more prone to metastatic disease than other tumors. krebs 145-150 aminoadipate-semialdehyde synthase Mus musculus 89-92 30159755-6 2018 Sdhb-silenced cells showed functional impairment of SDH with elevated succinate to fumarate ratio and decreased oxidative capacity. Succinic Acid 70-79 aminoadipate-semialdehyde synthase Mus musculus 52-55 30644349-9 2019 Further, in mitochondria, PQ-induced decrease in succinate dehydrogenase (SDH) activity and energy charge (MTT reduction), was restored with BM supplementation. Paraquat 26-28 aminoadipate-semialdehyde synthase Mus musculus 49-72 30644349-9 2019 Further, in mitochondria, PQ-induced decrease in succinate dehydrogenase (SDH) activity and energy charge (MTT reduction), was restored with BM supplementation. Paraquat 26-28 aminoadipate-semialdehyde synthase Mus musculus 74-77 30644349-9 2019 Further, in mitochondria, PQ-induced decrease in succinate dehydrogenase (SDH) activity and energy charge (MTT reduction), was restored with BM supplementation. BM 141-143 aminoadipate-semialdehyde synthase Mus musculus 49-72 30644349-9 2019 Further, in mitochondria, PQ-induced decrease in succinate dehydrogenase (SDH) activity and energy charge (MTT reduction), was restored with BM supplementation. BM 141-143 aminoadipate-semialdehyde synthase Mus musculus 74-77 29746885-5 2018 RESULTS: Oral administration of curcumin and metformin combated mitochondrial fatty acid oxidation and reduced hepatic succinate accumulation due to the inhibition of succinate dehydrogenase (SDH) activity and demonstrated inhibitory effect on hepatic fibrosis. Curcumin 32-40 aminoadipate-semialdehyde synthase Mus musculus 192-195 29746885-5 2018 RESULTS: Oral administration of curcumin and metformin combated mitochondrial fatty acid oxidation and reduced hepatic succinate accumulation due to the inhibition of succinate dehydrogenase (SDH) activity and demonstrated inhibitory effect on hepatic fibrosis. Metformin 45-54 aminoadipate-semialdehyde synthase Mus musculus 167-190 29746885-5 2018 RESULTS: Oral administration of curcumin and metformin combated mitochondrial fatty acid oxidation and reduced hepatic succinate accumulation due to the inhibition of succinate dehydrogenase (SDH) activity and demonstrated inhibitory effect on hepatic fibrosis. Metformin 45-54 aminoadipate-semialdehyde synthase Mus musculus 192-195 26912655-3 2016 Moreover, SIRT3 is a key regulator of succinate dehydrogenase (SDH), which catalyzes the oxidation of succinate to fumarate. Succinic Acid 38-47 aminoadipate-semialdehyde synthase Mus musculus 63-66 29464059-2 2018 SDH loss leads to accumulation of intracellular succinate, which competitively inhibits dioxygenase enzymes, causing activation of pseudohypoxic signaling and hypermethylation of histones and DNA. Succinic Acid 48-57 aminoadipate-semialdehyde synthase Mus musculus 0-3 28928232-7 2017 The stem-like characteristics are reversed by alpha-ketoglutarate, suggesting that SDH-associated tumorigenesis results from dedifferentiation driven by an imbalance in cellular metabolites of the TCA cycle. Ketoglutaric Acids 46-65 aminoadipate-semialdehyde synthase Mus musculus 83-86 28634116-3 2017 In neurons, oxygen-glucose deprivation induced succinate accumulation due to the reversal of succinate dehydrogenase (SDH) activation, leading to mitochondrial fission. Succinic Acid 47-56 aminoadipate-semialdehyde synthase Mus musculus 93-116 28634116-3 2017 In neurons, oxygen-glucose deprivation induced succinate accumulation due to the reversal of succinate dehydrogenase (SDH) activation, leading to mitochondrial fission. Succinic Acid 47-56 aminoadipate-semialdehyde synthase Mus musculus 118-121 27667687-3 2016 We show that increased mitochondrial oxidation of succinate via succinate dehydrogenase (SDH) and an elevation of mitochondrial membrane potential combine to drive mitochondrial reactive oxygen species (ROS) production. Succinic Acid 50-59 aminoadipate-semialdehyde synthase Mus musculus 64-87 27667687-3 2016 We show that increased mitochondrial oxidation of succinate via succinate dehydrogenase (SDH) and an elevation of mitochondrial membrane potential combine to drive mitochondrial reactive oxygen species (ROS) production. Succinic Acid 50-59 aminoadipate-semialdehyde synthase Mus musculus 89-92 27667687-3 2016 We show that increased mitochondrial oxidation of succinate via succinate dehydrogenase (SDH) and an elevation of mitochondrial membrane potential combine to drive mitochondrial reactive oxygen species (ROS) production. Reactive Oxygen Species 178-201 aminoadipate-semialdehyde synthase Mus musculus 64-87 27667687-3 2016 We show that increased mitochondrial oxidation of succinate via succinate dehydrogenase (SDH) and an elevation of mitochondrial membrane potential combine to drive mitochondrial reactive oxygen species (ROS) production. Reactive Oxygen Species 178-201 aminoadipate-semialdehyde synthase Mus musculus 89-92 27667687-3 2016 We show that increased mitochondrial oxidation of succinate via succinate dehydrogenase (SDH) and an elevation of mitochondrial membrane potential combine to drive mitochondrial reactive oxygen species (ROS) production. Reactive Oxygen Species 203-206 aminoadipate-semialdehyde synthase Mus musculus 64-87 27667687-3 2016 We show that increased mitochondrial oxidation of succinate via succinate dehydrogenase (SDH) and an elevation of mitochondrial membrane potential combine to drive mitochondrial reactive oxygen species (ROS) production. Reactive Oxygen Species 203-206 aminoadipate-semialdehyde synthase Mus musculus 89-92 29402957-0 2018 Selective Inhibition of Succinate Dehydrogenase in Reperfused Myocardium with Intracoronary Malonate Reduces Infarct Size. malonic acid 92-100 aminoadipate-semialdehyde synthase Mus musculus 24-47 29402957-8 2018 In conclusion, inhibition of SDH with intracoronary malonate during early reperfusion limits reperfusion injury and infarct size in pigs submitted to transient coronary occlusion without modifying reperfusion arrhythmias or contractile function in distant myocardium. malonic acid 52-60 aminoadipate-semialdehyde synthase Mus musculus 29-32 26912655-3 2016 Moreover, SIRT3 is a key regulator of succinate dehydrogenase (SDH), which catalyzes the oxidation of succinate to fumarate. Fumarates 115-123 aminoadipate-semialdehyde synthase Mus musculus 38-61 26912655-3 2016 Moreover, SIRT3 is a key regulator of succinate dehydrogenase (SDH), which catalyzes the oxidation of succinate to fumarate. Fumarates 115-123 aminoadipate-semialdehyde synthase Mus musculus 63-66 26912655-7 2016 Inhibiting SIRT3 using SIRT3 siRNA exacerbated HSC activation via the SDH-succinate-GPR91 pathway, and SIRT3 overexpression or honokiol treatment attenuated HSC activation in vitro In isolated liver and HSCs from methionine- and choline-deficient (MCD) diet-induced NAFLD, the expression of SIRT3 and SDH activity was decreased, and the succinate concentrations and GPR91 expression were increased. Succinic Acid 74-83 aminoadipate-semialdehyde synthase Mus musculus 70-73 26912655-7 2016 Inhibiting SIRT3 using SIRT3 siRNA exacerbated HSC activation via the SDH-succinate-GPR91 pathway, and SIRT3 overexpression or honokiol treatment attenuated HSC activation in vitro In isolated liver and HSCs from methionine- and choline-deficient (MCD) diet-induced NAFLD, the expression of SIRT3 and SDH activity was decreased, and the succinate concentrations and GPR91 expression were increased. honokiol 127-135 aminoadipate-semialdehyde synthase Mus musculus 301-304 26388266-14 2015 We further demonstrate that I/R injury in Sirt5(-/-) heart is restored to WT levels by pretreatment with dimethyl malonate, a competitive inhibitor of succinate dehydrogenase (SDH), implicating alteration in SDH activity as causative of the injury. methyl malonate 105-122 aminoadipate-semialdehyde synthase Mus musculus 151-174 26388266-14 2015 We further demonstrate that I/R injury in Sirt5(-/-) heart is restored to WT levels by pretreatment with dimethyl malonate, a competitive inhibitor of succinate dehydrogenase (SDH), implicating alteration in SDH activity as causative of the injury. methyl malonate 105-122 aminoadipate-semialdehyde synthase Mus musculus 176-179 26388266-14 2015 We further demonstrate that I/R injury in Sirt5(-/-) heart is restored to WT levels by pretreatment with dimethyl malonate, a competitive inhibitor of succinate dehydrogenase (SDH), implicating alteration in SDH activity as causative of the injury. methyl malonate 105-122 aminoadipate-semialdehyde synthase Mus musculus 208-211 26302408-1 2015 Succinate dehydrogenase (SDH) is a heterotetrameric nuclear-encoded complex responsible for the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Tricarboxylic Acids 138-156 aminoadipate-semialdehyde synthase Mus musculus 25-28 26302408-5 2015 We found that lack of SDH activity commits cells to consume extracellular pyruvate, which sustains Warburg-like bioenergetic features. Pyruvic Acid 74-82 aminoadipate-semialdehyde synthase Mus musculus 22-25 26302408-1 2015 Succinate dehydrogenase (SDH) is a heterotetrameric nuclear-encoded complex responsible for the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Succinic Acid 109-118 aminoadipate-semialdehyde synthase Mus musculus 0-23 26302408-1 2015 Succinate dehydrogenase (SDH) is a heterotetrameric nuclear-encoded complex responsible for the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Succinic Acid 109-118 aminoadipate-semialdehyde synthase Mus musculus 25-28 26051274-6 2015 Malonate, an inhibitor of succinate dehydrogenase (SDH), increased succinate levels in cultured HSCs and increased GPR91 and alpha-SMA expression. malonic acid 0-8 aminoadipate-semialdehyde synthase Mus musculus 26-49 26302408-1 2015 Succinate dehydrogenase (SDH) is a heterotetrameric nuclear-encoded complex responsible for the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Fumarates 122-130 aminoadipate-semialdehyde synthase Mus musculus 0-23 26302408-1 2015 Succinate dehydrogenase (SDH) is a heterotetrameric nuclear-encoded complex responsible for the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Fumarates 122-130 aminoadipate-semialdehyde synthase Mus musculus 25-28 26302408-1 2015 Succinate dehydrogenase (SDH) is a heterotetrameric nuclear-encoded complex responsible for the oxidation of succinate to fumarate in the tricarboxylic acid cycle. Tricarboxylic Acids 138-156 aminoadipate-semialdehyde synthase Mus musculus 0-23 26051274-6 2015 Malonate, an inhibitor of succinate dehydrogenase (SDH), increased succinate levels in cultured HSCs and increased GPR91 and alpha-SMA expression. malonic acid 0-8 aminoadipate-semialdehyde synthase Mus musculus 51-54 26051274-6 2015 Malonate, an inhibitor of succinate dehydrogenase (SDH), increased succinate levels in cultured HSCs and increased GPR91 and alpha-SMA expression. Succinic Acid 26-35 aminoadipate-semialdehyde synthase Mus musculus 51-54 25671108-0 2014 Succinate dehydrogenase inhibition leads to epithelial-mesenchymal transition and reprogrammed carbon metabolism. Carbon 95-101 aminoadipate-semialdehyde synthase Mus musculus 0-23 25874444-0 2015 Mitochondrial succinate dehydrogenase is involved in stimulus-secretion coupling and endogenous ROS formation in murine beta cells. Reactive Oxygen Species 96-99 aminoadipate-semialdehyde synthase Mus musculus 14-37 25874444-2 2015 Mitochondrial succinate dehydrogenase (SDH) fulfils a dual function with respect to mitochondrial energy supply: (1) the enzyme is part of mitochondrial respiratory chains; and (2) it catalyses oxidation of succinate to fumarate in the Krebs cycle. Succinic Acid 14-23 aminoadipate-semialdehyde synthase Mus musculus 39-42 25874444-2 2015 Mitochondrial succinate dehydrogenase (SDH) fulfils a dual function with respect to mitochondrial energy supply: (1) the enzyme is part of mitochondrial respiratory chains; and (2) it catalyses oxidation of succinate to fumarate in the Krebs cycle. Fumarates 220-228 aminoadipate-semialdehyde synthase Mus musculus 14-37 25874444-2 2015 Mitochondrial succinate dehydrogenase (SDH) fulfils a dual function with respect to mitochondrial energy supply: (1) the enzyme is part of mitochondrial respiratory chains; and (2) it catalyses oxidation of succinate to fumarate in the Krebs cycle. Fumarates 220-228 aminoadipate-semialdehyde synthase Mus musculus 39-42 25874444-2 2015 Mitochondrial succinate dehydrogenase (SDH) fulfils a dual function with respect to mitochondrial energy supply: (1) the enzyme is part of mitochondrial respiratory chains; and (2) it catalyses oxidation of succinate to fumarate in the Krebs cycle. krebs 236-241 aminoadipate-semialdehyde synthase Mus musculus 14-37 25874444-2 2015 Mitochondrial succinate dehydrogenase (SDH) fulfils a dual function with respect to mitochondrial energy supply: (1) the enzyme is part of mitochondrial respiratory chains; and (2) it catalyses oxidation of succinate to fumarate in the Krebs cycle. krebs 236-241 aminoadipate-semialdehyde synthase Mus musculus 39-42 25874444-5 2015 RESULTS: Inhibition of SDH with 3-nitropropionic acid (3-NPA) or monoethyl fumarate (MEF) reduced glucose-stimulated insulin secretion. 3-nitropropionic acid 32-53 aminoadipate-semialdehyde synthase Mus musculus 23-26 25874444-5 2015 RESULTS: Inhibition of SDH with 3-nitropropionic acid (3-NPA) or monoethyl fumarate (MEF) reduced glucose-stimulated insulin secretion. 3-nitropropionic acid 55-60 aminoadipate-semialdehyde synthase Mus musculus 23-26 25874444-5 2015 RESULTS: Inhibition of SDH with 3-nitropropionic acid (3-NPA) or monoethyl fumarate (MEF) reduced glucose-stimulated insulin secretion. Glucose 98-105 aminoadipate-semialdehyde synthase Mus musculus 23-26 25874444-7 2015 Blocking SDH decreased glucose-stimulated increase in intracellular FADH2 concentration without alterations in NAD(P)H. Glucose 23-30 aminoadipate-semialdehyde synthase Mus musculus 9-12 25874444-11 2015 CONCLUSIONS/INTERPRETATION: SDH is an important regulator of insulin secretion and ROS production. Reactive Oxygen Species 83-86 aminoadipate-semialdehyde synthase Mus musculus 28-31 25943561-4 2015 While training alone increased the exhaustive running performance, GW501516 treatment enhanced running endurance and the proportion of succinate dehydrogenase (SDH)-positive muscle fibres in both trained and untrained mice. GW 501516 67-75 aminoadipate-semialdehyde synthase Mus musculus 135-158 25943561-4 2015 While training alone increased the exhaustive running performance, GW501516 treatment enhanced running endurance and the proportion of succinate dehydrogenase (SDH)-positive muscle fibres in both trained and untrained mice. GW 501516 67-75 aminoadipate-semialdehyde synthase Mus musculus 160-163 25671108-1 2014 BACKGROUND: Succinate dehydrogenase (SDH) is a mitochondrial metabolic enzyme complex involved in both the electron transport chain and the citric acid cycle. Citric Acid 140-151 aminoadipate-semialdehyde synthase Mus musculus 12-35 25671108-1 2014 BACKGROUND: Succinate dehydrogenase (SDH) is a mitochondrial metabolic enzyme complex involved in both the electron transport chain and the citric acid cycle. Citric Acid 140-151 aminoadipate-semialdehyde synthase Mus musculus 37-40 24846270-4 2014 Our aim was to establish whether MAPK signaling may also play a role in aggressive, succinate dehydrogenase (SDH) B mutation-derived PHEOs/PGLs. pheos 133-138 aminoadipate-semialdehyde synthase Mus musculus 84-107 24846270-4 2014 Our aim was to establish whether MAPK signaling may also play a role in aggressive, succinate dehydrogenase (SDH) B mutation-derived PHEOs/PGLs. pheos 133-138 aminoadipate-semialdehyde synthase Mus musculus 109-112 24377586-7 2014 Mitochondrial enzymes such as isocitrate dehydrogenase (ICDH), alpha-keto dehydrogenase (alpha-KDH), succinate dehydrogenase (SDH) and the activities of respiratory chain enzymes NADH dehydrogenase and cytochrome c oxidase were found to be elevated in AOM-treated animals. Azoxymethane 252-255 aminoadipate-semialdehyde synthase Mus musculus 126-129 22211279-5 2013 Cisplatin treatment decreased the succinate dehydrogenase (SDH) activity in the mitochondria of kidney and DL cells and combination treatment caused further decrease in SDH activity in kidney and DL cells during 24-48 h of treatment. Cisplatin 0-9 aminoadipate-semialdehyde synthase Mus musculus 34-57 25638378-10 2014 RESULTS: IFN-gamma enhanced concentration of SDH-produced formazan by macrophages (not by splenocytes) by approximately 50%. Formazans 58-66 aminoadipate-semialdehyde synthase Mus musculus 45-48 25638378-13 2014 While pyrimidines with NO-inhibitory properties suppressed the IFN-gamma-enhanced levels of SDH-produced formazan, they did not change the LDH-dependent formazan production. Pyrimidines 6-17 aminoadipate-semialdehyde synthase Mus musculus 92-95 25638378-13 2014 While pyrimidines with NO-inhibitory properties suppressed the IFN-gamma-enhanced levels of SDH-produced formazan, they did not change the LDH-dependent formazan production. Formazans 105-113 aminoadipate-semialdehyde synthase Mus musculus 92-95 25638378-14 2014 CONCLUSION: IFN-gamma augments the SDH-produced formazan by macrophages. Formazans 48-56 aminoadipate-semialdehyde synthase Mus musculus 35-38 22211279-5 2013 Cisplatin treatment decreased the succinate dehydrogenase (SDH) activity in the mitochondria of kidney and DL cells and combination treatment caused further decrease in SDH activity in kidney and DL cells during 24-48 h of treatment. Cisplatin 0-9 aminoadipate-semialdehyde synthase Mus musculus 59-62 22211279-5 2013 Cisplatin treatment decreased the succinate dehydrogenase (SDH) activity in the mitochondria of kidney and DL cells and combination treatment caused further decrease in SDH activity in kidney and DL cells during 24-48 h of treatment. Cisplatin 0-9 aminoadipate-semialdehyde synthase Mus musculus 169-172 20734097-6 2011 3-NP-treated mice displayed changes in alkaline phosphatase (APase), succinic dehydrogenase (SDH), and cytochrome c oxidase (COX) levels in the gracilis and gastrocnemius muscles. 3-nitropropionic acid 0-4 aminoadipate-semialdehyde synthase Mus musculus 69-91 22465782-5 2012 Although no differences were observed in the configuration or number of TM-3 cell mitochondria following DHEA treatment, mitochondrial membrane permeability and the activity of succinate dehydrogenase (SDH) increased subsequent to 24h treatment of cells with 100 muM DHEA. Dehydroepiandrosterone 267-271 aminoadipate-semialdehyde synthase Mus musculus 177-200 22465782-5 2012 Although no differences were observed in the configuration or number of TM-3 cell mitochondria following DHEA treatment, mitochondrial membrane permeability and the activity of succinate dehydrogenase (SDH) increased subsequent to 24h treatment of cells with 100 muM DHEA. Dehydroepiandrosterone 267-271 aminoadipate-semialdehyde synthase Mus musculus 202-205 22416180-11 2012 At the mitochondrial level, rebamipide increased SDH and ATPase activities, NADH level and decreased mitochondrial swelling. rebamipide 28-38 aminoadipate-semialdehyde synthase Mus musculus 49-52 21628503-8 2011 M1-SDH(HBtail) also displayed unaltered growth patterns, increased intracellular ATP concentration and Hpr double phosphorylation, and significantly reduced pH tolerance, streptolysin S, and SpeB activities. Adenosine Triphosphate 81-84 aminoadipate-semialdehyde synthase Mus musculus 3-6 21441945-11 2011 At the level of the mitochondria, melatonin treatment significantly restored the activities of ATPase and SDH. Melatonin 34-43 aminoadipate-semialdehyde synthase Mus musculus 106-109 23535164-0 2013 Inhibition of Succinate Dehydrogenase by Diazoxide Is Independent of the ATP-Sensitive Potassium Channel Subunit Sulfonylurea Type 1 Receptor. Diazoxide 41-50 aminoadipate-semialdehyde synthase Mus musculus 14-37 23535164-4 2013 Diazoxide may be cardioprotective via inhibition of SDH, which can form part of an ATP-sensitive potassium channel or share its genetic material. Diazoxide 0-9 aminoadipate-semialdehyde synthase Mus musculus 52-55 23535164-5 2013 This study investigated the role of inhibition of SDH by diazoxide and its relationship to the SUR1 subunit. Diazoxide 57-66 aminoadipate-semialdehyde synthase Mus musculus 50-53 23535164-7 2013 Succinate dehydrogenase activity was measured by spectrophotometric analysis of 2,6-dichloroindophenol reduction for 20 minutes as the relative change in absorbance over time. 2,6-Dichloroindophenol 80-102 aminoadipate-semialdehyde synthase Mus musculus 0-23 23535164-9 2013 RESULTS: Both malonate and diazoxide inhibit SDH activity in mitochondria of wild-type mice and in mice lacking the SUR1 subunit (p < 0.05 vs control). malonic acid 14-22 aminoadipate-semialdehyde synthase Mus musculus 45-48 23535164-9 2013 RESULTS: Both malonate and diazoxide inhibit SDH activity in mitochondria of wild-type mice and in mice lacking the SUR1 subunit (p < 0.05 vs control). Diazoxide 27-36 aminoadipate-semialdehyde synthase Mus musculus 45-48 23535164-10 2013 CONCLUSIONS: The ability of DZX to inhibit SDH persists even after deletion of the SUR1 gene. Deoxy-Galacto-Noeurostegine 28-31 aminoadipate-semialdehyde synthase Mus musculus 43-46 23535164-12 2013 The inhibition of SDH by DZX can play a role in the cardioprotection afforded by DZX; however, this role is independent of the ATP-sensitive potassium channel subunit SUR1. Deoxy-Galacto-Noeurostegine 25-28 aminoadipate-semialdehyde synthase Mus musculus 18-21 23535164-12 2013 The inhibition of SDH by DZX can play a role in the cardioprotection afforded by DZX; however, this role is independent of the ATP-sensitive potassium channel subunit SUR1. Deoxy-Galacto-Noeurostegine 81-84 aminoadipate-semialdehyde synthase Mus musculus 18-21 20734097-6 2011 3-NP-treated mice displayed changes in alkaline phosphatase (APase), succinic dehydrogenase (SDH), and cytochrome c oxidase (COX) levels in the gracilis and gastrocnemius muscles. 3-nitropropionic acid 0-4 aminoadipate-semialdehyde synthase Mus musculus 93-96 19956719-1 2009 BACKGROUND: Mitochondrial succinate dehydrogenase (SDH) is a component of both the tricarboxylic acid cycle and the electron transport chain. Tricarboxylic Acids 83-101 aminoadipate-semialdehyde synthase Mus musculus 26-49 20862766-4 2010 Cellular succinate dehydrogenase (SDH) activity was estimated using the MTT method (3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, a yellow tetrazole), and activities were normalized to Teflon controls. monooxyethylene trimethylolpropane tristearate 72-75 aminoadipate-semialdehyde synthase Mus musculus 9-32 20862766-4 2010 Cellular succinate dehydrogenase (SDH) activity was estimated using the MTT method (3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, a yellow tetrazole), and activities were normalized to Teflon controls. monooxyethylene trimethylolpropane tristearate 72-75 aminoadipate-semialdehyde synthase Mus musculus 34-37 20862766-4 2010 Cellular succinate dehydrogenase (SDH) activity was estimated using the MTT method (3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, a yellow tetrazole), and activities were normalized to Teflon controls. thiazolyl blue 84-144 aminoadipate-semialdehyde synthase Mus musculus 9-32 20862766-4 2010 Cellular succinate dehydrogenase (SDH) activity was estimated using the MTT method (3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, a yellow tetrazole), and activities were normalized to Teflon controls. thiazolyl blue 84-144 aminoadipate-semialdehyde synthase Mus musculus 34-37 20862766-4 2010 Cellular succinate dehydrogenase (SDH) activity was estimated using the MTT method (3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, a yellow tetrazole), and activities were normalized to Teflon controls. 1H-tetrazole 155-164 aminoadipate-semialdehyde synthase Mus musculus 9-32 20862766-4 2010 Cellular succinate dehydrogenase (SDH) activity was estimated using the MTT method (3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, a yellow tetrazole), and activities were normalized to Teflon controls. 1H-tetrazole 155-164 aminoadipate-semialdehyde synthase Mus musculus 34-37 20862766-7 2010 After 12 weeks of immersion in saline, AHP exhibited the SDH activity above Tf (120%), followed by ERx (78%), ER (58%), PCS (38%), and EPH (28%), all statistically distinct (p < 0.05). Sodium Chloride 31-37 aminoadipate-semialdehyde synthase Mus musculus 57-60 20054649-4 2010 Curcumin supplementation to MNU treated mice was able to reduce significantly the activities of the G6P, G6I, hexokinase, LDH, SDH and increased the glycogen contents in both the regions of brain which were altered following MNU treatment. Curcumin 0-8 aminoadipate-semialdehyde synthase Mus musculus 127-130 20054649-4 2010 Curcumin supplementation to MNU treated mice was able to reduce significantly the activities of the G6P, G6I, hexokinase, LDH, SDH and increased the glycogen contents in both the regions of brain which were altered following MNU treatment. Methylnitrosourea 28-31 aminoadipate-semialdehyde synthase Mus musculus 127-130 19956719-1 2009 BACKGROUND: Mitochondrial succinate dehydrogenase (SDH) is a component of both the tricarboxylic acid cycle and the electron transport chain. Tricarboxylic Acids 83-101 aminoadipate-semialdehyde synthase Mus musculus 51-54 18951770-3 2009 The activity of TCA cycle enzymes such as isocitrate dehydrogenase (ICDH), succinate dehydrogenase (SDH), and malate dehydrogenase (MDH) have been studied. Tricarboxylic Acids 16-19 aminoadipate-semialdehyde synthase Mus musculus 75-98 18936211-1 2008 Alpha-aminoadipate delta-semialdehyde synthase (AASS) is the bifunctional enzyme containing the lysine alpha-ketoglutarate reductase (LKR) and saccharopine dehydrogenase activities responsible for the first 2 steps in the irreversible catabolism of lysine. Lysine 96-102 aminoadipate-semialdehyde synthase Mus musculus 134-137 18951770-3 2009 The activity of TCA cycle enzymes such as isocitrate dehydrogenase (ICDH), succinate dehydrogenase (SDH), and malate dehydrogenase (MDH) have been studied. Tricarboxylic Acids 16-19 aminoadipate-semialdehyde synthase Mus musculus 100-103 18765248-2 2009 3-nitropropionic acid (3NP) induces the inhibition of succinate dehydrogenase (SDH), an increase in oxidative stress and anatomic changes that are related to the pathophysiology of HD. 3-nitropropionic acid 0-21 aminoadipate-semialdehyde synthase Mus musculus 54-77 18765248-2 2009 3-nitropropionic acid (3NP) induces the inhibition of succinate dehydrogenase (SDH), an increase in oxidative stress and anatomic changes that are related to the pathophysiology of HD. 3-nitropropionic acid 0-21 aminoadipate-semialdehyde synthase Mus musculus 79-82 18765248-2 2009 3-nitropropionic acid (3NP) induces the inhibition of succinate dehydrogenase (SDH), an increase in oxidative stress and anatomic changes that are related to the pathophysiology of HD. 3-nitropropionic acid 23-26 aminoadipate-semialdehyde synthase Mus musculus 54-77 18765248-2 2009 3-nitropropionic acid (3NP) induces the inhibition of succinate dehydrogenase (SDH), an increase in oxidative stress and anatomic changes that are related to the pathophysiology of HD. 3-nitropropionic acid 23-26 aminoadipate-semialdehyde synthase Mus musculus 79-82 18765248-8 2009 Finally, 3NP induced a decrease in SDH activity at both ages. 3-nitropropionic acid 9-12 aminoadipate-semialdehyde synthase Mus musculus 35-38 18765248-9 2009 We suggest that the 3NP-induced OD in young mice is related to the inhibition of SDH activity. 3-nitropropionic acid 20-23 aminoadipate-semialdehyde synthase Mus musculus 81-84 18936211-1 2008 Alpha-aminoadipate delta-semialdehyde synthase (AASS) is the bifunctional enzyme containing the lysine alpha-ketoglutarate reductase (LKR) and saccharopine dehydrogenase activities responsible for the first 2 steps in the irreversible catabolism of lysine. Lysine 96-102 aminoadipate-semialdehyde synthase Mus musculus 143-169 18936211-2 2008 A rare disease in humans, familial hyperlysinemia, can be caused by very low LKR activity and, as expected, reduces the lysine "requirement" of the individual. Lysine 40-46 aminoadipate-semialdehyde synthase Mus musculus 77-80 18372923-3 2008 Here, we show that alpha-TOS inhibits succinate dehydrogenase (SDH) activity of complex II (CII) by interacting with the proximal and distal ubiquinone (UbQ)-binding site (Q(P) and Q(D), respectively). alpha-Tocopherol 19-28 aminoadipate-semialdehyde synthase Mus musculus 63-66 18372923-3 2008 Here, we show that alpha-TOS inhibits succinate dehydrogenase (SDH) activity of complex II (CII) by interacting with the proximal and distal ubiquinone (UbQ)-binding site (Q(P) and Q(D), respectively). Ubiquinone 141-151 aminoadipate-semialdehyde synthase Mus musculus 63-66 18372923-3 2008 Here, we show that alpha-TOS inhibits succinate dehydrogenase (SDH) activity of complex II (CII) by interacting with the proximal and distal ubiquinone (UbQ)-binding site (Q(P) and Q(D), respectively). Ubiquinone 153-156 aminoadipate-semialdehyde synthase Mus musculus 63-66 18372923-8 2008 We propose that alpha-TOS displaces UbQ in CII causing electrons generated by SDH to recombine with molecular oxygen to yield ROS. alpha-Tocopherol 16-25 aminoadipate-semialdehyde synthase Mus musculus 78-81 18372923-8 2008 We propose that alpha-TOS displaces UbQ in CII causing electrons generated by SDH to recombine with molecular oxygen to yield ROS. Ubiquinone 36-39 aminoadipate-semialdehyde synthase Mus musculus 78-81 18372923-8 2008 We propose that alpha-TOS displaces UbQ in CII causing electrons generated by SDH to recombine with molecular oxygen to yield ROS. Oxygen 110-116 aminoadipate-semialdehyde synthase Mus musculus 78-81 18372923-8 2008 We propose that alpha-TOS displaces UbQ in CII causing electrons generated by SDH to recombine with molecular oxygen to yield ROS. Reactive Oxygen Species 126-129 aminoadipate-semialdehyde synthase Mus musculus 78-81 19051581-1 2008 The present investigation was an attempt to evaluate the ameliorative effect of curcumin on aflatoxin-induced changes in activities of succinate dehydrogenase (SDH) and adenosine triphosphatase (ATPase) in liver and kidney of mice. Aflatoxins 92-101 aminoadipate-semialdehyde synthase Mus musculus 160-163 19051581-0 2008 Curcumin ameliorates aflatoxin-induced changes in SDH and ATPase activities in liver and kidney of mice. Curcumin 0-8 aminoadipate-semialdehyde synthase Mus musculus 50-53 17727843-6 2007 However, SDH(-/-) mice and C57BL/6N mice treated with SDH inhibitor, CP-470,711, were not protected against ischemia-induced retinal damage. cp-470 69-75 aminoadipate-semialdehyde synthase Mus musculus 54-57 19051581-0 2008 Curcumin ameliorates aflatoxin-induced changes in SDH and ATPase activities in liver and kidney of mice. Aflatoxins 21-30 aminoadipate-semialdehyde synthase Mus musculus 50-53 19051581-1 2008 The present investigation was an attempt to evaluate the ameliorative effect of curcumin on aflatoxin-induced changes in activities of succinate dehydrogenase (SDH) and adenosine triphosphatase (ATPase) in liver and kidney of mice. Curcumin 80-88 aminoadipate-semialdehyde synthase Mus musculus 135-158 19051581-1 2008 The present investigation was an attempt to evaluate the ameliorative effect of curcumin on aflatoxin-induced changes in activities of succinate dehydrogenase (SDH) and adenosine triphosphatase (ATPase) in liver and kidney of mice. Curcumin 80-88 aminoadipate-semialdehyde synthase Mus musculus 160-163 19051581-1 2008 The present investigation was an attempt to evaluate the ameliorative effect of curcumin on aflatoxin-induced changes in activities of succinate dehydrogenase (SDH) and adenosine triphosphatase (ATPase) in liver and kidney of mice. Aflatoxins 92-101 aminoadipate-semialdehyde synthase Mus musculus 135-158 19051581-7 2008 The results showed that in liver and kidney of mice activities of both the enzymes succinate dehydrogenase and adenosine triphosphatase were found to be reduced in the groups treated with low dose and high dose of aflatoxin, which were ameliorated by the treatment of curcumin along with aflatoxin in other groups. Aflatoxins 214-223 aminoadipate-semialdehyde synthase Mus musculus 83-106 19051581-7 2008 The results showed that in liver and kidney of mice activities of both the enzymes succinate dehydrogenase and adenosine triphosphatase were found to be reduced in the groups treated with low dose and high dose of aflatoxin, which were ameliorated by the treatment of curcumin along with aflatoxin in other groups. Curcumin 268-276 aminoadipate-semialdehyde synthase Mus musculus 83-106 19051581-7 2008 The results showed that in liver and kidney of mice activities of both the enzymes succinate dehydrogenase and adenosine triphosphatase were found to be reduced in the groups treated with low dose and high dose of aflatoxin, which were ameliorated by the treatment of curcumin along with aflatoxin in other groups. Aflatoxins 288-297 aminoadipate-semialdehyde synthase Mus musculus 83-106 19051581-8 2008 Thus, curcumin along with aflatoxin ameliorates aflatoxin-induced changes in succinate dehydrogenase and adenosine triphosphatase activities in liver and kidney of mice. Curcumin 6-14 aminoadipate-semialdehyde synthase Mus musculus 77-100 19051581-8 2008 Thus, curcumin along with aflatoxin ameliorates aflatoxin-induced changes in succinate dehydrogenase and adenosine triphosphatase activities in liver and kidney of mice. Aflatoxins 26-35 aminoadipate-semialdehyde synthase Mus musculus 77-100 19051581-8 2008 Thus, curcumin along with aflatoxin ameliorates aflatoxin-induced changes in succinate dehydrogenase and adenosine triphosphatase activities in liver and kidney of mice. Aflatoxins 48-57 aminoadipate-semialdehyde synthase Mus musculus 77-100 18569708-3 2008 Decreased activities of electron transport chain complexes and TCA cycle key enzymes such as isocitrate dehydrogenase (ICDH), succinate dehydrogenase (SDH), malate dehydrogenase (MDH) and alpha-ketoglutarate dehydrogenase (alpha-KGDH), in lung cancer bearing animals were observed. Tricarboxylic Acids 63-66 aminoadipate-semialdehyde synthase Mus musculus 126-149 18569708-3 2008 Decreased activities of electron transport chain complexes and TCA cycle key enzymes such as isocitrate dehydrogenase (ICDH), succinate dehydrogenase (SDH), malate dehydrogenase (MDH) and alpha-ketoglutarate dehydrogenase (alpha-KGDH), in lung cancer bearing animals were observed. Tricarboxylic Acids 63-66 aminoadipate-semialdehyde synthase Mus musculus 151-154 16463653-6 2005 It was found that Jat (50 mg/kg, 100 mg/kg) could significantly decrease blood glucose level in a dose- and time-dependent manner in both normal and alloxan-diabetic mice, increase the activity of SDH, but had no significant effects on the LC level and LDH activity. jatrorrhizine 18-21 aminoadipate-semialdehyde synthase Mus musculus 197-200 15992781-1 2005 In this study we investigated whether succinate, the accumulating substrate in succinate dehydrogenase (SDH) deficiencies and SDH inhibitor intoxication, causes lipoperoxidation and protein carbonylation, and if NMDA receptors are involved in the succinate-induced oxidative damage. Succinic Acid 38-47 aminoadipate-semialdehyde synthase Mus musculus 79-102 15992781-1 2005 In this study we investigated whether succinate, the accumulating substrate in succinate dehydrogenase (SDH) deficiencies and SDH inhibitor intoxication, causes lipoperoxidation and protein carbonylation, and if NMDA receptors are involved in the succinate-induced oxidative damage. Succinic Acid 38-47 aminoadipate-semialdehyde synthase Mus musculus 104-107 15992781-1 2005 In this study we investigated whether succinate, the accumulating substrate in succinate dehydrogenase (SDH) deficiencies and SDH inhibitor intoxication, causes lipoperoxidation and protein carbonylation, and if NMDA receptors are involved in the succinate-induced oxidative damage. Succinic Acid 38-47 aminoadipate-semialdehyde synthase Mus musculus 126-129 15992781-7 2005 These results suggest the involvement of NMDA receptors in these effects of succinate, which may of particular relevance for succinate-accumulating conditions, such as SDH inhibitors intoxication and inherited SDH deficiencies. Succinic Acid 76-85 aminoadipate-semialdehyde synthase Mus musculus 168-171 15098936-1 2004 Intrastriatal administration of the succinate dehydrogenase (SDH) inhibitor malonate produces neuronal injury by a "secondary excitotoxic" mechanism involving the generation of reactive oxygen species (ROS). malonic acid 76-84 aminoadipate-semialdehyde synthase Mus musculus 36-59 15098936-1 2004 Intrastriatal administration of the succinate dehydrogenase (SDH) inhibitor malonate produces neuronal injury by a "secondary excitotoxic" mechanism involving the generation of reactive oxygen species (ROS). malonic acid 76-84 aminoadipate-semialdehyde synthase Mus musculus 61-64 15098936-1 2004 Intrastriatal administration of the succinate dehydrogenase (SDH) inhibitor malonate produces neuronal injury by a "secondary excitotoxic" mechanism involving the generation of reactive oxygen species (ROS). Reactive Oxygen Species 177-200 aminoadipate-semialdehyde synthase Mus musculus 36-59 15098936-1 2004 Intrastriatal administration of the succinate dehydrogenase (SDH) inhibitor malonate produces neuronal injury by a "secondary excitotoxic" mechanism involving the generation of reactive oxygen species (ROS). Reactive Oxygen Species 177-200 aminoadipate-semialdehyde synthase Mus musculus 61-64 15098936-1 2004 Intrastriatal administration of the succinate dehydrogenase (SDH) inhibitor malonate produces neuronal injury by a "secondary excitotoxic" mechanism involving the generation of reactive oxygen species (ROS). Reactive Oxygen Species 202-205 aminoadipate-semialdehyde synthase Mus musculus 36-59 15098936-1 2004 Intrastriatal administration of the succinate dehydrogenase (SDH) inhibitor malonate produces neuronal injury by a "secondary excitotoxic" mechanism involving the generation of reactive oxygen species (ROS). Reactive Oxygen Species 202-205 aminoadipate-semialdehyde synthase Mus musculus 61-64 11026606-4 2000 APAP treatment resulted in elevation of SDH activity and BUN to 2,490 U/ml and 47 mg/dl, respectively. Acetaminophen 0-4 aminoadipate-semialdehyde synthase Mus musculus 40-43 14968292-7 2004 In the diabetic and non-diabetic groups, hAR-Tg:SDH null mice had the highest sorbitol content among all four genetic types including hAR-Tg:SDH null, SDH null, hAR-Tg and littermates. Sorbitol 78-86 aminoadipate-semialdehyde synthase Mus musculus 48-51 1515673-9 1992 The decrease in SDH activity after MTX, correlated to the decrease in the mitochondrial content, might be due to mitochondrial damage resulting form the indirect effect of MTX. Methotrexate 35-38 aminoadipate-semialdehyde synthase Mus musculus 16-19 10821428-5 2000 Sch B, but not DDB, pretreatment could also decrease the plasma SDH activity in CCl4-intoxicated mice. schizandrin B 0-5 aminoadipate-semialdehyde synthase Mus musculus 64-67 10821428-6 2000 The lowering of plasma SDH activity, indicative of hepatoprotection against CCl4 toxicity, by Sch B pretreatment was associated with an enhancement in hepatic mitochondrial glutathione redox status as well as an increase in mitochondrial glutathione reductase (mtGRD) activity in both non-CCl4 and CCl4-treated mice. schizandrin B 94-99 aminoadipate-semialdehyde synthase Mus musculus 23-26 10821428-6 2000 The lowering of plasma SDH activity, indicative of hepatoprotection against CCl4 toxicity, by Sch B pretreatment was associated with an enhancement in hepatic mitochondrial glutathione redox status as well as an increase in mitochondrial glutathione reductase (mtGRD) activity in both non-CCl4 and CCl4-treated mice. Glutathione 173-184 aminoadipate-semialdehyde synthase Mus musculus 23-26 10567240-1 1999 Lysine-oxoglutarate reductase and saccharopine dehydrogenase are enzymic activities that catalyse the first two steps of lysine degradation through the saccharopine pathway in upper eukaryotes. Lysine 121-127 aminoadipate-semialdehyde synthase Mus musculus 0-29 10567240-1 1999 Lysine-oxoglutarate reductase and saccharopine dehydrogenase are enzymic activities that catalyse the first two steps of lysine degradation through the saccharopine pathway in upper eukaryotes. Lysine 121-127 aminoadipate-semialdehyde synthase Mus musculus 34-60 10567240-9 1999 Lysine-injected mice also show an increase in lysine-oxoglutarate reductase and saccharopine dehydrogenase levels. Lysine 0-6 aminoadipate-semialdehyde synthase Mus musculus 46-75 10567240-9 1999 Lysine-injected mice also show an increase in lysine-oxoglutarate reductase and saccharopine dehydrogenase levels. Lysine 0-6 aminoadipate-semialdehyde synthase Mus musculus 80-106 8840929-3 1996 BAT thermogenic capacity was reduced in mice drinking ethanol, as shown by decreases in tissue protein and succinate dehydrogenase (SDH) activity and in the uncoupling protein content of isolated mitochondria. Ethanol 54-61 aminoadipate-semialdehyde synthase Mus musculus 107-130 8840929-3 1996 BAT thermogenic capacity was reduced in mice drinking ethanol, as shown by decreases in tissue protein and succinate dehydrogenase (SDH) activity and in the uncoupling protein content of isolated mitochondria. Ethanol 54-61 aminoadipate-semialdehyde synthase Mus musculus 132-135 8550124-3 1995 On the contrary, the observed enhanced activity of the enzyme SDH is attributed to increased supply of TCA cycle substrates from accelerated oxidation of fatty acids. Trichloroacetic Acid 103-106 aminoadipate-semialdehyde synthase Mus musculus 62-65 8550124-3 1995 On the contrary, the observed enhanced activity of the enzyme SDH is attributed to increased supply of TCA cycle substrates from accelerated oxidation of fatty acids. Fatty Acids 154-165 aminoadipate-semialdehyde synthase Mus musculus 62-65 10757527-3 2000 The mean SDH activity of motoneurons with CSAs between 100 and 400 microm2 decreased in SAMP6, but not SAMR1, at 60 weeks. csas 42-46 aminoadipate-semialdehyde synthase Mus musculus 9-12 1515673-9 1992 The decrease in SDH activity after MTX, correlated to the decrease in the mitochondrial content, might be due to mitochondrial damage resulting form the indirect effect of MTX. Methotrexate 172-175 aminoadipate-semialdehyde synthase Mus musculus 16-19 2050027-7 1991 Urethane-induced papillary adenomas exhibited intense SDH staining, whereas solid adenomas stained very lightly. Urethane 0-8 aminoadipate-semialdehyde synthase Mus musculus 54-57 2390738-4 1990 In mice made hyperthyroid by repeated triiodothyronine injections, losses of tissue SDH and proteins caused by food deprivation or surgical denervation were markedly suppressed, while the loss of UCP from the mitochondria remained unchanged. Triiodothyronine 38-54 aminoadipate-semialdehyde synthase Mus musculus 84-87 2260782-2 1990 The hepatocyte SDH activity gradient along the path between the portal veins (PV) and efferent terminal hepatic venules (THV) was analyzed by measuring the concentration of the chromophore precipitated in 10 consecutive hepatic parenchymal domains located along imaginary lines drawn across the entire PV-to-THV distance. THV 121-124 aminoadipate-semialdehyde synthase Mus musculus 15-18 2260782-3 1990 The profiles of intensity or of normalized relative optical density obtained on a high number of lines were correlated with distance values along the PV-to-THV pathway, enabling us to establish a general mathematical function relating SDH activity (chromophore concentration) to position values on a scale of 0 to 10 corresponding to the theoretical PV-to-THV distance. THV 156-159 aminoadipate-semialdehyde synthase Mus musculus 235-238 2260782-3 1990 The profiles of intensity or of normalized relative optical density obtained on a high number of lines were correlated with distance values along the PV-to-THV pathway, enabling us to establish a general mathematical function relating SDH activity (chromophore concentration) to position values on a scale of 0 to 10 corresponding to the theoretical PV-to-THV distance. THV 356-359 aminoadipate-semialdehyde synthase Mus musculus 235-238 2260782-4 1990 The equation can be used to interpolate the SDH activity surrounding any intrahepatic object located between the PV and the THV, thus making it possible to calculate the object"s anatomical-functional position coordinates in the liver acinus. THV 124-127 aminoadipate-semialdehyde synthase Mus musculus 44-47 1701184-0 1991 A cytochemical staining procedure for succinate dehydrogenase activity in pre-ovulatory mouse oocytes embedded in low gelling temperature agarose. Sepharose 138-145 aminoadipate-semialdehyde synthase Mus musculus 38-61 1701184-5 1991 We applied the procedure to oocytes matured in vitro and found that the location of the formazan precipitate as a result of SDH activity correlated well with the location of mitochondria. Formazans 88-96 aminoadipate-semialdehyde synthase Mus musculus 124-127 2046301-0 1991 [The effect of adrenaline on the succinate dehydrogenase activity in functionally changed (lymphoid leukosis) lymphocytes in mice]. Epinephrine 15-25 aminoadipate-semialdehyde synthase Mus musculus 33-56 2046301-1 1991 The activity of succinate dehydrogenase (SDH) in lymphocytes of peripheral blood of AKR mice was measured in response to intraperitoneal injection of epinephrine hydrochloride at a dose of 1 mg/kg. Epinephrine 150-175 aminoadipate-semialdehyde synthase Mus musculus 16-39 2046301-1 1991 The activity of succinate dehydrogenase (SDH) in lymphocytes of peripheral blood of AKR mice was measured in response to intraperitoneal injection of epinephrine hydrochloride at a dose of 1 mg/kg. Epinephrine 150-175 aminoadipate-semialdehyde synthase Mus musculus 41-44 2046301-2 1991 SDH reactions to epinephrine were of two types: increase or decrease of activity. Epinephrine 17-28 aminoadipate-semialdehyde synthase Mus musculus 0-3 2046301-4 1991 The decrease of epinephrine activation of SDH in lymphocytes was found to be correlated with the age of animals and hematological manifestations of hemoblastosis they developed. Epinephrine 16-27 aminoadipate-semialdehyde synthase Mus musculus 42-45 35351859-7 2022 Succinate levels were significantly reduced following treatment with inhibitors of succinate dehydrogenase (SDH), purine nucleotide cycle (PNC), and malate/aspartate shuttle (MAS), with the corresponding attenuation of oxidative stress, iron stress, neuronal damage, and cognitive impairment. Succinic Acid 0-9 aminoadipate-semialdehyde synthase Mus musculus 83-106 35472723-5 2022 Mechanistically, metabolomic and transcriptomic studies reveal that the loss of SDH causes excess succinate accumulation, which inappropriately activates mTORC1-regulated metabolic anabolism, including increased SREBP-regulated lipid synthesis. Succinic Acid 98-107 aminoadipate-semialdehyde synthase Mus musculus 80-83 2379144-4 1990 Urethane-induced papillary adenomas exhibited intense SDH staining while alveolar adenomas stained very lightly. Urethane 0-8 aminoadipate-semialdehyde synthase Mus musculus 54-57 34425095-6 2021 IRG1 catalyzes the production of a TCA derivative, itaconate, an inhibitor of succinate dehydrogenase (SDH). Tricarboxylic Acids 35-38 aminoadipate-semialdehyde synthase Mus musculus 78-101 34425095-6 2021 IRG1 catalyzes the production of a TCA derivative, itaconate, an inhibitor of succinate dehydrogenase (SDH). Tricarboxylic Acids 35-38 aminoadipate-semialdehyde synthase Mus musculus 103-106 34425095-6 2021 IRG1 catalyzes the production of a TCA derivative, itaconate, an inhibitor of succinate dehydrogenase (SDH). itaconic acid 51-60 aminoadipate-semialdehyde synthase Mus musculus 78-101 34425095-6 2021 IRG1 catalyzes the production of a TCA derivative, itaconate, an inhibitor of succinate dehydrogenase (SDH). itaconic acid 51-60 aminoadipate-semialdehyde synthase Mus musculus 103-106 34425095-10 2021 In alignment with the reduction in IRG1 levels and itaconate production, we observed an upregulation of SDH activity during obesity. itaconic acid 51-60 aminoadipate-semialdehyde synthase Mus musculus 104-107 34425095-12 2021 miR-144 silencing selectively reduced the activities of both SDH and FH resulting in the accumulation of their related substrates succinate and fumarate. Succinic Acid 130-139 aminoadipate-semialdehyde synthase Mus musculus 61-64 34425095-12 2021 miR-144 silencing selectively reduced the activities of both SDH and FH resulting in the accumulation of their related substrates succinate and fumarate. Fumarates 144-152 aminoadipate-semialdehyde synthase Mus musculus 61-64 34425095-13 2021 Moreover, molecular dynamics analyses revealed the potential role of itaconate as a competitive inhibitor of not only SDH but also FH. itaconic acid 69-78 aminoadipate-semialdehyde synthase Mus musculus 118-121 35135854-1 2022 Mutations in the AASS (Aminoadipate-Semialdehyde Synthase) gene encoding alpha-aminoadipic semialdehyde synthase lead to hyperlysinemia-I, a benign metabolic variant without clinical significance, and hyperlysinemia-II with developmental delay and intellectual disability. semialdehyde 91-103 aminoadipate-semialdehyde synthase Mus musculus 17-21 35135854-3 2022 Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development. Lysine 152-158 aminoadipate-semialdehyde synthase Mus musculus 20-24 35135854-3 2022 Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development. Lysine 152-158 aminoadipate-semialdehyde synthase Mus musculus 114-117 35135854-3 2022 Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development. Lysine 333-339 aminoadipate-semialdehyde synthase Mus musculus 20-24 35135854-3 2022 Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development. Lysine 333-339 aminoadipate-semialdehyde synthase Mus musculus 114-117 35135854-3 2022 Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development. Lysine 333-339 aminoadipate-semialdehyde synthase Mus musculus 209-213 35135854-3 2022 Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development. saccharopine 344-356 aminoadipate-semialdehyde synthase Mus musculus 20-24 35135854-3 2022 Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development. saccharopine 344-356 aminoadipate-semialdehyde synthase Mus musculus 114-117 35135854-3 2022 Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development. saccharopine 344-356 aminoadipate-semialdehyde synthase Mus musculus 209-213 35135854-7 2022 Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development. Lysine 101-107 aminoadipate-semialdehyde synthase Mus musculus 56-59 35135854-7 2022 Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development. Lysine 101-107 aminoadipate-semialdehyde synthase Mus musculus 70-74 35135854-7 2022 Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development. Lysine 249-255 aminoadipate-semialdehyde synthase Mus musculus 70-74 35135854-7 2022 Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development. Lysine 249-255 aminoadipate-semialdehyde synthase Mus musculus 192-195 35135854-7 2022 Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development. Lysine 249-255 aminoadipate-semialdehyde synthase Mus musculus 206-210 35135854-7 2022 Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development. saccharopine 260-272 aminoadipate-semialdehyde synthase Mus musculus 70-74 35135854-7 2022 Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development. saccharopine 260-272 aminoadipate-semialdehyde synthase Mus musculus 192-195 35135854-7 2022 Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development. saccharopine 260-272 aminoadipate-semialdehyde synthase Mus musculus 206-210 35351859-7 2022 Succinate levels were significantly reduced following treatment with inhibitors of succinate dehydrogenase (SDH), purine nucleotide cycle (PNC), and malate/aspartate shuttle (MAS), with the corresponding attenuation of oxidative stress, iron stress, neuronal damage, and cognitive impairment. Succinic Acid 0-9 aminoadipate-semialdehyde synthase Mus musculus 108-111 35351859-7 2022 Succinate levels were significantly reduced following treatment with inhibitors of succinate dehydrogenase (SDH), purine nucleotide cycle (PNC), and malate/aspartate shuttle (MAS), with the corresponding attenuation of oxidative stress, iron stress, neuronal damage, and cognitive impairment. Iron 237-241 aminoadipate-semialdehyde synthase Mus musculus 108-111 35351859-8 2022 Reversal catalysis of SDH through fumarate from the PNC and MAS pathways might be involved in hypoxia-induced succinate accumulation. Fumarates 34-42 aminoadipate-semialdehyde synthase Mus musculus 22-25 35351859-8 2022 Reversal catalysis of SDH through fumarate from the PNC and MAS pathways might be involved in hypoxia-induced succinate accumulation. Succinic Acid 110-119 aminoadipate-semialdehyde synthase Mus musculus 22-25 3252685-0 1988 Fluctuations of succinic dehydrogenase during morphine tolerance, dependence and withdrawals in the spinal cord and medulla oblongata of mice. Morphine 46-54 aminoadipate-semialdehyde synthase Mus musculus 16-38 2763303-3 1989 Chronic ethanol treatment via liquid diets from ages 20 to 55 days resulted in decreased activities of SDH and LDH at ages 40 and 44 days, and of GDH at ages 34, 40, and 44 days. Ethanol 8-15 aminoadipate-semialdehyde synthase Mus musculus 103-106 3252685-4 1988 There is a progressive inhibition of SDH upto six days of morphine treatment. Morphine 58-66 aminoadipate-semialdehyde synthase Mus musculus 37-40 3657067-4 1987 SDH activity was stimulated by hypoxia in a greater degree in the piracetam-treated mice. Piracetam 66-75 aminoadipate-semialdehyde synthase Mus musculus 0-3 3397540-5 1988 Because both NADH-DH and SDH contain numerous iron-sulfur clusters, damage to these structures may be one result of injury by activated macrophages. Iron 46-50 aminoadipate-semialdehyde synthase Mus musculus 25-28 3397540-5 1988 Because both NADH-DH and SDH contain numerous iron-sulfur clusters, damage to these structures may be one result of injury by activated macrophages. Sulfur 51-57 aminoadipate-semialdehyde synthase Mus musculus 25-28 3397540-12 1988 There was selective loss of 55Fe activity in the area of the gel corresponding to SDH and NADH-DH, suggesting that iron loss from iron-sulfur clusters may occur in L1210 cells injured by activated macrophages. Iron 115-119 aminoadipate-semialdehyde synthase Mus musculus 82-85 6672210-1 1983 Histochemical alterations of acute and chronic doxorubicin (DOX) cardiotoxicity in the mouse were assessed by the localization of succinate dehydrogenase (SDH), coenzyme Q10 (CoQ), cytochrome oxidase (COX), creatine phosphokinase (CPK), lactate dehydrogenase (LDH), reduced glutathione (GSH), and intracellular calcium. Doxorubicin 60-63 aminoadipate-semialdehyde synthase Mus musculus 130-153 6488084-4 1984 SDH activity was expressed either per micromole of creatine or per milligram of "true muscle fibre weight." Creatine 51-59 aminoadipate-semialdehyde synthase Mus musculus 0-3 4009299-1 1985 When fed a manganese-sufficient (20 ppm) diet, obese (ob/ob) mice have reduced levels of Mn in liver and brown adipose tissue (BAT), and depressed activities of succinate dehydrogenase (SDH) and manganese-containing superoxide dismutase (MnSOD) in BAT, compared to lean mice. Manganese 11-20 aminoadipate-semialdehyde synthase Mus musculus 161-184 4009299-1 1985 When fed a manganese-sufficient (20 ppm) diet, obese (ob/ob) mice have reduced levels of Mn in liver and brown adipose tissue (BAT), and depressed activities of succinate dehydrogenase (SDH) and manganese-containing superoxide dismutase (MnSOD) in BAT, compared to lean mice. Manganese 11-20 aminoadipate-semialdehyde synthase Mus musculus 186-189 3919098-7 1985 Expression of 20 alpha SDH in these cells is associated with resistance to growth inhibition by progesterone. Progesterone 96-108 aminoadipate-semialdehyde synthase Mus musculus 23-26 6672210-1 1983 Histochemical alterations of acute and chronic doxorubicin (DOX) cardiotoxicity in the mouse were assessed by the localization of succinate dehydrogenase (SDH), coenzyme Q10 (CoQ), cytochrome oxidase (COX), creatine phosphokinase (CPK), lactate dehydrogenase (LDH), reduced glutathione (GSH), and intracellular calcium. Doxorubicin 60-63 aminoadipate-semialdehyde synthase Mus musculus 155-158 7416733-1 1980 The effect of semisynthetic antibiotics, such as ampicillin and rifampicin on activity of succinate dehydrogenase (SDH) in the liver and spleen of mice immunized with heated typhoid vaccine was studied. Ampicillin 49-59 aminoadipate-semialdehyde synthase Mus musculus 90-113 6687816-7 1983 The data obtained indicate that the immunological effect of tuftcin is coupled with the changes in the activity of Krebs cycle enzymes (SDH) and pentose phosphate cycle enzymes (G-6-PDH). tuftcin 60-67 aminoadipate-semialdehyde synthase Mus musculus 136-139 6687816-7 1983 The data obtained indicate that the immunological effect of tuftcin is coupled with the changes in the activity of Krebs cycle enzymes (SDH) and pentose phosphate cycle enzymes (G-6-PDH). krebs 115-120 aminoadipate-semialdehyde synthase Mus musculus 136-139 6277242-5 1982 It should be noted that the inhibitory effect of rifampicin on the activity of SDH, TP and AP was less pronounced than that of lincomycin. Rifampin 49-59 aminoadipate-semialdehyde synthase Mus musculus 79-82 7416733-1 1980 The effect of semisynthetic antibiotics, such as ampicillin and rifampicin on activity of succinate dehydrogenase (SDH) in the liver and spleen of mice immunized with heated typhoid vaccine was studied. Ampicillin 49-59 aminoadipate-semialdehyde synthase Mus musculus 115-118 7416733-1 1980 The effect of semisynthetic antibiotics, such as ampicillin and rifampicin on activity of succinate dehydrogenase (SDH) in the liver and spleen of mice immunized with heated typhoid vaccine was studied. Rifampin 64-74 aminoadipate-semialdehyde synthase Mus musculus 90-113 7416733-1 1980 The effect of semisynthetic antibiotics, such as ampicillin and rifampicin on activity of succinate dehydrogenase (SDH) in the liver and spleen of mice immunized with heated typhoid vaccine was studied. Rifampin 64-74 aminoadipate-semialdehyde synthase Mus musculus 115-118 7416733-2 1980 The study showed that the average therapeutic dose of ampicillin, i.e. 50 mg/kg administered intramuscularly to the animals before and during the immunization increased the SDH activity in the spleen tissue by the 5th day. Ampicillin 54-64 aminoadipate-semialdehyde synthase Mus musculus 173-176 33667291-2 2021 We found that dietary quercetin supplementation in mice significantly increased oxidative fiber-related gene expression, slow-twitch fiber percentage and succinic dehydrogenase (SDH) activity. dietary quercetin 14-31 aminoadipate-semialdehyde synthase Mus musculus 154-176 33028985-0 2021 Tanshinone IIA prevents LPS-induced inflammatory responses in mice via inactivation of succinate dehydrogenase in macrophages. tanshinone 0-14 aminoadipate-semialdehyde synthase Mus musculus 87-110 33028985-4 2021 In lipopolysaccharides (LPS)-stimulated mouse bone marrow-derived macrophages (BMDMs), Tan-IIA (10 muM) significantly decreased succinate-boosted IL-1beta and IL-6 production, accompanied by upregulation of IL-1RA and IL-10 release via inhibiting succinate dehydrogenase (SDH). Succinic Acid 128-137 aminoadipate-semialdehyde synthase Mus musculus 247-270 33028985-4 2021 In lipopolysaccharides (LPS)-stimulated mouse bone marrow-derived macrophages (BMDMs), Tan-IIA (10 muM) significantly decreased succinate-boosted IL-1beta and IL-6 production, accompanied by upregulation of IL-1RA and IL-10 release via inhibiting succinate dehydrogenase (SDH). Succinic Acid 128-137 aminoadipate-semialdehyde synthase Mus musculus 272-275 33028985-5 2021 Tan-IIA concentration dependently inhibited SDH activity with an estimated IC50 of 4.47 muM in LPS-activated BMDMs. tanshinone 0-7 aminoadipate-semialdehyde synthase Mus musculus 44-47 33666092-4 2021 Current evidence suggests that elevated ROS production in ischemic tissues occurs due to accumulation of the mitochondrial metabolite succinate during ischemia via succinate dehydrogenase (SDH), and this succinate is rapidly oxidized at reperfusion. Reactive Oxygen Species 40-43 aminoadipate-semialdehyde synthase Mus musculus 164-187 33666092-4 2021 Current evidence suggests that elevated ROS production in ischemic tissues occurs due to accumulation of the mitochondrial metabolite succinate during ischemia via succinate dehydrogenase (SDH), and this succinate is rapidly oxidized at reperfusion. Reactive Oxygen Species 40-43 aminoadipate-semialdehyde synthase Mus musculus 189-192 33666092-4 2021 Current evidence suggests that elevated ROS production in ischemic tissues occurs due to accumulation of the mitochondrial metabolite succinate during ischemia via succinate dehydrogenase (SDH), and this succinate is rapidly oxidized at reperfusion. Succinic Acid 134-143 aminoadipate-semialdehyde synthase Mus musculus 164-187 33666092-4 2021 Current evidence suggests that elevated ROS production in ischemic tissues occurs due to accumulation of the mitochondrial metabolite succinate during ischemia via succinate dehydrogenase (SDH), and this succinate is rapidly oxidized at reperfusion. Succinic Acid 134-143 aminoadipate-semialdehyde synthase Mus musculus 189-192 33666092-4 2021 Current evidence suggests that elevated ROS production in ischemic tissues occurs due to accumulation of the mitochondrial metabolite succinate during ischemia via succinate dehydrogenase (SDH), and this succinate is rapidly oxidized at reperfusion. Succinic Acid 164-173 aminoadipate-semialdehyde synthase Mus musculus 189-192 33666092-9 2021 Our evidence also shows that inhibition of SDH by malonate treatment after birth extends the window of cardiomyocyte proliferation and regeneration in juvenile mice. malonic acid 50-58 aminoadipate-semialdehyde synthase Mus musculus 43-46 33666092-11 2021 Our metabolite analysis following SDH inhibition by malonate induces dynamic changes in adult cardiac metabolism. malonic acid 52-60 aminoadipate-semialdehyde synthase Mus musculus 34-37 33666092-12 2021 Conclusions: Inhibition of SDH by malonate promotes adult cardiomyocyte proliferation, revascularization, and heart regeneration via metabolic reprogramming. malonic acid 34-42 aminoadipate-semialdehyde synthase Mus musculus 27-30 33667291-2 2021 We found that dietary quercetin supplementation in mice significantly increased oxidative fiber-related gene expression, slow-twitch fiber percentage and succinic dehydrogenase (SDH) activity. dietary quercetin 14-31 aminoadipate-semialdehyde synthase Mus musculus 178-181 33247500-1 2021 Mutations in any of the genes encoding the four subunits of succinate dehydrogenase (SDH), a mitochondrial membrane-bound enzyme complex that is involved in both the tricarboxylic acid cycle and the electron transport chain, can lead to a variety of disorders. Tricarboxylic Acids 166-184 aminoadipate-semialdehyde synthase Mus musculus 60-83 33247500-1 2021 Mutations in any of the genes encoding the four subunits of succinate dehydrogenase (SDH), a mitochondrial membrane-bound enzyme complex that is involved in both the tricarboxylic acid cycle and the electron transport chain, can lead to a variety of disorders. Tricarboxylic Acids 166-184 aminoadipate-semialdehyde synthase Mus musculus 85-88 32567100-0 2020 Deletion of 2-aminoadipic semialdehyde synthase limits metabolite accumulation in cell and mouse models for glutaric aciduria type 1. glutaric 108-116 aminoadipate-semialdehyde synthase Mus musculus 12-47 32567100-4 2020 In the GA1 mouse model, deletion of Aass leads to a 4.3-, 3.8- and 3.2-fold decrease in the glutaric acid levels in urine, brain and liver, respectively. glutaric acid 92-105 aminoadipate-semialdehyde synthase Mus musculus 36-40 32567100-6 2020 These in vivo data demonstrate that the saccharopine pathway is the main source of glutaric acid production in the brain and periphery of a mouse model for GA1, and support the notion that pharmacological inhibition of AASS may represent an attractive strategy to treat GA1. saccharopine 40-52 aminoadipate-semialdehyde synthase Mus musculus 219-223 32567100-6 2020 These in vivo data demonstrate that the saccharopine pathway is the main source of glutaric acid production in the brain and periphery of a mouse model for GA1, and support the notion that pharmacological inhibition of AASS may represent an attractive strategy to treat GA1. glutaric acid 83-96 aminoadipate-semialdehyde synthase Mus musculus 219-223 32855685-10 2020 RCOL administration was found to reverse EE-induced mitochondrial structural damage and alleviated defects inflicted onto the energy supply mechanism by increasing CS, SDH, Na+-K+-ATPase and glycogen levels. rcol 0-4 aminoadipate-semialdehyde synthase Mus musculus 168-171 33023985-6 2020 The decrease in SDH levels in tumor cells resulted in an accumulation of succinate, which enhanced the stability of the transcription factor HIF1alpha and reprogrammed cell metabolism to a glycolytic state. Succinic Acid 73-82 aminoadipate-semialdehyde synthase Mus musculus 16-19 32648168-2 2022 During ischemia, succinate accumulates and its oxidation upon reperfusion by succinate dehydrogenase (SDH) drives ROS production. Succinic Acid 17-26 aminoadipate-semialdehyde synthase Mus musculus 77-100 32521505-11 2020 In total, five metabolism-related genes, namely, Aass, Cdo1, Cyp2b23, Nt5e, and Pck2, were expressed in all three knockout ESC lines, and three of them were associated with regulation of ATP generation. Adenosine Triphosphate 187-190 aminoadipate-semialdehyde synthase Mus musculus 49-53 32648168-2 2022 During ischemia, succinate accumulates and its oxidation upon reperfusion by succinate dehydrogenase (SDH) drives ROS production. Succinic Acid 17-26 aminoadipate-semialdehyde synthase Mus musculus 102-105 32648168-2 2022 During ischemia, succinate accumulates and its oxidation upon reperfusion by succinate dehydrogenase (SDH) drives ROS production. Reactive Oxygen Species 114-117 aminoadipate-semialdehyde synthase Mus musculus 77-100 32648168-2 2022 During ischemia, succinate accumulates and its oxidation upon reperfusion by succinate dehydrogenase (SDH) drives ROS production. Reactive Oxygen Species 114-117 aminoadipate-semialdehyde synthase Mus musculus 102-105 32648168-3 2022 Inhibition of succinate accumulation and/or oxidation by dimethyl malonate (DMM), a cell permeable prodrug of the SDH inhibitor malonate, can decrease I/R injury. Succinic Acid 14-23 aminoadipate-semialdehyde synthase Mus musculus 114-117 32648168-3 2022 Inhibition of succinate accumulation and/or oxidation by dimethyl malonate (DMM), a cell permeable prodrug of the SDH inhibitor malonate, can decrease I/R injury. methyl malonate 57-74 aminoadipate-semialdehyde synthase Mus musculus 114-117 32648168-3 2022 Inhibition of succinate accumulation and/or oxidation by dimethyl malonate (DMM), a cell permeable prodrug of the SDH inhibitor malonate, can decrease I/R injury. methyl malonate 76-79 aminoadipate-semialdehyde synthase Mus musculus 114-117 32648168-3 2022 Inhibition of succinate accumulation and/or oxidation by dimethyl malonate (DMM), a cell permeable prodrug of the SDH inhibitor malonate, can decrease I/R injury. malonic acid 66-74 aminoadipate-semialdehyde synthase Mus musculus 114-117 32396064-4 2020 Upon M1 stimulation, myeloid-specific Bmal1 knockout (M-BKO) renders macrophages unable to sustain mitochondrial function, enhancing succinate dehydrogenase (SDH)-mediated mitochondrial ROS production and Hif-1a-dependent metabolic reprogramming and inflammatory damage. ros 186-189 aminoadipate-semialdehyde synthase Mus musculus 133-156 32396064-4 2020 Upon M1 stimulation, myeloid-specific Bmal1 knockout (M-BKO) renders macrophages unable to sustain mitochondrial function, enhancing succinate dehydrogenase (SDH)-mediated mitochondrial ROS production and Hif-1a-dependent metabolic reprogramming and inflammatory damage. ros 186-189 aminoadipate-semialdehyde synthase Mus musculus 158-161 32396064-6 2020 Consequently, M-BKO increases melanoma tumor burden, while administrating an SDH inhibitor dimethyl malonate suppresses tumor growth. methyl malonate 91-108 aminoadipate-semialdehyde synthase Mus musculus 77-80