PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9724635-4 1998 In contrast, PDH activity increased biphasically, with an initial rapid phase accompanying the rise in [Ca2+]m, followed by a sustained secondary activation phase associated with a decline in cellular ATP. Adenosine Triphosphate 201-204 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 13-16 15736311-1 2005 Pyruvate dehydrogenase (PDH) catalyzes the conversion of pyruvate to acetyl-coenzyme A, which enters into the Krebs cycle, providing adenosine triphosphate (ATP) to the cell. Adenosine Triphosphate 133-155 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 0-22 15736311-1 2005 Pyruvate dehydrogenase (PDH) catalyzes the conversion of pyruvate to acetyl-coenzyme A, which enters into the Krebs cycle, providing adenosine triphosphate (ATP) to the cell. Adenosine Triphosphate 133-155 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 24-27 15736311-1 2005 Pyruvate dehydrogenase (PDH) catalyzes the conversion of pyruvate to acetyl-coenzyme A, which enters into the Krebs cycle, providing adenosine triphosphate (ATP) to the cell. Adenosine Triphosphate 157-160 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 0-22 15736311-1 2005 Pyruvate dehydrogenase (PDH) catalyzes the conversion of pyruvate to acetyl-coenzyme A, which enters into the Krebs cycle, providing adenosine triphosphate (ATP) to the cell. Adenosine Triphosphate 157-160 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 24-27 12556353-12 2003 The increased activation of PDH was not explained by changes in muscle pyruvate or the ATP/ADP ratio but may be related to a decrease in the NADH/NAD(+) ratio or an epinephrine-induced increase in calcium concentration. Adenosine Triphosphate 87-90 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 28-31 3674888-0 1987 Regulation of pea mitochondrial pyruvate dehydrogenase complex activity: inhibition of ATP-dependent inactivation. Adenosine Triphosphate 87-90 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 32-54 3277539-9 1988 The PDH-stimulating activity eluted after bacitracin but ahead of ATP during gel filtration chromatography, and it was destroyed by exposure to NH4OH or alkaline phosphatase and by boiling in water. Adenosine Triphosphate 66-69 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 4-7 9723179-3 1998 Perturbations in the expression of this subunit lead to reduced or lost function of the PDH complex as a whole, resulting in a loss of ATP production. Adenosine Triphosphate 135-138 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 88-91 9555066-2 1998 During reperfusion, PDH activities were suppressed corresponding to the poor recovery of ATP and PCr concentrations and the increase in lactate concentration in the hyperglycemic group, suggesting that preischemic hyperglycemia may impair metabolism by suppressing PDH activity. Adenosine Triphosphate 89-92 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 20-23 3674888-5 1987 A model is proposed for the pyruvate plus thiamine pyrophosphate inhibition of ATP-dependent inactivation of the pyruvate dehydrogenase complex in which pyruvate exerts its inhibition of inactivation by altering or protecting the protein substrate from phosphorylation and not by directly inhibiting PDH kinase. Adenosine Triphosphate 79-82 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 113-135 3674888-5 1987 A model is proposed for the pyruvate plus thiamine pyrophosphate inhibition of ATP-dependent inactivation of the pyruvate dehydrogenase complex in which pyruvate exerts its inhibition of inactivation by altering or protecting the protein substrate from phosphorylation and not by directly inhibiting PDH kinase. Adenosine Triphosphate 79-82 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 300-303 33964039-5 2021 PDHX expression was required for the maintenance of PDH activity and the production of ATP, and its knockdown inhibited the proliferation of cancer stem cells (CSCs) and in vivo tumor growth. Adenosine Triphosphate 87-90 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 0-3 2985364-7 1985 Mediator behaved as an activator of PDH phosphatase, apparently by abolishing the inhibitory effects of ATP on phosphatase activity, but had no effect on PDH kinase activity. Adenosine Triphosphate 104-107 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 36-39 33606971-2 2021 (2020) demonstrate that pyruvate dehydrogenase (PDH) overactivation blunts NAD+ regeneration by overcharging the mitochondrial membrane potential and driving ATP synthesis beyond demand. Adenosine Triphosphate 158-161 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 24-46 33725483-3 2021 Here, we report that Rheb regulates mitochondrial tricarboxylic acid cycle flux of acetyl-CoA by activating pyruvate dehydrogenase (PDH) to increase ATP production. Adenosine Triphosphate 149-152 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 108-130 33725483-3 2021 Here, we report that Rheb regulates mitochondrial tricarboxylic acid cycle flux of acetyl-CoA by activating pyruvate dehydrogenase (PDH) to increase ATP production. Adenosine Triphosphate 149-152 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 132-135 33606971-2 2021 (2020) demonstrate that pyruvate dehydrogenase (PDH) overactivation blunts NAD+ regeneration by overcharging the mitochondrial membrane potential and driving ATP synthesis beyond demand. Adenosine Triphosphate 158-161 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 48-51 32782783-8 2020 PDP1 accelerated intracellular ATP production, leading to sufficient energy to support rapid cancer progression. Adenosine Triphosphate 31-34 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 0-4 26930489-4 2016 PDH phosphorylation was induced by a high fat diet in the liver of obese mice, which was associated with ATP elevation. Adenosine Triphosphate 105-108 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 0-3 29444744-5 2019 The results demonstrated that overexpression of the PDHA1 gene inhibited aerobic glycolysis with lower lactate via increased PDH activity; meanwhile, mitochondrial OXPHOS was enhanced accompanied with higher ATP and lower glucose consumption. Adenosine Triphosphate 208-211 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 52-55 30342991-7 2018 By this way, miR-23a promotes PDH activation and oxidative phosphorylation to generate sufficient ATP for cell proliferation. Adenosine Triphosphate 98-101 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 30-33 28132899-6 2017 We suggest that increased NCLX activity will increase sodium/proton exchange, potentially undermining oxidative phosphorylation, although this is balanced by dephosphorylation and activation of pyruvate dehydrogenase (PDH) in response to the increased [Ca2+]m. Consistent with this model, while ATP content in patient derived or control fibroblasts was not different, ATP increased significantly in response to CGP-37157 in the patient but not the control cells. Adenosine Triphosphate 295-298 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 218-221 28132899-6 2017 We suggest that increased NCLX activity will increase sodium/proton exchange, potentially undermining oxidative phosphorylation, although this is balanced by dephosphorylation and activation of pyruvate dehydrogenase (PDH) in response to the increased [Ca2+]m. Consistent with this model, while ATP content in patient derived or control fibroblasts was not different, ATP increased significantly in response to CGP-37157 in the patient but not the control cells. Adenosine Triphosphate 368-371 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 218-221 26930489-8 2016 The PDH phosphorylation was induced by incubation of mitochondrial lysate with ATP in vitro without altering the expression of PDH kinase 2 (PDK2) and 4 (PDK4). Adenosine Triphosphate 79-82 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 4-7 25737951-7 2015 However, dual knockdowns of pyruvate dehydrogenase (PDH), in combination with reduced lipid uptake or lipid/amino acid oxidation (ETFDH), does reduce ATP synthesis, TCA cycle flux, and metabolic flexibility. Adenosine Triphosphate 150-153 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 28-50 25737951-7 2015 However, dual knockdowns of pyruvate dehydrogenase (PDH), in combination with reduced lipid uptake or lipid/amino acid oxidation (ETFDH), does reduce ATP synthesis, TCA cycle flux, and metabolic flexibility. Adenosine Triphosphate 150-153 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 52-55 25152236-1 2014 Pyruvate dehydrogenase E1alpha (PDHA1) is the first component enzyme of the pyruvate dehydrogenase (PDH) complex that transforms pyruvate, via pyruvate decarboxylation, into acetyl-CoA that is subsequently used by both the citric acid cycle and oxidative phosphorylation to generate ATP. Adenosine Triphosphate 283-286 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 0-22 25152236-1 2014 Pyruvate dehydrogenase E1alpha (PDHA1) is the first component enzyme of the pyruvate dehydrogenase (PDH) complex that transforms pyruvate, via pyruvate decarboxylation, into acetyl-CoA that is subsequently used by both the citric acid cycle and oxidative phosphorylation to generate ATP. Adenosine Triphosphate 283-286 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 76-98 25152236-1 2014 Pyruvate dehydrogenase E1alpha (PDHA1) is the first component enzyme of the pyruvate dehydrogenase (PDH) complex that transforms pyruvate, via pyruvate decarboxylation, into acetyl-CoA that is subsequently used by both the citric acid cycle and oxidative phosphorylation to generate ATP. Adenosine Triphosphate 283-286 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 32-35