PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32368714-4 2020 Additionally, many legumes possess prephenate dehydrogenases (PDH/TyrAp), which are insensitive to Tyr and localized to the cytosol. Tyrosine 66-69 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 62-65 24962578-0 2014 Tyr-94 phosphorylation inhibits pyruvate dehydrogenase phosphatase 1 and promotes tumor growth. Tyrosine 0-3 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 32-54 28671678-2 2017 Tyr can be synthesized via two alternative routes by different key regulatory TyrA family enzymes, prephenate dehydrogenase (PDH, also known as TyrAp) or arogenate dehydrogenase (ADH, also known as TyrAa), representing a unique divergence of primary metabolic pathways. Tyrosine 0-3 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 99-123 28671678-2 2017 Tyr can be synthesized via two alternative routes by different key regulatory TyrA family enzymes, prephenate dehydrogenase (PDH, also known as TyrAp) or arogenate dehydrogenase (ADH, also known as TyrAa), representing a unique divergence of primary metabolic pathways. Tyrosine 0-3 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 125-128 28671678-6 2017 Reciprocal mutagenesis of the corresponding residue in divergent plant ADHs further introduced PDH activity and relaxed Tyr sensitivity, highlighting the critical role of this residue in TyrA substrate specificity that underlies the evolution of alternative Tyr biosynthetic pathways in plants. Tyrosine 120-123 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 95-98 28671678-6 2017 Reciprocal mutagenesis of the corresponding residue in divergent plant ADHs further introduced PDH activity and relaxed Tyr sensitivity, highlighting the critical role of this residue in TyrA substrate specificity that underlies the evolution of alternative Tyr biosynthetic pathways in plants. Tyrosine 187-190 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 95-98 26848621-0 2016 Src drives the Warburg effect and therapy resistance by inactivating pyruvate dehydrogenase through tyrosine-289 phosphorylation. Tyrosine 100-108 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 69-91 26848621-7 2016 Src inactivated PDH through direct phosphorylation of tyrosine-289 of PDH E1alpha subunit (PDHA1). Tyrosine 54-62 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 16-19 26848621-7 2016 Src inactivated PDH through direct phosphorylation of tyrosine-289 of PDH E1alpha subunit (PDHA1). Tyrosine 54-62 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 70-73 26848621-9 2016 Expression of a tyrosine-289 non-phosphorable PDHA1 mutant in Src-hyperactivated cancer cells restored PDH activity, increased mitochondrial respiration and oxidative stress, decreased experimental metastasis, and sensitized cancer cells to pro-oxidant treatment. Tyrosine 16-24 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 46-49 26848621-10 2016 The results suggest that Src contributes to the Warburg phenotype by inactivating PDH through tyrosine phosphorylation, and the metabolic effect of Src is essential for Src-driven malignancy and therapy resistance. Tyrosine 94-102 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 82-85 25104357-0 2014 Tyr-301 phosphorylation inhibits pyruvate dehydrogenase by blocking substrate binding and promotes the Warburg effect. Tyrosine 0-3 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 33-55 29164132-4 2017 Tyr is synthesized via two alternative routes mediated by a TyrA family enzyme, prephenate, or arogenate dehydrogenase (PDH/TyrAp or ADH/TyrAa), typically found in microbes and plants, respectively. Tyrosine 0-3 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 120-123 24962578-4 2014 We previously reported that tyrosine phosphorylation activates and inhibits mitochondrial pyruvate dehydrogenase kinase (PDK) and phosphatase (PDP), respectively, leading to enhanced inhibitory serine phosphorylation of pyruvate dehydrogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells. Tyrosine 28-36 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 90-112 24962578-4 2014 We previously reported that tyrosine phosphorylation activates and inhibits mitochondrial pyruvate dehydrogenase kinase (PDK) and phosphatase (PDP), respectively, leading to enhanced inhibitory serine phosphorylation of pyruvate dehydrogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells. Tyrosine 28-36 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 220-242 24962578-4 2014 We previously reported that tyrosine phosphorylation activates and inhibits mitochondrial pyruvate dehydrogenase kinase (PDK) and phosphatase (PDP), respectively, leading to enhanced inhibitory serine phosphorylation of pyruvate dehydrogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells. Tyrosine 28-36 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 244-247 24962578-4 2014 We previously reported that tyrosine phosphorylation activates and inhibits mitochondrial pyruvate dehydrogenase kinase (PDK) and phosphatase (PDP), respectively, leading to enhanced inhibitory serine phosphorylation of pyruvate dehydrogenase (PDH) and consequently inhibition of pyruvate dehydrogenase complex (PDC) in cancer cells. Tyrosine 28-36 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 220-242 24962578-5 2014 In particular, Tyr-381 phosphorylation of PDP1 dissociates deacetylase SIRT3 and recruits acetyltransferase ACAT1 to PDC, resulting in increased inhibitory lysine acetylation of PDHA1 and PDP1. Tyrosine 15-18 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 42-46 24962578-5 2014 In particular, Tyr-381 phosphorylation of PDP1 dissociates deacetylase SIRT3 and recruits acetyltransferase ACAT1 to PDC, resulting in increased inhibitory lysine acetylation of PDHA1 and PDP1. Tyrosine 15-18 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 188-192 24962578-6 2014 Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. Tyrosine 47-55 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 82-86 24962578-6 2014 Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. Tyrosine 47-55 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 122-126 24962578-6 2014 Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. Tyrosine 47-55 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 122-126 24962578-6 2014 Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. Tyrosine 65-68 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 82-86 24962578-6 2014 Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. Tyrosine 65-68 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 122-126 24962578-6 2014 Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. Tyrosine 65-68 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 122-126 24962578-7 2014 We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients. Tyrosine 82-85 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 74-78 24962578-7 2014 We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients. Tyrosine 94-97 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 120-124 24962578-9 2014 Together, our findings suggest that phosphorylation at different tyrosine residues inhibits PDP1 through independent mechanisms, which act in concert to regulate PDC activity and promote the Warburg effect. Tyrosine 65-73 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 92-96 24486017-0 2014 Tyr phosphorylation of PDP1 toggles recruitment between ACAT1 and SIRT3 to regulate the pyruvate dehydrogenase complex. Tyrosine 0-3 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 23-27 24486017-0 2014 Tyr phosphorylation of PDP1 toggles recruitment between ACAT1 and SIRT3 to regulate the pyruvate dehydrogenase complex. Tyrosine 0-3 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 88-110 20432447-6 2010 Tyr/Phe, Gln and Met restriction increase phosphorylation of GSK3beta-Ser(9), phosphorylation of p53-Ser(15) and reduce the mitochondrial localization of PDH. Tyrosine 0-3 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 154-157 21415930-3 2011 Restriction of tyrosine and phenylalanine (Tyr/Phe), glutamine (Gln) or methionine (Met) differentially modulated glucose metabolism and PDH and antioxidant enzyme activity in the mitochondria of the two prostate cancer cell lines. Tyrosine 15-23 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 137-140 21415930-3 2011 Restriction of tyrosine and phenylalanine (Tyr/Phe), glutamine (Gln) or methionine (Met) differentially modulated glucose metabolism and PDH and antioxidant enzyme activity in the mitochondria of the two prostate cancer cell lines. Tyrosine 43-46 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 137-140 20432447-2 2010 This study shows that restriction of tyrosine and phenylalanine (Tyr/Phe), glutamine (Gln), or methionine (Met) differentially modulates glucose metabolism, glycogen synthase kinase 3beta (GSK3beta), p53, and pyruvate dehydrogenase (PDH) in these two cell lines. Tyrosine 37-45 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 209-231 20432447-2 2010 This study shows that restriction of tyrosine and phenylalanine (Tyr/Phe), glutamine (Gln), or methionine (Met) differentially modulates glucose metabolism, glycogen synthase kinase 3beta (GSK3beta), p53, and pyruvate dehydrogenase (PDH) in these two cell lines. Tyrosine 37-45 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 233-236 20432447-2 2010 This study shows that restriction of tyrosine and phenylalanine (Tyr/Phe), glutamine (Gln), or methionine (Met) differentially modulates glucose metabolism, glycogen synthase kinase 3beta (GSK3beta), p53, and pyruvate dehydrogenase (PDH) in these two cell lines. Tyrosine 65-68 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 209-231 20432447-2 2010 This study shows that restriction of tyrosine and phenylalanine (Tyr/Phe), glutamine (Gln), or methionine (Met) differentially modulates glucose metabolism, glycogen synthase kinase 3beta (GSK3beta), p53, and pyruvate dehydrogenase (PDH) in these two cell lines. Tyrosine 65-68 pyruvate dehydrogenase phosphatase catalytic subunit 1 Homo sapiens 233-236