PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17555402-6 2007 In combination with the hypoxia-induced expression of LDHA (lactate dehydrogenase A), which converts pyruvate into lactate, PDK1 reduces the delivery of acetyl-CoA to the tricarboxylic acid cycle, thus reducing the levels of NADH and FADH2 delivered to the electron-transport chain. NAD 225-229 lactate dehydrogenase A Homo sapiens 54-58 17555402-6 2007 In combination with the hypoxia-induced expression of LDHA (lactate dehydrogenase A), which converts pyruvate into lactate, PDK1 reduces the delivery of acetyl-CoA to the tricarboxylic acid cycle, thus reducing the levels of NADH and FADH2 delivered to the electron-transport chain. NAD 225-229 lactate dehydrogenase A Homo sapiens 60-83 30209241-2 2018 Lactate dehydrogenase A (LDHA) has a key role in aerobic glycolysis (the Warburg effect) through regeneration of the electron acceptor NAD+ and is widely regarded as a desirable target for cancer therapeutics. NAD 135-139 lactate dehydrogenase A Homo sapiens 0-23 16198644-6 2005 For the oxidation of glyoxylate, K(M) values were 0.18 mM and 0.26 mM for LDHA and LDHB respectively with NAD+ as cofactor. NAD 106-110 lactate dehydrogenase A Homo sapiens 74-78 7986093-1 1994 The interaction between muscle-type lactate dehydrogenase (LDHm) and tubulin was investigated by monitoring the combined effect of NADH and tubulin on steady-state kinetics and the combined effect of NADH and pH on complex formation between tubulin and the enzyme. NAD 131-135 lactate dehydrogenase A Homo sapiens 59-63 7986093-1 1994 The interaction between muscle-type lactate dehydrogenase (LDHm) and tubulin was investigated by monitoring the combined effect of NADH and tubulin on steady-state kinetics and the combined effect of NADH and pH on complex formation between tubulin and the enzyme. NAD 200-204 lactate dehydrogenase A Homo sapiens 59-63 7986093-7 1994 In contrast to the absence of tubulin, its presence induced a modification of the kinetic behavior of LDHm; i.e., the velocity dependence on NADH concentration displayed a marked sigmoid response. NAD 141-145 lactate dehydrogenase A Homo sapiens 102-106 7986093-11 1994 NAD+ was much less effective than NADH in dissociating LDHm from immobilized tubulin. NAD 0-4 lactate dehydrogenase A Homo sapiens 55-59 7986093-11 1994 NAD+ was much less effective than NADH in dissociating LDHm from immobilized tubulin. NAD 34-38 lactate dehydrogenase A Homo sapiens 55-59 31035592-3 2019 LDHA has a higher affinity for pyruvate, preferentially converting pyruvate to lactate, and NADH to NAD+ in anaerobic conditions, whereas LDHB possess a higher affinity for lactate, preferentially converting lactate to pyruvate, and NAD+ to NADH, when oxygen is abundant. NAD 233-237 lactate dehydrogenase A Homo sapiens 0-4 31035592-3 2019 LDHA has a higher affinity for pyruvate, preferentially converting pyruvate to lactate, and NADH to NAD+ in anaerobic conditions, whereas LDHB possess a higher affinity for lactate, preferentially converting lactate to pyruvate, and NAD+ to NADH, when oxygen is abundant. NAD 241-245 lactate dehydrogenase A Homo sapiens 0-4 7630349-8 1995 These findings suggest that the disease severity in our patients may be related to the degree of NADH reoxidation by glycerol 3-phosphate dehydrogenase substituting for LDH. NAD 97-101 lactate dehydrogenase A Homo sapiens 169-172 34725423-1 2021 Lactate dehydrogenase (LDH) catalyses the conversion of pyruvate to lactate and NADH to NAD+; it has two isoforms, LDHA and LDHB. NAD 80-84 lactate dehydrogenase A Homo sapiens 115-119 34725423-1 2021 Lactate dehydrogenase (LDH) catalyses the conversion of pyruvate to lactate and NADH to NAD+; it has two isoforms, LDHA and LDHB. NAD 88-92 lactate dehydrogenase A Homo sapiens 115-119 32647171-4 2020 LDHA binds to NADH and promotes reactive oxygen species (ROS) to induce catabolic changes through stabilization of IkappaB-zeta, a critical pro-inflammatory mediator in chondrocytes. NAD 14-18 lactate dehydrogenase A Homo sapiens 0-4 31035592-3 2019 LDHA has a higher affinity for pyruvate, preferentially converting pyruvate to lactate, and NADH to NAD+ in anaerobic conditions, whereas LDHB possess a higher affinity for lactate, preferentially converting lactate to pyruvate, and NAD+ to NADH, when oxygen is abundant. NAD 92-96 lactate dehydrogenase A Homo sapiens 0-4 31035592-3 2019 LDHA has a higher affinity for pyruvate, preferentially converting pyruvate to lactate, and NADH to NAD+ in anaerobic conditions, whereas LDHB possess a higher affinity for lactate, preferentially converting lactate to pyruvate, and NAD+ to NADH, when oxygen is abundant. NAD 100-104 lactate dehydrogenase A Homo sapiens 0-4 30209241-2 2018 Lactate dehydrogenase A (LDHA) has a key role in aerobic glycolysis (the Warburg effect) through regeneration of the electron acceptor NAD+ and is widely regarded as a desirable target for cancer therapeutics. NAD 135-139 lactate dehydrogenase A Homo sapiens 25-29 29194006-5 2018 Kinetic characterization of the fusion GST-hLDHA protein toward GSH and NADH, suggested retention of functional activities of GST and hLDHA in fused protein as indicated by the kinetic parameters km and kcat/km. NAD 72-76 lactate dehydrogenase A Homo sapiens 43-48 29194006-5 2018 Kinetic characterization of the fusion GST-hLDHA protein toward GSH and NADH, suggested retention of functional activities of GST and hLDHA in fused protein as indicated by the kinetic parameters km and kcat/km. NAD 72-76 lactate dehydrogenase A Homo sapiens 134-139 25664730-1 2015 Lactate dehydrogenase (LDH) is an essential metabolic enzyme that catalyzes the interconversion of pyruvate and lactate using NADH/NAD(+) as a co-substrate. NAD 126-130 lactate dehydrogenase A Homo sapiens 23-26 26114812-7 2015 In Raji cells exposed to compound 1 we evidenced the occurrence of effects usually observed in cancer cells after LDH-A inhibition: reduced lactate production and NAD/NADH ratio, apoptosis. NAD 163-166 lactate dehydrogenase A Homo sapiens 114-119 26114812-7 2015 In Raji cells exposed to compound 1 we evidenced the occurrence of effects usually observed in cancer cells after LDH-A inhibition: reduced lactate production and NAD/NADH ratio, apoptosis. NAD 167-171 lactate dehydrogenase A Homo sapiens 114-119 28950656-1 2017 Several human cancers including the breast display elevated expression of Lactate dehydrogenase-A (LDH-A), the enzyme that converts pyruvate to lactate and oxidizes NADH to NAD+. NAD 165-169 lactate dehydrogenase A Homo sapiens 74-97 28950656-1 2017 Several human cancers including the breast display elevated expression of Lactate dehydrogenase-A (LDH-A), the enzyme that converts pyruvate to lactate and oxidizes NADH to NAD+. NAD 165-169 lactate dehydrogenase A Homo sapiens 99-104 28950656-1 2017 Several human cancers including the breast display elevated expression of Lactate dehydrogenase-A (LDH-A), the enzyme that converts pyruvate to lactate and oxidizes NADH to NAD+. NAD 173-177 lactate dehydrogenase A Homo sapiens 74-97 28950656-1 2017 Several human cancers including the breast display elevated expression of Lactate dehydrogenase-A (LDH-A), the enzyme that converts pyruvate to lactate and oxidizes NADH to NAD+. NAD 173-177 lactate dehydrogenase A Homo sapiens 99-104 28525376-10 2017 Addition of NAD+ re-stabilized LDHA and reversed riluzole induced cell death. NAD 12-16 lactate dehydrogenase A Homo sapiens 31-35 26085945-2 2015 Full-atom models of lactate dehydrogenase A (in complex with NADH and in the apo form) have been generated to enable structure-based design of novel inhibitors competing with pyruvate and NADH. NAD 61-65 lactate dehydrogenase A Homo sapiens 20-43 26085945-2 2015 Full-atom models of lactate dehydrogenase A (in complex with NADH and in the apo form) have been generated to enable structure-based design of novel inhibitors competing with pyruvate and NADH. NAD 188-192 lactate dehydrogenase A Homo sapiens 20-43 25664730-1 2015 Lactate dehydrogenase (LDH) is an essential metabolic enzyme that catalyzes the interconversion of pyruvate and lactate using NADH/NAD(+) as a co-substrate. NAD 131-137 lactate dehydrogenase A Homo sapiens 23-26 25664730-4 2015 The X-ray crystal structures of LDHA in complex with each inhibitor were determined; both inhibitors bind to a site overlapping with the NADH-binding site. NAD 137-141 lactate dehydrogenase A Homo sapiens 32-36 25664730-5 2015 Further, an apo LDHA crystal structure solved in a new space group is reported, as well as a complex with both NADH and the substrate analogue oxalate bound in seven of the eight molecules and an oxalate only bound in the eighth molecule in the asymmetric unit. NAD 111-115 lactate dehydrogenase A Homo sapiens 16-20 26246802-1 2015 Lactate dehydrogenase A (LDHA) is the enzyme that converts pyruvate to lactate and oxidizes the reduced form of nicotinamide adenine dinucleotide (NADH) to NAD+. NAD 112-145 lactate dehydrogenase A Homo sapiens 0-23 26246802-1 2015 Lactate dehydrogenase A (LDHA) is the enzyme that converts pyruvate to lactate and oxidizes the reduced form of nicotinamide adenine dinucleotide (NADH) to NAD+. NAD 112-145 lactate dehydrogenase A Homo sapiens 25-29 26246802-1 2015 Lactate dehydrogenase A (LDHA) is the enzyme that converts pyruvate to lactate and oxidizes the reduced form of nicotinamide adenine dinucleotide (NADH) to NAD+. NAD 147-151 lactate dehydrogenase A Homo sapiens 0-23 26246802-1 2015 Lactate dehydrogenase A (LDHA) is the enzyme that converts pyruvate to lactate and oxidizes the reduced form of nicotinamide adenine dinucleotide (NADH) to NAD+. NAD 147-151 lactate dehydrogenase A Homo sapiens 25-29 26246802-1 2015 Lactate dehydrogenase A (LDHA) is the enzyme that converts pyruvate to lactate and oxidizes the reduced form of nicotinamide adenine dinucleotide (NADH) to NAD+. NAD 156-160 lactate dehydrogenase A Homo sapiens 0-23 26246802-1 2015 Lactate dehydrogenase A (LDHA) is the enzyme that converts pyruvate to lactate and oxidizes the reduced form of nicotinamide adenine dinucleotide (NADH) to NAD+. NAD 156-160 lactate dehydrogenase A Homo sapiens 25-29 25918543-5 2015 Theoretical molecular docking studies of hLDH-A indicate that PGG acts through competitive binding at the NADH cofactor site, effects confirmed by functional enzyme studies where the IC50 = 27.32 nM was reversed with increasing concentration of NADH. NAD 106-110 lactate dehydrogenase A Homo sapiens 41-47 25918543-5 2015 Theoretical molecular docking studies of hLDH-A indicate that PGG acts through competitive binding at the NADH cofactor site, effects confirmed by functional enzyme studies where the IC50 = 27.32 nM was reversed with increasing concentration of NADH. NAD 245-249 lactate dehydrogenase A Homo sapiens 41-47 23307072-6 2013 The addition of lactic acid rescued and knockdown of LDH-A replicated the effects of [NAD(H)] on motility. NAD 86-92 lactate dehydrogenase A Homo sapiens 53-58 24819061-0 2014 Identification of LDH-A as a therapeutic target for cancer cell killing via (i) p53/NAD(H)-dependent and (ii) p53-independent pathways. NAD 84-90 lactate dehydrogenase A Homo sapiens 18-23 25037916-2 2014 Biochemical and surface plasmon resonance experiments performed with a screening hit (LDHA IC50=1.7 muM) indicated that the compound specifically associated with human LDHA in a manner that required simultaneous binding of the NADH co-factor. NAD 227-231 lactate dehydrogenase A Homo sapiens 86-90 25037916-2 2014 Biochemical and surface plasmon resonance experiments performed with a screening hit (LDHA IC50=1.7 muM) indicated that the compound specifically associated with human LDHA in a manner that required simultaneous binding of the NADH co-factor. NAD 227-231 lactate dehydrogenase A Homo sapiens 168-172 24819061-2 2014 The enzyme lactate dehydrogenase-A (LDH-A) is key to cancer"s glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD(+)) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. NAD 115-148 lactate dehydrogenase A Homo sapiens 11-34 24819061-2 2014 The enzyme lactate dehydrogenase-A (LDH-A) is key to cancer"s glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD(+)) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. NAD 115-148 lactate dehydrogenase A Homo sapiens 36-41 24819061-2 2014 The enzyme lactate dehydrogenase-A (LDH-A) is key to cancer"s glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD(+)) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. NAD 150-156 lactate dehydrogenase A Homo sapiens 11-34 24819061-2 2014 The enzyme lactate dehydrogenase-A (LDH-A) is key to cancer"s glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD(+)) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. NAD 150-156 lactate dehydrogenase A Homo sapiens 36-41 24819061-2 2014 The enzyme lactate dehydrogenase-A (LDH-A) is key to cancer"s glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD(+)) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. NAD 171-204 lactate dehydrogenase A Homo sapiens 11-34 24819061-2 2014 The enzyme lactate dehydrogenase-A (LDH-A) is key to cancer"s glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD(+)) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. NAD 171-204 lactate dehydrogenase A Homo sapiens 36-41 24819061-2 2014 The enzyme lactate dehydrogenase-A (LDH-A) is key to cancer"s glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD(+)) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. NAD 206-210 lactate dehydrogenase A Homo sapiens 11-34 24819061-2 2014 The enzyme lactate dehydrogenase-A (LDH-A) is key to cancer"s glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD(+)) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. NAD 206-210 lactate dehydrogenase A Homo sapiens 36-41 24819061-7 2014 Thus, LDH-A silencing by RNAi, or its inhibition using a small-molecule inhibitor, resulted in a p53-dependent increase in the cancer cell ratio of NADH:NAD(+). NAD 148-152 lactate dehydrogenase A Homo sapiens 6-11 24819061-7 2014 Thus, LDH-A silencing by RNAi, or its inhibition using a small-molecule inhibitor, resulted in a p53-dependent increase in the cancer cell ratio of NADH:NAD(+). NAD 153-159 lactate dehydrogenase A Homo sapiens 6-11 24819061-12 2014 To summarise, this work indicates two distinct mechanisms by which suppressing LDH-A could potentially be used to kill cancer cells selectively, (i) through induction of apoptosis, irrespective of cancer cell p53 status and (ii) as a part of a combinatorial approach with redox-sensitive anticancer drugs via a novel p53/NAD(H)-dependent mechanism. NAD 321-327 lactate dehydrogenase A Homo sapiens 79-84 24816116-1 2014 Lactate dehydrogenase A (LDH-A) is a key enzyme in anaerobic respiration that is predominantly found in skeletal muscle and catalyses the reversible conversion of pyruvate to lactate in the presence of NADH. NAD 202-206 lactate dehydrogenase A Homo sapiens 0-23 24816116-1 2014 Lactate dehydrogenase A (LDH-A) is a key enzyme in anaerobic respiration that is predominantly found in skeletal muscle and catalyses the reversible conversion of pyruvate to lactate in the presence of NADH. NAD 202-206 lactate dehydrogenase A Homo sapiens 25-30 24280423-8 2013 RESULTS: 3-((3-carbamoyl-7-(3,5-dimethylisoxazol-4-yl)-6-methoxyquinolin-4-yl) amino) benzoic acid was identified as an NADH-competitive LDHA inhibitor. NAD 120-124 lactate dehydrogenase A Homo sapiens 137-141 23628333-2 2013 Biochemical, surface plasmon resonance, and saturation transfer difference NMR experiments indicated that the compound specifically associated with human LDHA in a manner that required simultaneous binding of the NADH co-factor. NAD 213-217 lactate dehydrogenase A Homo sapiens 154-158 23237800-2 2013 Binding is prevented by NADH, suggesting that the coenzyme site is involved in the interaction LDH-A/ssDNA. NAD 24-28 lactate dehydrogenase A Homo sapiens 95-100 23237800-3 2013 We recently identified an inhibitor of LDH-A enzymatic activity (Galloflavin, GF) which occupies the NADH site. NAD 101-105 lactate dehydrogenase A Homo sapiens 39-44 23237800-9 2013 Our results suggest that: (i) inhibitors which bind the NADH site can exert their antiproliferative activity not only by blocking aerobic glycolysis but also by causing an inhibition of RNA synthesis independent from the effect on glycolysis; (ii) GF can be a useful tool to study the biological role of LDH-A binding to ssDNA. NAD 56-60 lactate dehydrogenase A Homo sapiens 304-309 22417091-1 2012 Lactate dehydrogenase A (LDHA) catalyzes the conversion of pyruvate to lactate, utilizing NADH as a cofactor. NAD 90-94 lactate dehydrogenase A Homo sapiens 0-23 22417091-1 2012 Lactate dehydrogenase A (LDHA) catalyzes the conversion of pyruvate to lactate, utilizing NADH as a cofactor. NAD 90-94 lactate dehydrogenase A Homo sapiens 25-29 23460848-9 2013 In addition, lactate dehydrogenase A and malate dehydrogenase 1 partially associate with human liver peroxisomes and enzyme activity profiles support the idea that NAD(+) becomes regenerated during fatty acid beta-oxidation by alternative shuttling processes in human peroxisomes involving lactate dehydrogenase and/or malate dehydrogenase. NAD 164-170 lactate dehydrogenase A Homo sapiens 13-36 22052811-6 2012 To determine the mechanism of action, we collected LDH-A and -B inhibition data in competition reactions with pyruvate or NADH and evaluated the results using software for enzyme kinetics analysis. NAD 122-126 lactate dehydrogenase A Homo sapiens 51-63 21969607-0 2011 Tyrosine phosphorylation of lactate dehydrogenase A is important for NADH/NAD(+) redox homeostasis in cancer cells. NAD 69-73 lactate dehydrogenase A Homo sapiens 28-51 21969607-0 2011 Tyrosine phosphorylation of lactate dehydrogenase A is important for NADH/NAD(+) redox homeostasis in cancer cells. NAD 74-80 lactate dehydrogenase A Homo sapiens 28-51 21969607-2 2011 Lactate dehydrogenase A (LDH-A) regulates the last step of glycolysis that generates lactate and permits the regeneration of NAD(+). NAD 125-131 lactate dehydrogenase A Homo sapiens 0-23 21969607-2 2011 Lactate dehydrogenase A (LDH-A) regulates the last step of glycolysis that generates lactate and permits the regeneration of NAD(+). NAD 125-131 lactate dehydrogenase A Homo sapiens 25-30 21969607-6 2011 Phosphorylation at Y10 and Y83 enhances LDH-A activity by enhancing the formation of active, tetrameric LDH-A and the binding of LDH-A substrate NADH, respectively. NAD 145-149 lactate dehydrogenase A Homo sapiens 40-45 21969607-8 2011 Interestingly, cancer cells with stable knockdown of endogenous LDH-A and rescue expression of a catalytic hypomorph LDH-A mutant, Y10F, demonstrate increased respiration through mitochondrial complex I to sustain glycolysis by providing NAD(+). NAD 238-244 lactate dehydrogenase A Homo sapiens 64-69 21969607-8 2011 Interestingly, cancer cells with stable knockdown of endogenous LDH-A and rescue expression of a catalytic hypomorph LDH-A mutant, Y10F, demonstrate increased respiration through mitochondrial complex I to sustain glycolysis by providing NAD(+). NAD 238-244 lactate dehydrogenase A Homo sapiens 117-122 21969607-11 2011 Our findings suggest that tyrosine phosphorylation enhances LDH-A enzyme activity to promote the Warburg effect and tumor growth by regulating the NADH/NAD(+) redox homeostasis, representing an acute molecular mechanism underlying the enhanced lactate production in cancer cells. NAD 147-151 lactate dehydrogenase A Homo sapiens 60-65 21969607-11 2011 Our findings suggest that tyrosine phosphorylation enhances LDH-A enzyme activity to promote the Warburg effect and tumor growth by regulating the NADH/NAD(+) redox homeostasis, representing an acute molecular mechanism underlying the enhanced lactate production in cancer cells. NAD 152-158 lactate dehydrogenase A Homo sapiens 60-65 21332213-5 2011 We have discovered new and efficient N-hydroxyindole-based inhibitors of LDH-A, which are isoform-selective (over LDH-B) and competitive with both the substrate (pyruvate) and the cofactor (NADH). NAD 190-194 lactate dehydrogenase A Homo sapiens 73-78