PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29312595-1 2017 Pyruvate kinase (PK) catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP, a rate-limiting reaction in glycolysis. Pyruvic Acid 60-68 pyruvate kinase M1/2 Homo sapiens 17-19 29393401-8 2018 PKM2 knockdown also resulted in lower glycolytic activities and decreased levels of some intracellular metabolites, such as pyruvate and polyamine; however, it led to elevated levels of reactive oxygen species. Pyruvic Acid 124-132 pyruvate kinase M1/2 Homo sapiens 0-4 29225125-7 2018 Thus, we assumed that combination of TLSC702 with shikonin-a specific inhibitor of pyruvate kinase M2 (PKM2) that acts as a driver of TCA cycle by supplying pyruvate and which is known to be specifically expressed in cancer cells-would have anticancer effects. Pyruvic Acid 83-91 pyruvate kinase M1/2 Homo sapiens 103-107 29182273-1 2017 Pyruvate kinase muscle isoform 2 (PKM2) catalyzes the terminal step in glycolysis, transferring a phosphoryl group from phosphoenolpyruvate to ADP, to produce pyruvate and ATP. Pyruvic Acid 131-139 pyruvate kinase M1/2 Homo sapiens 0-32 29182273-1 2017 Pyruvate kinase muscle isoform 2 (PKM2) catalyzes the terminal step in glycolysis, transferring a phosphoryl group from phosphoenolpyruvate to ADP, to produce pyruvate and ATP. Pyruvic Acid 131-139 pyruvate kinase M1/2 Homo sapiens 34-38 27810895-1 2016 The pyruvate kinase (PK) is a rate-limiting glycolytic enzyme catalyzing the dephosphorylation of phosphoenolpyruvate to pyruvate, yielding one molecule of ATP. Pyruvic Acid 4-12 pyruvate kinase M1/2 Homo sapiens 21-23 27152240-1 2016 Pyruvate kinase is a key enzyme in the glycolytic pathway that converts phosphoenolpyruvate to pyruvate, and the M2 isoform of pyruvate kinase (PKM2) is associated with cancer. Pyruvic Acid 83-91 pyruvate kinase M1/2 Homo sapiens 144-148 25645022-1 2015 Pyruvate kinase isoform M2 (PKM2) converts phosphoenolpyruvate (PEP) to pyruvate and plays an important role in cancer metabolism. Pyruvic Acid 54-62 pyruvate kinase M1/2 Homo sapiens 0-26 25645022-1 2015 Pyruvate kinase isoform M2 (PKM2) converts phosphoenolpyruvate (PEP) to pyruvate and plays an important role in cancer metabolism. Pyruvic Acid 54-62 pyruvate kinase M1/2 Homo sapiens 28-32 24972138-3 2014 Here, we review the pyruvate kinase M2 (PKM2) isoform, a glycolytic enzyme involved in ATP generation and pyruvate production, which plays an essential role in tumor metabolism and growth, and also functions as a protein kinase that phosphorylates histones during genes transcription and chromatin remodeling. Pyruvic Acid 20-28 pyruvate kinase M1/2 Homo sapiens 40-44 25320009-8 2014 PKM2 silencing decreased PK activity, intracellular lactate levels, and conversion of pyruvate to lactate in the same manner as TMZ, and Chk1 silencing blocked the TMZ-induced decrease in PKM2 expression. Pyruvic Acid 86-94 pyruvate kinase M1/2 Homo sapiens 0-4 23576436-1 2013 Pyruvate kinase isoform M2 (PKM2) is an enzyme-catalyzing conversion of phosphoenolpyruvate to pyruvate in the glycolysis pathway. Pyruvic Acid 83-91 pyruvate kinase M1/2 Homo sapiens 0-26 23576436-1 2013 Pyruvate kinase isoform M2 (PKM2) is an enzyme-catalyzing conversion of phosphoenolpyruvate to pyruvate in the glycolysis pathway. Pyruvic Acid 83-91 pyruvate kinase M1/2 Homo sapiens 28-32 22262476-6 2011 Cell growth signals further decrease PKM2 activity, and cells with less active PKM2 use another pathway with separate regulatory properties to convert PEP to pyruvate. Pyruvic Acid 158-166 pyruvate kinase M1/2 Homo sapiens 79-83 23212076-3 2013 Expression of PK type M2 (PKM2) is increased and facilitates lactate production in cancer cells, which determines whether the glucose carbons are degraded to pyruvate and lactate or are channeled into synthetic processes. Pyruvic Acid 158-166 pyruvate kinase M1/2 Homo sapiens 14-24 23212076-3 2013 Expression of PK type M2 (PKM2) is increased and facilitates lactate production in cancer cells, which determines whether the glucose carbons are degraded to pyruvate and lactate or are channeled into synthetic processes. Pyruvic Acid 158-166 pyruvate kinase M1/2 Homo sapiens 26-30 23451252-2 2013 Tumors, in contrast, express the less active PKM2 isoform, which limits pyruvate production and spares glycolytic intermediates for the generation of macromolecules needed for proliferation. Pyruvic Acid 72-80 pyruvate kinase M1/2 Homo sapiens 45-49 23064226-5 2012 This reduction in PKM2 activity shifts cells to a fuel-efficient mode in which more pyruvate is diverted to the mitochondria and more glucose-derived carbon is channelled into serine biosynthesis to support cell proliferation. Pyruvic Acid 84-92 pyruvate kinase M1/2 Homo sapiens 18-22 22433951-2 2012 When the majority of PKM2 molecules are in the highly active tetrameric conformation, glucose is primarily degraded to pyruvate and lactate with the regeneration of energy. Pyruvic Acid 119-127 pyruvate kinase M1/2 Homo sapiens 21-25 22306293-1 2012 Pyruvate kinase isoform M2 (PKM2) is a glycolysis enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate by transferring a phosphate from PEP to ADP. Pyruvic Acid 93-101 pyruvate kinase M1/2 Homo sapiens 0-26 22306293-1 2012 Pyruvate kinase isoform M2 (PKM2) is a glycolysis enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate by transferring a phosphate from PEP to ADP. Pyruvic Acid 93-101 pyruvate kinase M1/2 Homo sapiens 28-32 21673231-7 2011 We observed that increased expression and activity of PKM2 in TPA-treated JB6 P+ cells and pretreatment with succinate or malate/pyruvate suppressed the effects. Pyruvic Acid 129-137 pyruvate kinase M1/2 Homo sapiens 54-58 33473116-3 2021 Herein we found that SUMOylation of the M2 isoform of pyruvate kinase (PKM2), a rate-limiting glycolytic enzyme catalyzing the dephosphorylation of phosphoenolpyruvate to pyruvate, is prevalent in a variety of leukemic cell lines as well as primary samples from patients with leukemia through multiple-reaction monitoring based targeted mass spectrometry analysis. Pyruvic Acid 54-62 pyruvate kinase M1/2 Homo sapiens 71-75 35610475-2 2022 Pyruvate kinase M1/2 (PKM) is an enzyme that catalyzes the last step in glycolysis, which converts phosphoenolpyruvate to pyruvate. Pyruvic Acid 122-130 pyruvate kinase M1/2 Homo sapiens 0-20 35610475-2 2022 Pyruvate kinase M1/2 (PKM) is an enzyme that catalyzes the last step in glycolysis, which converts phosphoenolpyruvate to pyruvate. Pyruvic Acid 122-130 pyruvate kinase M1/2 Homo sapiens 22-25 35048565-2 2022 Pyruvate kinase M2 isoform (PKM2) catalyzes the conversion of phosphoenolpyruvate to pyruvate and regulates the last rate-limiting step of glycolysis. Pyruvic Acid 85-93 pyruvate kinase M1/2 Homo sapiens 0-26 35048565-2 2022 Pyruvate kinase M2 isoform (PKM2) catalyzes the conversion of phosphoenolpyruvate to pyruvate and regulates the last rate-limiting step of glycolysis. Pyruvic Acid 85-93 pyruvate kinase M1/2 Homo sapiens 28-32 35048565-5 2022 The pyruvate produced by PKM2 directly binds to SSRP1, which increases the association of FACT complex with gammaH2AX and subsequently facilitates FACT-mediated chromatin loading of gammaH2AX, ultimately promoting DNA repair and tumor cell survival. Pyruvic Acid 4-12 pyruvate kinase M1/2 Homo sapiens 25-29 35048565-8 2022 The finding demonstrates a novel mechanism by which PKM2-produced pyruvate promotes DNA repair by regulating gammaH2AX loading to chromatin and establishes a critical role of this mechanism in glioblastoma radiation resistance. Pyruvic Acid 66-74 pyruvate kinase M1/2 Homo sapiens 52-56 33526685-5 2021 This was confirmed by using 13C-labeled flux measurements and immunoblotting, revealing that the key regulatory step of phosphoenolpyruvate to pyruvate was inhibited via down-regulation of the tetrameric pyruvate kinase M2 (PKM2). Pyruvic Acid 131-139 pyruvate kinase M1/2 Homo sapiens 204-222 33526685-5 2021 This was confirmed by using 13C-labeled flux measurements and immunoblotting, revealing that the key regulatory step of phosphoenolpyruvate to pyruvate was inhibited via down-regulation of the tetrameric pyruvate kinase M2 (PKM2). Pyruvic Acid 131-139 pyruvate kinase M1/2 Homo sapiens 224-228 34355179-1 2021 Pyruvate kinase M2 (PKM2) catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate. Pyruvic Acid 83-91 pyruvate kinase M1/2 Homo sapiens 0-18 34355179-1 2021 Pyruvate kinase M2 (PKM2) catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate. Pyruvic Acid 83-91 pyruvate kinase M1/2 Homo sapiens 20-24 35189247-4 2022 Out of these, the most prominent genetic alterations (PRKAR-1A, CTNNB1, ZNRF3, TP53, CCNE1 and TERF2 genes) are linked with a glycolytic enzyme pyruvate kinase M2 (PKM2), which converts phosphoenolpyruvate (PEP) to pyruvate in the glycolytic pathway. Pyruvic Acid 215-223 pyruvate kinase M1/2 Homo sapiens 144-162 35189247-4 2022 Out of these, the most prominent genetic alterations (PRKAR-1A, CTNNB1, ZNRF3, TP53, CCNE1 and TERF2 genes) are linked with a glycolytic enzyme pyruvate kinase M2 (PKM2), which converts phosphoenolpyruvate (PEP) to pyruvate in the glycolytic pathway. Pyruvic Acid 215-223 pyruvate kinase M1/2 Homo sapiens 164-168 2813362-11 1989 Since pyruvate kinase is a key enzyme in regulating cellular ADP, ATP, and pyruvate, our findings suggest that p58 may be involved in mediating some of the cellular metabolic effects induced by thyroid hormones. Pyruvic Acid 6-14 pyruvate kinase M1/2 Homo sapiens 111-114 32295714-2 2020 PKM catalyzes the conversion of phosphoenol-pyruvate to pyruvate in glycolytic pathway. Pyruvic Acid 44-52 pyruvate kinase M1/2 Homo sapiens 0-3 33335484-2 2020 Mindful that L-lactate originates only from pyruvate, the question arises as to how can this be sustained in those tissues where pyruvate kinase activity is reduced due to dimerization of PKM2 isoform or inhibited by oxidative/nitrosative stress, posttranslational modifications or mutations, all widely reported findings in the very same cells. Pyruvic Acid 129-137 pyruvate kinase M1/2 Homo sapiens 188-192 33125108-5 2020 Moreover, the effects of BA-NLs were further validated by demonstrating that the key targets of HK2, PFK-1, PEP and PK isoenzyme M2 (PKM2) in glycolysis, and of ACSL1, CPT1a and PEP in fatty acid metabolism, were blocked by BA-NLs, which play key roles in the inhibition of glycolysis and fatty acid-mediated production of pyruvate and lactate. Pyruvic Acid 323-331 pyruvate kinase M1/2 Homo sapiens 116-131 33125108-5 2020 Moreover, the effects of BA-NLs were further validated by demonstrating that the key targets of HK2, PFK-1, PEP and PK isoenzyme M2 (PKM2) in glycolysis, and of ACSL1, CPT1a and PEP in fatty acid metabolism, were blocked by BA-NLs, which play key roles in the inhibition of glycolysis and fatty acid-mediated production of pyruvate and lactate. Pyruvic Acid 323-331 pyruvate kinase M1/2 Homo sapiens 133-137 32641713-6 2020 Oxidized ATM up-regulates GLUT1, PKM2, and PDHa expressions to enhance the uptake of glucose and production of pyruvate rather than lactate products, which facilitates glycolytic flux to mitochondrial pyruvate and citrate, thus resulting in accumulation of cytoplasmic acetyl-CoA instead of the tricarboxylic acid (TCA) cycle by regulating ATP-citrate lyase (ACLY) activity. Pyruvic Acid 111-119 pyruvate kinase M1/2 Homo sapiens 33-37 32295714-2 2020 PKM catalyzes the conversion of phosphoenol-pyruvate to pyruvate in glycolytic pathway. Pyruvic Acid 56-64 pyruvate kinase M1/2 Homo sapiens 0-3 30700935-3 2018 Pyruvate kinase isoform M2 (PKM2), a glycolytic enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate, confers a growth advantage to the tumor cells and enables them to adapt to the tumor microenvironment. Pyruvic Acid 91-99 pyruvate kinase M1/2 Homo sapiens 0-26 32208360-4 2020 Pyruvate kinase M2 (PKM2) is a rate limiting enzyme in the glycolysis which catalyzes phosphoenolpyruvic acid transforming into pyruvate. Pyruvic Acid 128-136 pyruvate kinase M1/2 Homo sapiens 0-18 32208360-4 2020 Pyruvate kinase M2 (PKM2) is a rate limiting enzyme in the glycolysis which catalyzes phosphoenolpyruvic acid transforming into pyruvate. Pyruvic Acid 128-136 pyruvate kinase M1/2 Homo sapiens 20-24 30866966-15 2019 Synergistically upregulated LDHA, PKM2 levels resulted in low levels of pyruvate, as well as poor patient survival. Pyruvic Acid 72-80 pyruvate kinase M1/2 Homo sapiens 34-38 30700935-3 2018 Pyruvate kinase isoform M2 (PKM2), a glycolytic enzyme catalyzing conversion of phosphoenolpyruvate (PEP) to pyruvate, confers a growth advantage to the tumor cells and enables them to adapt to the tumor microenvironment. Pyruvic Acid 91-99 pyruvate kinase M1/2 Homo sapiens 28-32