Relevant bibliographies by topics / Pyruvate kinase M2 (PKM2)

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Academic literature on the topic 'Pyruvate kinase M2 (PKM2)'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Pyruvate kinase M2 (PKM2)"

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Kurihara-Shimomura, Miyako, Tomonori Sasahira, Chie Nakashima, Hiroki Kuniyasu, Hiroyuki Shimomura, and Tadaaki Kirita. "The Multifarious Functions of Pyruvate Kinase M2 in Oral Cancer Cells." International Journal of Molecular Sciences 19, no. 10 (2018): 2907. http://dx.doi.org/10.3390/ijms19102907.

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Head and neck cancers, including oral squamous cell carcinoma (OSCC), are the sixth most common malignancies worldwide. OSCC frequently leads to oral dysfunction, which worsens a patient’s quality of life. Moreover, its prognosis remains poor. Unlike normal cells, tumor cells preferentially metabolize glucose by aerobic glycolysis. Pyruvate kinase (PK) catalyzes the final step in glycolysis, and the transition from PKM1 to PKM2 is observed in many cancer cells. However, little is known about PKM expression and function in OSCC. In this study, we investigated the expression of PKM in OSCC speci
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Sturgill, Eric M., and Monica L. Guzman. "Cytokine Induced Nuclear Localization Of Pyruvate Kinase M2 In Acute Myeloid Leukemia." Blood 122, no. 21 (2013): 5406. http://dx.doi.org/10.1182/blood.v122.21.5406.5406.

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Abstract A common characteristic among nearly all cancers, including leukemia, is the cell’s metabolic proclivity for glycolysis over the more energy efficient process of oxidative phosphorylation (OXPHOS) in the presence of oxygen. This altered state of aerobic glycolysis was observed in tumor cells by Otto Warburg over fifty years ago (Warburg, 1956) and continues to be intensely investigated in hopes of ultimately exploiting this “Warburg effect” in the treatment of cancer (Vander Heiden et al. 2009). Recent studies have revealed that the M2 isoform of the enzyme pyruvate kinase (PKM2) play
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Nayak, Manasa, Nirav Dhanesha, Manish Jain, and Anil Chauhan. "Manipulating Metabolic Plasticity By Targeting Pyruvate Kinase M2 in Platelets Inhibits Arterial Thrombosis." Blood 132, Supplement 1 (2018): 868. http://dx.doi.org/10.1182/blood-2018-99-112704.

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Abstract Background: Most of the cellular responses initiated upon platelet activation are energy consuming. Like normal cells, resting platelets rely primarily on oxidative phosphorylation (OXPHOS) to generate ATP, whereas activated platelets exhibit a high level of aerobic glycolysis (conversion of glucose to lactate in the presence of oxygen, a phenomenon referred to as the Warburg effect in tumor cells) suggesting that metabolic plasticity exists in activated platelets. Although aerobic glycolysis yields less total ATP when compared to OXPHOS, the rate of ATP generation is faster in aerobi
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Xia, Li, Xin-Ran Wang, Ran Wei, Jin-Song Yan, Guo-Qiang Chen, and Ying Lu. "Sumoylation of Pyruvate Kinase M2 Inhibits Myeloid Differentiation in Hematopoietic Cells." Blood 132, Supplement 1 (2018): 3919. http://dx.doi.org/10.1182/blood-2018-99-117899.

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Abstract The pyruvate kinase (PK) is a rate-limiting glycolytic enzyme catalyzing the dephosphorylation of phosphoenolpyruvate to pyruvate. M2 form of PK (PKM2) is expressed during embryogenesis and is the predominant form in tumors of different types. In contrast to the essential role of PKM2 in solid tumors, much less is known about the effects of PKM2 in hematopoietic cells and the development of leukemia. Here we found that PKM2 is modified by small ubiquitin-like modifier 1(SUMO1), which can be reduced by a SUMO1-specific protease SENP1 in hematopoietic cells. SUMOylation induced nuclear
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Su, Yan, Sujuan Guo, Chunyan Liu, et al. "Endometrial pyruvate kinase M2 is essential for decidualization during early pregnancy." Journal of Endocrinology 245, no. 3 (2020): 357–68. http://dx.doi.org/10.1530/joe-19-0553.

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Embryo implantation is essential for normal pregnancy. Decidualization is known to facilitate embryo implantation and maintain pregnancy. Uterine stromal cells undergo transformation into decidual cells after embryo attachment to the endometrium. Pyruvate kinase M2 (PKM2) is a rate limiting enzyme in the glycolysis process which catalyzes phosphoenolpyruvic acid into pyruvate. However, little is known regarding the role of PKM2 during endometrial decidualization. In this study, PKM2 was found to be mainly located in the uterine glandular epithelium and luminal epithelium on day 1 and day 4 of
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Esen, I., Y. Van Sleen, P. Heeringa, A. Boots, and E. Brouwer. "AB0471 ELEVATED EXPRESSION OF PYRUVATE KINASE M2 IN GIANT CELL ARTERITIS." Annals of the Rheumatic Diseases 79, Suppl 1 (2020): 1534.1–1534. http://dx.doi.org/10.1136/annrheumdis-2020-eular.1699.

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Background:Giant Cell Arteritis (GCA) is an inflammatory disease of large and medium vessels. In GCA, expression of interleukin-6 (IL-6), a systemic marker of inflammation, is elevated and it has been shown that treatment with IL-6 receptor blockade (Tocilizumab) is beneficial for GCA patients.1To investigate the role of the IL-6 signaling pathway in GCA pathogenesis in more depth, we focused on the metabolic enzyme Pyruvate Kinase M2 (PKM2). PKM2 may exist as a tetramer, a dimer and/or a monomer in the cell. Tetrameric PKM2 acts as a glycolytic enzyme and catalyzes the last steps of glycolysi
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Goldberg, Michael S., and Phillip A. Sharp. "Pyruvate kinase M2-specific siRNA induces apoptosis and tumor regression." Journal of Experimental Medicine 209, no. 2 (2012): 217–24. http://dx.doi.org/10.1084/jem.20111487.

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The development of cancer-specific therapeutics has been limited because most healthy cells and cancer cells depend on common pathways. Pyruvate kinase (PK) exists in M1 (PKM1) and M2 (PKM2) isoforms. PKM2, whose expression in cancer cells results in aerobic glycolysis and is suggested to bestow a selective growth advantage, is a promising target. Because many oncogenes impart a common alteration in cell metabolism, inhibition of the M2 isoform might be of broad applicability. We show that several small interfering (si) RNAs designed to target mismatches between the M2 and M1 isoforms confer s
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Sharma, Pankaj. "Molecular docking analysis of pyruvate kinase M2 with a potential inhibitor from the ZINC database." Bioinformation 17, no. 1 (2021): 139–46. http://dx.doi.org/10.6026/97320630017139.

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The pyruvate kinase M2 isoform (PKM2) is linked with cancer. Therefore, it is of interest to document the molecular docking analysis of Pyruvate Kinase M2 (PDB ID: 4G1N) with potential activators from the ZINC database. Thus, we document the optimal molecular docking features of a compound having ID ZINC000034285235 with PKM2 for further consideration.
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Choi, Hae-Seul, Chang-Zhu Pei, Jun-Hyeok Park, et al. "Protein Stability of Pyruvate Kinase Isozyme M2 Is Mediated by HAUSP." Cancers 12, no. 6 (2020): 1548. http://dx.doi.org/10.3390/cancers12061548.

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The ubiquitin–proteasome system (UPS) is responsible for proteasomal degradation, regulating the half-life of the protein. Deubiquitinating enzymes (DUBs) are components of the UPS and inhibit degradation by removing ubiquitins from protein substrates. Herpesvirus-associated ubiquitin-specific protease (HAUSP) is one such deubiquitinating enzyme and has been closely associated with tumor development. In a previous study, we isolated putative HAUSP binding substrates by two-dimensional electrophoresis (2-DE) and identified them by matrix-assisted laser desorption-ionization time-of-flight mass
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Rathod, Bhagyashri, Shivam Chak, Sagarkumar Patel, and Amit Shard. "Tumor pyruvate kinase M2 modulators: a comprehensive account of activators and inhibitors as anticancer agents." RSC Medicinal Chemistry 12, no. 7 (2021): 1121–41. http://dx.doi.org/10.1039/d1md00045d.

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Dissertations / Theses on the topic "Pyruvate kinase M2 (PKM2)"

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Gao, Xueliang. "Nuclear Pyruvate Kinase M2 Functional Study in Cancer Cells." Digital Archive @ GSU, 2010. http://digitalarchive.gsu.edu/biology_diss/89.

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Cancer cells take more glucose to provide energy and phosphoryl intermediates for cancer progression. Meanwhile, energy-provider function of mitochondria in cancer cells is disrupted. This phenomenon is so-called Warburg effect, which is discovered over eighty years ago. The detail mechanisms for Warburg effect are not well defined. How glycolytic enzymes contribute to cancer progression is not well known. PKM2 is a glycolytic enzyme dominantly localized in the cytosol, catalyzing the production of ATP from PEP. In this study, we discovered that there were more nuclear PKM2 expressed in highly
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Bahr, Brigham L. "Different Expression of Placental Pyruvate Kinase M2 in Normal, Preeclamptic, and Intrauterine Growth Restriction Pregnancies." BYU ScholarsArchive, 2014. https://scholarsarchive.byu.edu/etd/3901.

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This thesis will be organized into two chapters discussing the placental expression of two proteins, pyruvate kinase M2 (PKM2) and heat shock protein 27 (HSP 27), in human placentas. Understanding the mechanisms of placental metabolism in healthy and diseased placentas helps us understand how placenta disorders occur and how we can treat these disorders. The goal is to investigate these proteins to gain an understanding of their roles in placental disorders and help decrease maternal and fetal mortality rates. Chapter one covers the background of pyruvate kinase M2 (PKM2) in cancer and embryon
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Kimball, Rebecca Lutz. "The Role of Hypoxia on Pyruvate Kinase M2, mammalian Target of Rapamycin, Mitochondrial Function, and Cell Invasion in the Trophoblast." BYU ScholarsArchive, 2016. https://scholarsarchive.byu.edu/etd/5723.

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This thesis will be organized into two chapters discussing the role of hypoxia in the human placenta. The goal of this thesis is to characterize pyruvate kinase M2, mammalian target of rapamycin, mitochondrial function, and cell invasion in hypoxic conditions in the trophoblast. Understanding the mechanisms of placental metabolism can lead to further treatments for placental diseases. Chapter one covers the background of intrauterine growth restriction, hypoxia, placental metabolism, and pyruvate kinase M2 (PKM2). Little is currently understood about the role of the mitochondria in placental d
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Mitchell, Rosie. "The regulation of human M2 pyruvate kinase." Thesis, University of Edinburgh, 2015. http://hdl.handle.net/1842/21690.

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Pyruvate kinase catalyses the final step in glycolysis and is responsible for net ATP production. There are four pyruvate kinase isoforms expressed in humans; LPYK, RPYK, M1PYK and M2PYK. The allosteric enzyme M2PYK plays an important role in cancer cell metabolism and is subject to complex regulation by numerous naturally occurring small-molecule metabolites. Post-translational modifications have also been found to play a key role in the regulation of M2PYK, among these cysteine oxidation. This thesis describes the production and characterisation of M2PYK cysteine point mutants in order to in
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Hasan, Diya [Verfasser]. "Hypoxic regulation and selective silencing of pyruvate kinase isoforms PKM1 and PKM2 by siRNA / Diya Hasan." Gießen : Universitätsbibliothek, 2012. http://d-nb.info/1064024580/34.

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Dayton, Talya Lucia. "Examining the roles of the pyruvate kinase isoforms, PKMI1 and PKM2, in systemic metabolism and tumor development." Thesis, Massachusetts Institute of Technology, 2016. http://hdl.handle.net/1721.1/104176.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2016.<br>Cataloged from PDF version of thesis. Vita.<br>Includes bibliographical references.<br>Alternative splicing of the Pkm gene product generates the PKM1 and PKM2 isoforms of pyruvate kinase, and PKM2 expression is closely linked to embryogenesis, tissue regeneration, and cancer. PKM1 expression, on the other hand, is restricted mostly to skeletal muscle, heart, and brain. To interrogate the functional requirement for PKM1 or PKM2 during development and tissue homeostasis, we generated germline PKM1 (Pkm1-/-) o
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Kumar, Y. "Clinical review and experimental evaluation of tumour M2-pyruvate kinase in pancreatic cancer." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/17418/.

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The treatment of pancreatic cancer is challenging. Patients are often beyond curative surgical therapy and palliative treatment with chemotherapy provides limited benefit. New markers of cancer activity and therapeutic targets are required. This thesis has firstly reviewed the available literature on Tumour M2-PK, a dimeric form of M2 isoenzyme of pyruvate kinase, in GI cancer and carried out a meta-analysis of the clinical data on pancreatic cancer. Experimental work evaluated the measurement of M2-pyruvate kinase in human pancreatic cancer cell lines with altered microenvironment (hypoxia, a
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Zaccaro, Cristina <1987&gt. "Evaluation of Tumor M2 Pyruvate Kinase and Endocannabinoid System Expression in Colorectal Preneoplastic and Neoplastic Lesions: Possible Use for non Invasive Diagnosis." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2016. http://amsdottorato.unibo.it/7357/.

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Colorectal cancer (CRC) is a multistep process that goes through adenoma-carcinoma sequence. Many forms of CRC may be prevented by routine control, which can detect precancerous neoplasm before they undergo malignant transformation (123). For this reasons we hypothesized that a combination of simple faecal tests, may help to identify patients with higher risk of adenomas and/or CRC. The aim of this study is to clarify whether FOBT, enzyme Tumor M2-PK and endocannabinoid system molecules (CB1, CB2, FAAH), could represent diagnostic non-invasive markers, alone or in combination, for early diagno
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Lavik, Andrew R. "The Role of Inositol 1,4,5-Trisphosphate Receptor-Interacting Proteins in Regulating Inositol 1,4,5-Trisphosphate Receptor-Dependent Calcium Signals and Cell Survival." Case Western Reserve University School of Graduate Studies / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=case1448532307.

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Dharaneeswaran, Harita. "Pyruvate kinase M2 (PKM2), a glycolytic enzyme, is required to maintain vascular barrier function." Thesis, 2017. https://hdl.handle.net/2144/23713.

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RATIONALE - Metabolic enzymes, like pyruvate kinase M2 (PKM2), play an essential role in altering endothelial cell (EC) phenotypes and behavior. Extensive research has elucidated the function of PKM2, a rate-limiting glycolytic enzyme, in the context of cancer cells and in activated immune cells, but its role in EC biology is only newly emerging. Recent findings show PKM2 acts as a key regulator of angiogenesis. Where exogenous circulating PKM2 induces EC cell proliferation leading to increased tumor angiogenesis and growth. Also, PKM2 deficient ECs exhibit decreased proliferation and migratio
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Book chapters on the topic "Pyruvate kinase M2 (PKM2)"

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Prakasam, Gopinath, Mohammad Askandar Iqbal, Vibhor Gupta, Bhupender Kumar, and Rameshwar N. K. Bamezai. "Pyruvate Kinase M2." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101893.

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Prakasam, Gopinath, Mohammad Askandar Iqbal, Vibhor Gupta, Bhupender Kumar, and Rameshwar N. K. Bamezai. "Pyruvate Kinase M2." In Encyclopedia of Signaling Molecules. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101893-1.

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Gupta, Vibhor, Mohd Askandar Iqbal, Bhupender Kumar, and Rameshwar N. K. Bamezai. "Pyruvate Kinase M2: A Metabolic Tuner." In Tumor Cell Metabolism. Springer Vienna, 2015. http://dx.doi.org/10.1007/978-3-7091-1824-5_6.

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Eigenbrodt, E., S. Mazurek, and R. R. Friis. "Double role of pyruvate kinase type M2 in the regulation of phosphometabolite pools." In Cell Growth and Oncogenesis. Birkhäuser Basel, 1998. http://dx.doi.org/10.1007/978-3-0348-8950-6_2.

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Mazurek, S. "Pyruvate Kinase Type M2: A Key Regulator Within the Tumour Metabolome and a Tool for Metabolic Profiling of Tumours." In Oncogenes Meet Metabolism. Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/2789_2008_091.

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Conference papers on the topic "Pyruvate kinase M2 (PKM2)"

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Lim, Jae Yun, Sun Och Yoon, Soon Won Hong, Jong Won Kim, Seung Ho Choi, and Jae Yong Cho. "Abstract 4540: Pyruvate kinase M2 (PKM2) associated with poor prognosis in gastric signet ring cell carcinoma." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4540.

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Mishra, A., A. Jaiswal, N. Stahr, S. Makhija, M. Sandey, and A. Suryawanshi. "Pyruvate Kinase M2 (PKM2) - Mediated Glycolytic Upregulation in Lung CD11c+ Cells Facilitates Alternaria-Induced Acute Airway Inflammation." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a1286.

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Biyik-Sit, Rumeysa, Traci Kruer, Susan M. Dougherty, et al. "Abstract 4933: Nuclear Pyruvate Kinase M2 (PKM2) contributes to PSAT1-mediated cell migration in EGFR-activated lung cancer cells." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-4933.

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Sit, Rumeysa B., Traci Kruer, James Bradley, Michael Merchant, John O. Trent, and Brian F. Clem. "Abstract 3563: Potential role for a phosphoserine aminotransferase 1 and pyruvate kinase M2 (PSAT1:PKM2) functional interaction in lung cancer cells." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3563.

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Sturgill, Eric M., and Monica L. Guzman. "Abstract 4793: The M2 isoform of pyruvate kinase (PKM2) contributes to leukemia stem cell persistence by maintaining oxidative homeostasis and promoting glycolysis." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4793.

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Patel, Chirag B., Corinne Beinat, Yuanyang Xie, Edwin Chang, and Sanjiv S. Gambhir. "Abstract 5271: Molecular imaging of pyruvate kinase M2 (PKM2) with [18F]DASA-23 detects temozolomide- and tumor treating fields (TTFields)-induced changes in glycolysis in glioblastoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-5271.

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Patel, Chirag B., Corinne Beinat, Yuanyang Xie, Edwin Chang, and Sanjiv S. Gambhir. "Abstract 5271: Molecular imaging of pyruvate kinase M2 (PKM2) with [18F]DASA-23 detects temozolomide- and tumor treating fields (TTFields)-induced changes in glycolysis in glioblastoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-5271.

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Rai, N., T. Novoyatleva, N. Weissmann, H. A. Ghofrani, R. T. Schermuly, and W. Seeger. "Role of Pyruvate Kinase 2 Muscle (PKM2) Oligomerization in Pulmonary Arterial Hypertension." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5278.

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Xu, Zhi, Angela Liu, Nikki Lee, Jinfei Chen, and John M. Luk. "Abstract 3352: miR-122 targets pyruvate kinase M2 and affects metabolism of hepatocellular carcinoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3352.

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Tan, S., EJ Forty, PF Durrenberger, RJ McAnulty, RC Chambers, and PF Mercer. "P50 Localisation of the glycolytic isozyme, pyruvate kinase m2 in the lung of idiopathic pulmonary fibrosis." In British Thoracic Society Winter Meeting 2017, QEII Centre Broad Sanctuary Westminster London SW1P 3EE, 6 to 8 December 2017, Programme and Abstracts. BMJ Publishing Group Ltd and British Thoracic Society, 2017. http://dx.doi.org/10.1136/thoraxjnl-2017-210983.192.

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