Gotowa bibliografia na temat „PKM1/PKM2”
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Artykuły w czasopismach na temat "PKM1/PKM2"
Li, Lin, Siyuan Cheng i Xiuping Yu. "The expression of PKM1 and PKM2 in benign and cancerous prostatic tissues." Journal of Clinical Oncology 41, nr 16_suppl (1.06.2023): e17058-e17058. http://dx.doi.org/10.1200/jco.2023.41.16_suppl.e17058.
Pełny tekst źródłaKim, Seong Ho, Ji Hun Wi, HyeRan Gwak, Eun Gyeong Yang i So Yeon Kim. "Single-Cell FISH Analysis Reveals Distinct Shifts in PKM Isoform Populations during Drug Resistance Acquisition". Biomolecules 12, nr 8 (6.08.2022): 1082. http://dx.doi.org/10.3390/biom12081082.
Pełny tekst źródłaVerbrugge, Sander A. J., Sebastian Gehlert, Lian E. M. Stadhouders, Daniel Jacko, Thorben Aussieker, Gerard M. J. de Wit, Ilse S. P. Vogel i in. "PKM2 Determines Myofiber Hypertrophy In Vitro and Increases in Response to Resistance Exercise in Human Skeletal Muscle". International Journal of Molecular Sciences 21, nr 19 (25.09.2020): 7062. http://dx.doi.org/10.3390/ijms21197062.
Pełny tekst źródłaBuneeva, Olga, Arthur Kopylov, Oksana Gnedenko, Marina Medvedeva, Alexander Veselovsky, Alexis Ivanov, Victor Zgoda i Alexei Medvedev. "Proteomic Profiling of Mouse Brain Pyruvate Kinase Binding Proteins: A Hint for Moonlighting Functions of PKM1?" International Journal of Molecular Sciences 24, nr 8 (21.04.2023): 7634. http://dx.doi.org/10.3390/ijms24087634.
Pełny tekst źródłaKurihara-Shimomura, Miyako, Tomonori Sasahira, Chie Nakashima, Hiroki Kuniyasu, Hiroyuki Shimomura i Tadaaki Kirita. "The Multifarious Functions of Pyruvate Kinase M2 in Oral Cancer Cells". International Journal of Molecular Sciences 19, nr 10 (25.09.2018): 2907. http://dx.doi.org/10.3390/ijms19102907.
Pełny tekst źródłaWilliams, Allison Lesher, Vedbar Khadka, Mingxin Tang, Abigail Avelar, Kathryn J. Schunke, Mark Menor i Ralph V. Shohet. "HIF1 mediates a switch in pyruvate kinase isoforms after myocardial infarction". Physiological Genomics 50, nr 7 (1.07.2018): 479–94. http://dx.doi.org/10.1152/physiolgenomics.00130.2017.
Pełny tekst źródłaLee, Yuumi, Yuko Ito, Kohei Taniguchi, Takashi Nuri, SangWoong Lee i Koichi Ueda. "Experimental Study of Warburg Effect in Keloid Nodules: Implication for Downregulation of miR-133b". Plastic and Reconstructive Surgery - Global Open 11, nr 8 (sierpień 2023): e5202. http://dx.doi.org/10.1097/gox.0000000000005202.
Pełny tekst źródłaKuranaga, Yuki, Nobuhiko Sugito, Haruka Shinohara, Takuya Tsujino, Kohei Taniguchi, Kazumasa Komura, Yuko Ito, Tomoyoshi Soga i Yukihiro Akao. "SRSF3, a Splicer of the PKM Gene, Regulates Cell Growth and Maintenance of Cancer-Specific Energy Metabolism in Colon Cancer Cells". International Journal of Molecular Sciences 19, nr 10 (2.10.2018): 3012. http://dx.doi.org/10.3390/ijms19103012.
Pełny tekst źródłaXia, Yong, Xing Wang, Yan Liu, Ellen Shapiro, Herbert Lepor, Moon-Shong Tang, Tung-Tien Sun i Xue-Ru Wu. "PKM2 Is Essential for Bladder Cancer Growth and Maintenance". Cancer Research 82, nr 4 (13.12.2021): 571–85. http://dx.doi.org/10.1158/0008-5472.can-21-0403.
Pełny tekst źródłaGrant, Melissa M. "Pyruvate Kinase, Inflammation and Periodontal Disease". Pathogens 10, nr 7 (22.06.2021): 784. http://dx.doi.org/10.3390/pathogens10070784.
Pełny tekst źródłaRozprawy doktorskie na temat "PKM1/PKM2"
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.
Pełny tekst źródłaDelobelle, Quentin. "Simulations de dynamique moléculaire à haute résolution des isoformes 1 et 2 de la pyruvate kinase musculaire". Electronic Thesis or Diss., Sorbonne université, 2024. http://www.theses.fr/2024SORUS067.
Pełny tekst źródłaIn both normal physiological processes and cancer cell growth, glycolytic metabolism plays a pivotal role. The Pyruvate Kinase Muscle isoforms 1 and 2, denoted PKM1/2, are crucial proteins that regulate this metabolism. Characterizing the structural dynamics of these biomolecules is thus imperative in order to develop new drugs targeting PMK enzymes in tumor cells. To address this, we performed extensive molecular dynamics (MD) simulations of these two proteins at high-resolution. To do so, we employed adaptive sampling techniques coupled with the polarizable AMOEBA force field to understand the conformational flexibility of the enzyme. We propose a high-resolution structural analysis for PKM2 and introduce structural insights for PKM1. We are studying the oligomerization process of the PKM2 enzyme (from monomer to tetramer) while focusing on the structuring of key structural sites, in particular the active site and the binding pocket for Fructose Biphosphate (FBP), a physiological conformational inducer. We also provide data explaining the impact of TEPP-46, a pharmacological activator, on PKM2 structure and their similarity with PKM2 bound to FBP in conformity to biological results. Finally, we propose the first high-resolution MD simulation of the biological active PKM1 and reveal important structural information in link with strong structural similarities with PKM2 when linked to FBP. These findings provide new insights concerning the structural dynamics and key sites structuration during PKM2 oligomerization that could be critical in drug discovery