Скачать с ютуб Эффекторы G-белка: система фосфолипазы С. в хорошем качестве

Эффекторы G-белка: система фосфолипазы С.

В видео рассматривается система фосфолипазы С, разбираются вторичные посредники – инозитол-3-фосфат и диациглицерол – и описываются их эффекты, рассматриваются функции кальмодулина и протеинкиназы С. Поддержать автора: https://yoomoney.ru/to/410014822609774 ОСНОВНОЙ ИСТОЧНИК: Boron, Walter F., Boulpaep, Emile L. (Eds.) (2009) Medical physiology: a cellular and molecular approach. Philadelphia, PA: Saunders/Elsevier ТАКЖЕ ИСПОЛЬЗОВАЛАСЬ ИНФОРМАЦИЯ ИЗ ИСТОЧНИКОВ: Xia Z, Storm DR. The role of calmodulin as a signal integrator for synaptic plasticity. Nat Rev Neurosci. 2005;6(4):267-76. doi: 10.1038/nrn1647. Harper MT, Poole AW. Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation. J Thromb Haemost. 2010 Mar;8(3):454-62. doi: 10.1111/j.1538-7836.2009.03722.x. Khalil RA. Regulation of Vascular Smooth Muscle Function. San Rafael (CA): Morgan & Claypool Life Sciences; 2010. Chapter 6, Protein Kinase C. Féraille E, Carranza ML, Buffin-Meyer B, Rousselot M, Doucet A, Favre H. Protein kinase C-dependent stimulation of Na(+)-K(+)-ATP epsilon in rat proximal convoluted tubules. Am J Physiol. 1995;268(5 Pt 1):C1277-83. doi: 10.1152/ajpcell.1995.268.5.C1277. Farese RV, Sajan MP. Metabolic functions of atypical protein kinase C: "good" and "bad" as defined by nutritional status. Am J Physiol Endocrinol Metab. 2010;298(3):E385-E394. doi:10.1152/ajpendo.00608.2009 Newton AC. Protein kinase C: perfectly balanced. Crit Rev Biochem Mol Biol. 2018;53(2):208-230. doi: 10.1080/10409238.2018.1442408. Black AR, Black JD. Protein kinase C signaling and cell cycle regulation. Front Immunol. 2013 17;3:423. doi: 10.3389/fimmu.2012.00423. Kolczynska K, Loza-Valdes A, Hawro I, Sumara G. Diacylglycerol-evoked activation of PKC and PKD isoforms in regulation of glucose and lipid metabolism: a review. Lipids Health Dis. 2020;19(1):113. doi: 10.1186/s12944-020-01286-8 Mabuchi Y, Mabuchi K, Stafford WF, Grabarek Z. Modular structure of smooth muscle Myosin light chain kinase: hydrodynamic modeling and functional implications. Biochemistry. 2010;49(13):2903-2917. doi:10.1021/bi901963e Essen LO, Perisic O, Cheung R, Katan M, Williams RL. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature. 1996;380(6575):595-602. doi:10.1038/380595a0 Leonard TA, Różycki B, Saidi LF, Hummer G, Hurley JH. Crystal structure and allosteric activation of protein kinase C βII. Cell. 2011;144(1):55-66. doi:10.1016/j.cell.2010.12.013 Mika D, Richter W, Conti M. A CaMKII/PDE4D negative feedback regulates cAMP signaling. Proc Natl Acad Sci U S A. 2015;112(7):2023-2028. doi:10.1073/pnas.1419992112 Brushia RJ, Walsh DA. Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure. Front Biosci. 1999;4:D618-D641. 1999. doi:10.2741/brushia Heinz D. W., Essen L. O., and Williams R. L.. 1998. Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C. J. Mol. Biol. 275:635–650. Nitsche, J., Josts, I., Heidemann, J. et al. Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1, 206 (2018). https://doi.org/10.1038/s42003-018-02... Kang JH, Toita R, Kim CW, Katayama Y. Protein kinase C (PKC) isozyme-specific substrates and their design. Biotechnol Adv. 2012;30(6):1662-1672. doi:10.1016/j.biotechadv.2012.07.004