Littérature scientifique sur le sujet « AKT PHOSPHORYLATION »
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Articles de revues sur le sujet "AKT PHOSPHORYLATION"
Ono, Hiraku, Hideyuki Sakoda, Midori Fujishiro, Motonobu Anai, Akifumi Kushiyama, Yasushi Fukushima, Hideki Katagiri et al. « Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways ». American Journal of Physiology-Cell Physiology 293, no 5 (novembre 2007) : C1576—C1585. http://dx.doi.org/10.1152/ajpcell.00570.2006.
Texte intégralHausenloy, Derek J., A. Tsang, Mihaela M. Mocanu et Derek M. Yellon. « Ischemic preconditioning protects by activating prosurvival kinases at reperfusion ». American Journal of Physiology-Heart and Circulatory Physiology 288, no 2 (février 2005) : H971—H976. http://dx.doi.org/10.1152/ajpheart.00374.2004.
Texte intégralAshcroft, Margaret, Robert L. Ludwig, Douglas B. Woods, Terry D. Copeland, H. Oliver Weber, Elizabeth J. MacRae et Karen H. Vousden. « Phosphorylation of HDM2 by Akt ». Oncogene 21, no 13 (mars 2002) : 1955–62. http://dx.doi.org/10.1038/sj.onc.1205276.
Texte intégralKim, Albert H., Gus Khursigara, Xuan Sun, Thomas F. Franke et Moses V. Chao. « Akt Phosphorylates and Negatively Regulates Apoptosis Signal-Regulating Kinase 1 ». Molecular and Cellular Biology 21, no 3 (1 février 2001) : 893–901. http://dx.doi.org/10.1128/mcb.21.3.893-901.2001.
Texte intégralRomic, Snjezana, Snezana Tepavcevic, Zorica Zakula, Tijana Milosavljevic, Mojca Stojiljkovic, Maja Zivkovic, Milan Popovic, Aleksandra Stankovic et Goran Koricanac. « Does oestradiol attenuate the damaging effects of a fructose-rich diet on cardiac Akt/endothelial nitric oxide synthase signalling ? » British Journal of Nutrition 109, no 11 (16 octobre 2012) : 1940–48. http://dx.doi.org/10.1017/s0007114512004114.
Texte intégralDunn, Ewan F., Rachel Fearns et John H. Connor. « Akt Inhibitor Akt-IV Blocks Virus Replication through an Akt-Independent Mechanism ». Journal of Virology 83, no 22 (9 septembre 2009) : 11665–72. http://dx.doi.org/10.1128/jvi.01092-09.
Texte intégralKim, Ji-Eun, Duk-Shin Lee, Tae-Hyun Kim, Hana Park et Tae-Cheon Kang. « Distinct Roles of CK2- and AKT-Mediated NF-κB Phosphorylations in Clasmatodendrosis (Autophagic Astroglial Death) within the Hippocampus of Chronic Epilepsy Rats ». Antioxidants 12, no 5 (28 avril 2023) : 1020. http://dx.doi.org/10.3390/antiox12051020.
Texte intégralXiang, Binggang, Guoying Zhang, Junling Liu, Andrew J. Morris, Susan S. Smyth, T. Kent Gartner et Zhenyu Li. « A novel P2Y12-Independent Signaling Pathway Mediating Akt Phosphorylation In Response to Thrombin Receptors ». Blood 116, no 21 (19 novembre 2010) : 3191. http://dx.doi.org/10.1182/blood.v116.21.3191.3191.
Texte intégralKim, Soochong, Jianguo Jin et Satya P. Kunapuli. « Relative contribution of G-protein-coupled pathways to protease-activated receptor-mediated Akt phosphorylation in platelets ». Blood 107, no 3 (1 février 2006) : 947–54. http://dx.doi.org/10.1182/blood-2005-07-3040.
Texte intégralGayer, Christopher P., Lakshmi S. Chaturvedi, Shouye Wang, Brittany Alston, Thomas L. Flanigan et Marc D. Basson. « Delineating the signals by which repetitive deformation stimulates intestinal epithelial migration across fibronectin ». American Journal of Physiology-Gastrointestinal and Liver Physiology 296, no 4 (avril 2009) : G876—G885. http://dx.doi.org/10.1152/ajpgi.90648.2008.
Texte intégralThèses sur le sujet "AKT PHOSPHORYLATION"
Schrötter, Sandra. « Specificity of developmental- and growth factor-dependent phosphorylation of Akt isoforms in neurons ». Doctoral thesis, Humboldt-Universität zu Berlin, Lebenswissenschaftliche Fakultät, 2016. http://dx.doi.org/10.18452/17593.
Texte intégralA major pathway involved in neuronal development is the PI3K-PTEN-Akt pathway. Akt comprises three isoforms, which are activated by phosphorylation of the residues S473 and T308. KO animals for the isoforms have shown differential as well as redundant functions of the three isoforms. However, their individual role in neuronal signaling pathways has not yet been studied in great detail. The aim of this study was to obtain further insight into differential Akt isoform signaling in response to changes in the activity of PI3K and PTEN pathway. A new isoelectric focusing method was established, which allowed us to separate Akt proteins according to their charge, therefore, providing a refined read-out to study dynamics of Akt phosphorylation in a neuronal background. In the course of this project we were able to identify previously undescribed features of Akt phosphorylation and activation. First, we could provide evidence for an uncoupling of the two activating phosphorylation events at S473 and T308 in neuroblastoma cells and differential sensitivities of Akt1 forms towards PI3K inhibition. Secondly, we found a transient shift in Akt isoform activation and abundance during postnatal rat brain development. Thirdly, we were able to show that the activation of different Akt isoforms is dependent of the upstream signal as well as the age of the neuron. Immature neurons were found to be highly responsive to BDNF treatment, whereas mature neurons were most responsive to EGF stimulation leading exclusively to activation of Akt2 in an EGFR- and PI3K/p110α-dependent manner. Stimulation of Akt phosphorylation by the loss of PTEN led to an activation of mainly Akt1 forms, which suggests inherent differences in the Akt pools that are accessible to growth factors dependent PI3Ks as compared to the pools that are controlled by PTEN. In summary, this thesis demonstrates the presence of complex phosphorylation events of Akt in a developmental- and signal-dependent manner in neurons.
Lefevre, Carine. « Mécanismes de régulation de la balance prolifération/différenciation érythroïde par les facteurs de transcription GATA-1, FOG-1, E2F et la voie de signalisation Akt ». Thesis, Paris 11, 2013. http://www.theses.fr/2013PA11T010/document.
Texte intégralWith more than 100 billion red blood cells generated every day, the erythroid lineage has the largest output of cell production in adult mammals. This production requires a tight balance between cell proliferation, mainly controlled by erythropoietin (Epo)/PI3K/Akt signaling pathway, and erythroid differentiation induced by GATA-1 and FOG-1 transcription factors. Various links between these two processes have been previously demonstrated in the laboratory: 1) Epo-activated Akt directly phosphorylates GATA-1 transcription factors, and this phosphorylation seems to be involved in erythroid differentiation; 2) GATA-1 binds to the cell cycle regulator retinoblastoma protein (pRb), and the resulting complex is essential for terminal erythropoiesis.We investigated the molecular mechanisms involved in the cell proliferation/differentiation balance during terminal erythropoiesis; in particular, we studied the molecular and physiological role of Epo-induced GATA-1 phosphorylation. Our findings suggest that this phosphorylation is one of the key processes in erythropoiesis dynamics. In its unphosphorylated form, GATA-1 can break cell cycle progression via GATA-1/pRb/E2F complex. This preliminary step is necessary for terminal erythroid differentiation. GATA-1 phosphorylation promotes GATA-1/pRb/E2F dissociation, allowing cell cycle progression, and GATA-1/FOG-1 binding, necessary to activate erythroid genes. Our model provides a molecular explanation for the arrest of terminal erythroid differentiation observed in the non-FOG-1-binding mutant GATA-1V205G. We show that the constitutive phosphorylation of GATA-1V205G and the increase of FOG-1 protein amount rescue erythroid differentiation in vitro. Finally, knock-in expression of unphosphorylatable GATA-1 in mice leads to lethal anemia when the IGF-1 signaling pathway is inhibited. This shows the importance of the molecular dynamics of GATA-1 phosphorylation, and highlights the major role of IGF-1 in erythropoiesis, in vivo.In conclusion, we propose a new molecular model for the control of the balance between proliferation and erythroid differentiation. GATA-1 phosphorylation by Akt coordinates the involvement of GATA-1 in two different functional protein complexes: GATA-1/pRb/E2F and GATA-1/FOG-1. We also highlight the major role of IGF-1 in compensating for the lack of GATA-1 phosphorylation in vivo
Conley, Travis B. « The influence of training status on ERK and AKT phosphorylation in human skeletal muscle ». Virtual Press, 2005. http://liblink.bsu.edu/uhtbin/catkey/1319219.
Texte intégralSchool of Physical Education, Sport, and Exercise Science
Lyons, Traci Renae. « Analysis of potential substrates for the pro-survival kinase AKT / ». Connect to full text via ProQuest. Limited to UCD Anschutz Medical Campus, 2006.
Trouver le texte intégralTypescript. Includes bibliographical references (leaves 194-209). Free to UCD Anschutz Medical Campus. Online version available via ProQuest Digital Dissertations;
Chopra, Ines. « Molecular Mechanisms of AMPK- and Akt-Dependent Survival of Glucose-Starved Cardiac Myocytes ». Scholarly Repository, 2012. http://scholarlyrepository.miami.edu/oa_dissertations/710.
Texte intégralGoodwani, Sunil G. « Amoxicillin and Augmentin Reduce Ethanol Intake and Increase GLT1 Expression as well as AKT Phosphorylation in Mesocorticolimbic Regions ». University of Toledo Health Science Campus / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=mco1403873055.
Texte intégralTamburini-Bonnefoy, Jérôme. « Régulation des voies de signalisation P13K/Akt et mTOR dans les leucémies aiguës myéloïdes : implications physiopathologiques et thérapeutiques ». Paris 7, 2009. http://www.theses.fr/2009PA077179.
Texte intégralIn acute myeloid leukemia (AML), aberrant activation of signal transduction pathways enhances the survival of leukemic cells. We showed that 50% of primary AML samples had a constitutive activation of -PI3K/Akt generally due to an autocrine IGF-1/IGF-1R loop. However, specific PI3K and ÏGF-1R inhibitors'only showed limited anti-leukemic activity. The specific inhibition of mTORCl by rapamycm induced an IGF 1-dependent overactivation of PI3K that limited thé anti-leukemic potential of rapamycm. This emphasized the potential benefit of dual PI3K and mTORCl inhibitors in AML. Surprismgly, the mRNA translation process was not controlled by mTORCl in AML, and rapamycm failed to reduce the expression of oncogenic proteins. The Pim-2 kinase was involved in this mechamsm suggesting a potential benefit for Pim-2 inhibitors in the future. We showed that directly targeting the translation initiating complex by the 4EGI-1 compound decreased AML cell survival while sparing normal hematopoiesis, suggesting other therapeutic perspectives in AML therapy. We also showed that mTOR controlled by complex phosphorylation events the translation regulator 4E-BP1 m AML, independently of mTORCl and mTORC2 Finally, we activated the LKB1/AMPK pathway using metformin, which represents a physiological repressor of mTOR activity. This molecule markedly impaired the translation of oncogenic mRNA and repressed the growth of AML cells. The present work therefore contributed to emphasize the oncogenic deregulation of mRNA translation as a valuable target m AML that could be inhibited using different physiologic-based approaches
Lyros, Orestis, Ann-Kristin Lamprecht, Linghui Nie, René Thieme, Katharina Götzel, Mario Gasparri, George Haasler, Parvaneh Rafiee, Reza Shaker et Ines Gockel. « Dickkopf-1 (DKK1) promotes tumor growth via Akt-phosphorylation and independently of Wnt-axis in Barrett’s associated esophageal adenocarcinoma ». e-Century Publishing, 2019. https://ul.qucosa.de/id/qucosa%3A33709.
Texte intégralMurakami, Tomoaki. « Angiopoietin-1 attenuates H2O2-induced SEK1/JNK phosphorylation through the phosphatidylinositol 3-kinase/Akt pathway in vascular endothelial cells ». Kyoto University, 2006. http://hdl.handle.net/2433/143830.
Texte intégralMatthews, Jason Aaron. « Investigation of the effects of increased levels of O-GlcNAc protein modification on protein kinase C and Akt ». [Tampa, Fla] : University of South Florida, 2006. http://purl.fcla.edu/usf/dc/et/SFE0001723.
Texte intégralLivres sur le sujet "AKT PHOSPHORYLATION"
Beninger, Richard J. Life's rewards. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780198824091.001.0001.
Texte intégralJancura, Daniel, et Erik Sedlák. Bioenergetika. Univerzita Pavla Jozefa Šafárika, Vydavateľstvo ŠafárikPress, 2021. http://dx.doi.org/10.33542/be2021-0022-6.
Texte intégralChapitres de livres sur le sujet "AKT PHOSPHORYLATION"
Hirai, K., T. Hayashi, P. H. Chan, V. J. Basus, T. L. James et Lawrence Litt. « Akt phosphorylation and cell survival after hypoxia-induced cytochrome c release in superfused respiring neonatal rat cerebrocortical slices ». Dans Brain Edema XII, 227–30. Vienna : Springer Vienna, 2003. http://dx.doi.org/10.1007/978-3-7091-0651-8_49.
Texte intégralAppuhamy, J. A. D. R. N., et M. D. Hanigan. « Modeling the effects of insulin and amino acids on the phosphorylation of mTOR, Akt, and 4EBP1 in mammary cells ». Dans Modelling nutrient digestion and utilisation in farm animals, 225–32. Wageningen : Wageningen Academic Publishers, 2011. http://dx.doi.org/10.3920/978-90-8686-712-7_25.
Texte intégralPirincci Ercan, Deniz, et Frank Uhlmann. « Analysis of Cell Cycle Progression in the Budding Yeast S. cerevisiae ». Dans Methods in Molecular Biology, 265–76. New York, NY : Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1538-6_19.
Texte intégralPu, Jing, et Pingsheng Liu. « Fatty Acids Stimulate Glucose Uptake by the PI3K/AMPK/Akt and PI3K/ERK1/2 Pathways ». Dans Protein Phosphorylation in Human Health. InTech, 2012. http://dx.doi.org/10.5772/52456.
Texte intégralYildiz, Aysegul, et Yesim Kaya. « Post-Translational Regulation of the Activity of ERK/MAPK and PI3K/AKT Signaling Pathways in Neuroblastoma Cancer ». Dans Post-Translational Modifications in Cellular Functions and Diseases [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96176.
Texte intégralNing, Junyu, et David R. Clemmons. « IGF-I Suppresses AMPK Activity through Stimulation of Akt Mediated Phosphorylation of AMPK at S485. » Dans The Endocrine Society's 92nd Annual Meeting, June 19–22, 2010 - San Diego, P1–137—P1–137. Endocrine Society, 2010. http://dx.doi.org/10.1210/endo-meetings.2010.part1.p3.p1-137.
Texte intégralBerrou, Mohammed, Basel Taha, Alemu Fite, Nabanita S. Datta et Abdul B. Abou-Samra. « Globular Adiponectin Increases the Phosphorylation of AKT, ERK1/2 and CREB in MC3T3-E1 Cells, Affecting Their Proliferation, Gene Expression and Glucose Uptake ». Dans BASIC - Bone, Calciotropic Hormones & ; Vitamin D, P1–186—P1–186. The Endocrine Society, 2011. http://dx.doi.org/10.1210/endo-meetings.2011.part1.p9.p1-186.
Texte intégralActes de conférences sur le sujet "AKT PHOSPHORYLATION"
Adi, Y. A., F. Adi-Kusumo, L. Aryati et M. S. Hardianti. « Modelling inhibition of AKT phosphorylation in acute myeloid leukemia ». Dans THE 2016 CONFERENCE ON FUNDAMENTAL AND APPLIED SCIENCE FOR ADVANCED TECHNOLOGY (CONFAST 2016) : Proceeding of ConFAST 2016 Conference Series : International Conference on Physics and Applied Physics Research (ICPR 2016), International Conference on Industrial Biology (ICIBio 2016), and International Conference on Information System and Applied Mathematics (ICIAMath 2016). Author(s), 2016. http://dx.doi.org/10.1063/1.4953987.
Texte intégralAdi, Y. A., F. A. Kusumo, L. Aryati et M. S. Hardianti. « A mathematical model of phosphorylation AKT in Acute Myeloid Leukemia ». Dans SYMPOSIUM ON BIOMATHEMATICS (SYMOMATH 2015). AIP Publishing LLC, 2016. http://dx.doi.org/10.1063/1.4945059.
Texte intégralKoirala, Pratirodh, et Yin Yuan MO. « Abstract 155 : LncRNA AK023948 promotes breast tumorigenesis by enhancing AKT phosphorylation ». Dans Proceedings : AACR 106th Annual Meeting 2015 ; April 18-22, 2015 ; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-155.
Texte intégralAli, Amna, et Diane F. Matesic. « Abstract 4523 : Chaetoglobosin K, a dual Akt and JNK inhibitor, modulates Akt phosphorylation in an mTORC2 independent manner ». Dans 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.am2014-4523.
Texte intégralElshiekh, Duaa Ibnomer, Hadeel Hendawi, Aya Goul, Dina Awartan, Isra Marei, Christopher Triggle et Haissam Abou Saleh. « Effect of Hyperglycemia on eNOS function in EPCs ». Dans Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0215.
Texte intégralMacEwan, Melanie, Ismatun Swati, Suqing Xie, Olena Ardacheva, Codrin Iacob, Edward Shin, Augustine Moscatello, Stimson Schantz, Raj K. Tiwari et Jan Geliebter. « Abstract 3921 : Androgens stimulate phosphorylation of ERK and AKT in thyroid cancer cells ». Dans 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.am2012-3921.
Texte intégralKoromilas, Antonis E., Rajesh Kamindla, Andreas I. Papadakis, Urszula Kazimierczak, Philippos Peidis, Shuo Wang, Clara Tenkerian et al. « Abstract C51 : eIF2alpha phosphorylation determines cell susceptibility to oxidative stress via Akt activation. » Dans Abstracts : AACR-NCI-EORTC International Conference : Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013 ; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-c51.
Texte intégralRoldan, Diana Barea, Christoph Hartmann, Stefanie Hubich-Rau, Tim Beissert, Claudia Paret, Giuseppe Cagna, Christoph Rohde, Stefan Wöll, Ugur Sahin et Ozlem Tureci. « Abstract 763 : PLAC1 interacts with FGF7 and promotes phosphorylation of FGFR2 and AKT ». Dans Proceedings : AACR Annual Meeting 2018 ; April 14-18, 2018 ; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-763.
Texte intégralShou, J., KC Osborne, J. Gee, R. Nicholson et R. Schiff. « Akt-dependent phosphorylation on AIB1 serine 967 contributes to breast cancer tamoxifen resistance. » Dans CTRC-AACR San Antonio Breast Cancer Symposium : 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-3021.
Texte intégralThakur, Shreya, Charyguly Annageldiyev, Srinivasa Ramisetti, Trupti Patel, Saumya Iyer, Pavan Dhanyamraju, Shantu Amiin, Arun Sharma, David Claxton et Arati Sharma. « Abstract 358 : Inhibition of AKT phosphorylation in acute myeloid leukemia by ISC 4 ». Dans 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.am2019-358.
Texte intégralRapports d'organisations sur le sujet "AKT PHOSPHORYLATION"
Wang, Yanru, et Keqiang Ye. Akt Phosphorylation and PI (3, 4, 5) P3 Binding Coordinately Inhibit the Tumor Suppressive Activity of Merlin. Fort Belvoir, VA : Defense Technical Information Center, février 2010. http://dx.doi.org/10.21236/ada523196.
Texte intégralDa Silva, Thiago. CDK2 Phosphorylation on Threonine39 by AKT and Its Implication on Cyclin Binding, Cellular Localization, and Cell Cycle Progression. Fort Belvoir, VA : Defense Technical Information Center, octobre 2007. http://dx.doi.org/10.21236/ada488284.
Texte intégralGranot, David, Richard Amasino et Avner Silber. Mutual effects of hexose phosphorylation enzymes and phosphorous on plant development. United States Department of Agriculture, janvier 2006. http://dx.doi.org/10.32747/2006.7587223.bard.
Texte intégralGao, Daming, Hiroyuki Inuzuka, Alan Tseng et Wenyi Wei. Investigating the Role of Akt1 in Prostate Cancer Development Through Phosphorylation-Dependent Regulation of Skp2 Stability and Oncogenic Function. Fort Belvoir, VA : Defense Technical Information Center, septembre 2010. http://dx.doi.org/10.21236/ada535175.
Texte intégralWei, Wenyi, Daming Gao, Hiroyuki Inuzuka et Alan Tseng. Investigating the Role of Akt1 in Prostate Cancer Development through Phosphorylation-dependent Regulation of Skp2 Stability and Oncogenic Function. Fort Belvoir, VA : Defense Technical Information Center, septembre 2012. http://dx.doi.org/10.21236/ada566865.
Texte intégralChamovitz, Daniel A., et Xing-Wang Deng. Developmental Regulation and Light Signal Transduction in Plants : The Fus5 Subunit of the Cop9 Signalosome. United States Department of Agriculture, septembre 2003. http://dx.doi.org/10.32747/2003.7586531.bard.
Texte intégralLocy, Robert D., Hillel Fromm, Joe H. Cherry et Narendra K. Singh. Regulation of Arabidopsis Glutamate Decarboxylase in Response to Heat Stress : Modulation of Enzyme Activity and Gene Expression. United States Department of Agriculture, janvier 2001. http://dx.doi.org/10.32747/2001.7575288.bard.
Texte intégralGranot, David, Scott Holaday et Randy D. Allen. Enhancing Cotton Fiber Elongation and Cellulose Synthesis by Manipulating Fructokinase Activity. United States Department of Agriculture, 2008. http://dx.doi.org/10.32747/2008.7613878.bard.
Texte intégralDelmer, Deborah P., et Prem S. Chourey. The Importance of the Enzyme Sucrose Synthase for Cell Wall Synthesis in Plants. United States Department of Agriculture, octobre 1994. http://dx.doi.org/10.32747/1994.7568771.bard.
Texte intégralPhilosoph-Hadas, Sonia, Peter B. Kaufman, Shimon Meir et Abraham H. Halevy. Inhibition of the Gravitropic Shoot Bending in Stored Cut Flowers Through Control of Their Graviperception : Involvement of the Cytoskeleton and Cytosolic Calcium. United States Department of Agriculture, décembre 2005. http://dx.doi.org/10.32747/2005.7586533.bard.
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