Academic literature on the topic 'Subcellular compartmentalization'

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Journal articles on the topic "Subcellular compartmentalization"

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Mohr, Evita. "Subcellular RNA compartmentalization." Progress in Neurobiology 57, no. 5 (1999): 507–25. http://dx.doi.org/10.1016/s0301-0082(98)00066-5.

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Pederson, N. E. "Regulation of herpesvirus replication by subcellular compartmentalization." Medical Hypotheses 54, no. 1 (2000): 64–68. http://dx.doi.org/10.1054/mehy.1998.0814.

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Gilligan, A., H. Kawamura, and J. L. Vaitukaitis. "Rat ovarian subcellular compartmentalization of luteinizing hormone." Molecular and Cellular Endocrinology 46, no. 2 (1986): 155–62. http://dx.doi.org/10.1016/0303-7207(86)90094-8.

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Pilch, P. "SUBCELLULAR COMPARTMENTALIZATION OF INSULIN-REGULATED VESICULAR TRAFFIC." Biochemical Society Transactions 25, no. 3 (1997): 461S. http://dx.doi.org/10.1042/bst025461sb.

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Hart, Clyde E., Glen H. Nuckolls, and John G. Wood. "Subcellular compartmentalization of phosphorylated neurofilament polypeptides in neurons." Cell Motility and the Cytoskeleton 7, no. 4 (1987): 393–403. http://dx.doi.org/10.1002/cm.970070411.

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Luby-Phelps, Katherine, and D. Lansing Taylor. "Subcellular compartmentalization by local differentiation of cytoplasmic structure." Cell Motility and the Cytoskeleton 10, no. 1-2 (1988): 28–37. http://dx.doi.org/10.1002/cm.970100107.

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Gill, R. Montgomery, and Paul A. Hamel. "Subcellular Compartmentalization of E2f Family Members Is Required for Maintenance of the Postmitotic State in Terminally Differentiated Muscle." Journal of Cell Biology 148, no. 6 (2000): 1187–202. http://dx.doi.org/10.1083/jcb.148.6.1187.

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Maintenance of cells in a quiescent state after terminal differentiation occurs through a number of mechanisms that regulate the activity of the E2F family of transcription factors. We report here that changes in the subcellular compartmentalization of the E2F family proteins are required to prevent nuclei in terminally differentiated skeletal muscle from reentering S phase. In terminally differentiated L6 myotubes, E2F-1, E2F-3, and E2F-5 were primarily cytoplasmic, E2F-2 was nuclear, whereas E2F-4 became partitioned between both compartments. In these same cells, pRB family members, pRB, p10
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Leandro, João, and Sander M. Houten. "The lysine degradation pathway: Subcellular compartmentalization and enzyme deficiencies." Molecular Genetics and Metabolism 131, no. 1-2 (2020): 14–22. http://dx.doi.org/10.1016/j.ymgme.2020.07.010.

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Wistuba, A., A. Kern, S. Weger, D. Grimm, and J. A. Kleinschmidt. "Subcellular compartmentalization of adeno-associated virus type 2 assembly." Journal of virology 71, no. 2 (1997): 1341–52. http://dx.doi.org/10.1128/jvi.71.2.1341-1352.1997.

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FORST, CHRISTIAN V., LAWRENCE CABUSORA, KWASI G. MAWUENYEGA, and XIAN CHEN. "BIOLOGICAL SYSTEMS ANALYSIS BY A NETWORK PROTEOMICS APPROACH AND SUBCELLULAR PROTEIN PROFILING." Advances in Complex Systems 09, no. 04 (2006): 299–314. http://dx.doi.org/10.1142/s0219525906000835.

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We provide a systematic analysis of a biological system, the microbial pathogen Mycobacterium tuberculosis (Mtb) by directly profiling its gene products. This analysis combines high-throughput proteomics and biocomputational approaches to elucidate the globally expressed complements of the three subcellular compartments (the cell wall, membrane and cytosol) of Mtb. We report the compartmentalization of 1,044 identified proteins using proteomics methods. Genome-based biological network analyses were performed and integrated with proteomics data to reconstruct response networks. From the reconst
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Dissertations / Theses on the topic "Subcellular compartmentalization"

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Song, Jingwen. "Subcellular compartmentalization of Akt contributes to signaling intensity." Thesis, McGill University, 2013. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=114537.

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Background: In the Current Model of Akt activation, a key event is its recruitment to the plasma membrane, where it is fully activated subsequent to sequential phosphorylation at positions Ser473 and Thr308. The distribution of Akt into various subcellular compartments may contribute to the different signaling pathways which it influences. There is evidence of compartment-specific regulators in plasma membrane (PM) and endosomes. Previous experiment in our laboratory showed that Akt achieved greater specific activity in PM compared to cytosol after insulin treatment. This raised the question w
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Banach-Latapy, Agata. "Monitoring dynamic changes of glutathione redox state in subcellular compartments of human cells : a novel approach based on rxYFP biosensors." Thesis, Paris 11, 2013. http://www.theses.fr/2013PA112346.

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La biologie des réactions redox est particulièrement difficile à étudier de par la compartimentation spatiale mais aussi cinétique des différents systèmes redox cellulaires. Les biosenseurs codés génétiquement, incluant la «redox-sensitive Yellow Fluorescent Protein» (rxYFP) sont une manière de contourner les limitations des méthodes conventionnelles de mesure du couple glutathion/glutathion disulfure (GSH/GSSG). Cette étude présente l’utilisation des biosenseurs rxYFP pour analyser les états redox dans des différents compartiments cellulaires, et leur dynamique en réponse au stress dans les c
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Foureau, Emilien. "Elucidation de la voie de biosynthèse des alcaloïdes de Catharanthus roseus et ingénierie métabolique dans la levure." Thesis, Tours, 2016. http://www.theses.fr/2016TOUR3805/document.

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Catharanthus roseus est une plante médicinale produisant divers types d’alcaloïdes indoliques monoterpéniques (AIM) d’intérêt en santé humaine. Ainsi, les AIM dimères comme la vinblastine et la vincristine sont utilisés en chimiothérapie anticancéreuse et les alcaloïdes monomères de type hétéroyohimbine présentent diverses activités pharmacologiques. La fabrication de ces molécules dans la plante est fort complexe. Elle requiert un haut niveau de compartimentation tissulaire et subcellulaire et met en jeu plus d’une trentaine d’étapes enzymatiques, dont certaines sont encore très mal connues.
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Tsai, Yu Wen, and 蔡郁玟. "Subcellular Compartmentalization of Anaerobic Cholesterol Metabolism in Sterolibacterium denitrificans." Thesis, 2013. http://ndltd.ncl.edu.tw/handle/03164341075891474076.

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碩士<br>長庚大學<br>中醫學系天然藥物<br>101<br>Abstract Out to the mass excretion and decomposition by human and livestock activities, cholesterol is a ubiquitous and abundant compound in nature. In addition, small amounts of cholesterol are also produced by plants and fungi. It processes complex chemical structure and low water solubility which render cholesterol hardly to be degraded by microorganism, especially under anoxic conditions . The oxic degradation pathway of cholesterol has been studied in some detail, and the oxic 9,10-seco-pathway for cholesterol degradation was established about thirty y
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Books on the topic "Subcellular compartmentalization"

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Corpas, Francisco J., and José Manuel Palma, eds. Subcellular Compartmentalization of Plant Antioxidants and ROS Generating Systems. Frontiers Media SA, 2021. http://dx.doi.org/10.3389/978-2-88966-632-4.

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Book chapters on the topic "Subcellular compartmentalization"

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Agudo-Ibañez, Lorena, Piero Crespo, and Berta Casar. "Analysis of Ras/ERK Compartmentalization by Subcellular Fractionation." In Methods in Molecular Biology. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6424-6_11.

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Mohr, E., and D. Richter. "Neuroendocrine Cells Revisited: A System for Studying Subcellular mRNA Compartmentalization." In Neuroendocrinology. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60915-2_5.

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Petersen, Ole, Michael Ashby, Myoung Park, Nicholas Dolman, and Alexei Tepikin. "Subcellular Compartmentalization of Calcium Signaling." In Calcium Signaling, Second Edition. CRC Press, 2005. http://dx.doi.org/10.1201/9781420038231.ch15.

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"Subcellular Compartmentalization of Calcium Signaling." In Calcium Signaling. CRC Press, 2005. http://dx.doi.org/10.1201/9781420038231-20.

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Conference papers on the topic "Subcellular compartmentalization"

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Tourlomousis, Filippos, and Robert C. Chang. "2D and 3D Multiscale Computational Modeling of Dynamic Microorgan Devices as Drug Screening Platforms." In ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52734.

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The ability to incorporate three-dimensional (3D) hepatocyte-laden hydrogel constructs using layered fabrication approaches into devices that can be perfused with drugs enables the creation of dynamic microorgan devices (DMDs) that offer an optimal analog of the in vivo liver metabolism scenario. The dynamic nature of such in vitro metabolism models demands reliable numerical tools to determine the optimum process, material, and geometric parameters for the most effective metabolic conversion of the perfused drug into the liver microenvironment. However, there is a current lack of literature t
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