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Journal articles on the topic 'Subcellular compartmentalization'

Author: Grafiati

Published: 4 June 2021

Last updated: 2 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Sachs, B. D., and K. Akassoglou. "Regulation of cAMP by the p75 neurotrophin receptor: insight into drug design of selective phosphodiesterase inhibitors." Biochemical Society Transactions 35, no. 5 (2007): 1273–77. http://dx.doi.org/10.1042/bst0351273.

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Subcellular compartmentalization of PDEs (phosphodiesterases) is a major mechanism for the regulation of cAMP signalling. The identification of the proteins that recruit specific PDE isoforms to subcellular compartments can shed light on the regulation of spatial and temporal cAMP gradients in living cells and provide novel therapeutic targets for inhibiting functions of PDEs. We showed recently that p75NTR (p75 neurotrophin receptor) interacts directly with a single PDE isoform, namely PDE4A4/5, via binding to its unique C-terminal region, and targets cAMP degradation to the membrane. The pur

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12

Faruque, Omar M., Dung Le-Nguyen, Anne-Dominique Lajoix, et al. "Cell-permeable peptide-based disruption of endogenous PKA-AKAP complexes: a tool for studying the molecular roles of AKAP-mediated PKA subcellular anchoring." American Journal of Physiology-Cell Physiology 296, no. 2 (2009): C306—C316. http://dx.doi.org/10.1152/ajpcell.00216.2008.

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Stimulation of numerous G protein-coupled receptors leads to the elevation of intracellular concentrations of cAMP, which subsequently activates the PKA pathway. Specificity of the PKA signaling module is determined by a sophisticated subcellular targeting network that directs the spatiotemporal activation of the kinase. This specific compartmentalization mechanism occurs through high-affinity interactions of PKA with A-kinase anchoring proteins (AKAPs), the role of which is to target the kinase to discrete subcellular microdomains. Recently, a peptide designated “AKAPis” has been proposed to

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13

Bobrovskikh, Aleksandr, Ulyana Zubairova, Alexey Kolodkin, and Alexey Doroshkov. "Subcellular compartmentalization of the plant antioxidant system: an integrated overview." PeerJ 8 (July 16, 2020): e9451. http://dx.doi.org/10.7717/peerj.9451.

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The antioxidant system (AOS) maintains the optimal concentration of reactive oxygen species (ROS) in a cell and protects it against oxidative stress. In plants, the AOS consists of seven main classes of antioxidant enzymes, low-molecular antioxidants (e.g., ascorbate, glutathione, and their oxidized forms) and thioredoxin/glutaredoxin systems which can serve as reducing agents for antioxidant enzymes. The number of genes encoding AOS enzymes varies between classes, and same class enzymes encoded by different gene copies may have different subcellular localizations, functional loads and modes o

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14

Welshons, W. V., L. H. Grady, B. M. Judy, V. C. Jordan, and D. E. Preziosi. "Subcellular compartmentalization of MCF-7 estrogen receptor synthesis and degradation." Molecular and Cellular Endocrinology 94, no. 2 (1993): 183–94. http://dx.doi.org/10.1016/0303-7207(93)90167-i.

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15

Tchikov, Vladimir, Uwe Bertsch, Jürgen Fritsch, Bärbel Edelmann, and Stefan Schütze. "Subcellular compartmentalization of TNF receptor-1 and CD95 signaling pathways." European Journal of Cell Biology 90, no. 6-7 (2011): 467–75. http://dx.doi.org/10.1016/j.ejcb.2010.11.002.

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16

Scott, JD, and DW Carr. "Subcellular Localization of the Type II cAMP-Dependent Protein Kinase." Physiology 7, no. 4 (1992): 143–48. http://dx.doi.org/10.1152/physiologyonline.1992.7.4.143.

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Diverse biochemical effects of different neurotransmitters or hormones that stimulate cAMP production may occur through activation of compartmentalized pools of cAMP-dependent protein kinase (PKA). Evidence suggests that compartmentalization of type II PKA is maintained through protein-protein interactions between the regulatory subunit and specific anchoring proteins.

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17

Grisan, Francesca, Liliana F. Iannucci, Nicoletta C. Surdo, et al. "PKA compartmentalization links cAMP signaling and autophagy." Cell Death & Differentiation 28, no. 8 (2021): 2436–49. http://dx.doi.org/10.1038/s41418-021-00761-8.

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AbstractAutophagy is a highly regulated degradative process crucial for maintaining cell homeostasis. This important catabolic mechanism can be nonspecific, but usually occurs with fine spatial selectivity (compartmentalization), engaging only specific subcellular sites. While the molecular machines driving autophagy are well understood, the involvement of localized signaling events in this process is not well defined. Among the pathways that regulate autophagy, the cyclic AMP (cAMP)/protein kinase A (PKA) cascade can be compartmentalized in distinct functional units called microdomains. Howev

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18

Duso, Lorenzo, and Christoph Zechner. "Stochastic reaction networks in dynamic compartment populations." Proceedings of the National Academy of Sciences 117, no. 37 (2020): 22674–83. http://dx.doi.org/10.1073/pnas.2003734117.

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Compartmentalization of biochemical processes underlies all biological systems, from the organelle to the tissue scale. Theoretical models to study the interplay between noisy reaction dynamics and compartmentalization are sparse, and typically very challenging to analyze computationally. Recent studies have made progress toward addressing this problem in the context of specific biological systems, but a general and sufficiently effective approach remains lacking. In this work, we propose a mathematical framework based on counting processes that allows us to study dynamic compartment populatio

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19

Winisdorffer, Guillaume, Maja Musse, Stéphane Quellec, Marie-Françoise Devaux, Marc Lahaye, and François Mariette. "MRI investigation of subcellular water compartmentalization and gas distribution in apples." Magnetic Resonance Imaging 33, no. 5 (2015): 671–80. http://dx.doi.org/10.1016/j.mri.2015.02.014.

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20

Nikitin, E. S., and P. M. Balaban. "Compartmentalization of Non-Synaptic Plasticity in Neurons at the Subcellular Level." Neuroscience and Behavioral Physiology 44, no. 7 (2014): 725–30. http://dx.doi.org/10.1007/s11055-014-9975-5.

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21

Watson, Robert T., and Jeffrey E. Pessin. "Subcellular Compartmentalization and Trafficking of the Insulin-Responsive Glucose Transporter, GLUT4." Experimental Cell Research 271, no. 1 (2001): 75–83. http://dx.doi.org/10.1006/excr.2001.5375.

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22

Fernandez, Juliette, Cédric Hassen-Khodja, Virginie Georget, et al. "Measuring the subcellular compartmentalization of viral infections by protein complementation assay." Proceedings of the National Academy of Sciences 118, no. 2 (2021): e2010524118. http://dx.doi.org/10.1073/pnas.2010524118.

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The recent emergence and reemergence of viruses in the human population has highlighted the need to develop broader panels of therapeutic molecules. High-throughput screening assays opening access to untargeted steps of the viral replication cycle will provide powerful leverage to identify innovative antiviral molecules. We report here the development of an innovative protein complementation assay, termed αCentauri, to measure viral translocation between subcellular compartments. As a proof of concept, the Centauri fragment was either tethered to the nuclear pore complex or sequestered in the

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23

Upadhyay, Srijana, Xinping Xu, David Lowry, Jennifer C. Jackson, Robert W. Roberson, and Xiaorong Lin. "Subcellular Compartmentalization and Trafficking of the Biosynthetic Machinery for Fungal Melanin." Cell Reports 14, no. 11 (2016): 2511–18. http://dx.doi.org/10.1016/j.celrep.2016.02.059.

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24

Vance, Jean E. "Compartmentalization and differential labeling of phospholipids of rat liver subcellular membranes." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 963, no. 1 (1988): 10–20. http://dx.doi.org/10.1016/0005-2760(88)90332-3.

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25

Mastroiacovo, Federica, Francesca Biagioni, Paola Lenzi, et al. "Stoichiometric Analysis of Shifting in Subcellular Compartmentalization of HSP70 within Ischemic Penumbra." Molecules 26, no. 12 (2021): 3578. http://dx.doi.org/10.3390/molecules26123578.

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The heat shock protein (HSP) 70 is considered the main hallmark in preclinical studies to stain the peri-infarct region defined area penumbra in preclinical models of brain ischemia. This protein is also considered as a potential disease modifier, which may improve the outcome of ischemic damage. In fact, the molecule HSP70 acts as a chaperonine being able to impact at several level the homeostasis of neurons. Despite being used routinely to stain area penumbra in light microscopy, the subcellular placement of this protein within area penumbra neurons, to our knowledge, remains undefined. This

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26

Akins, R. E., and R. S. Tuan. "Transepithelial calcium transport in the chick chorioallantoic membrane. II. Compartmentalization of calcium during uptake." Journal of Cell Science 105, no. 2 (1993): 381–88. http://dx.doi.org/10.1242/jcs.105.2.381.

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Calcium transport from the eggshell to the developing chick embryo is carried out by the ectoderm cells of the chick chorioallantoic membrane. Primary cells isolated from chick chorioallantoic membrane ectoderm were used to analyze the subcellular distribution of 45Ca2+ accumulated from the extracellular medium. We present evidence suggesting that calcium may be sequestered into endosome-like vesicles during the initial phase of uptake. A combination of techniques were utilized to monitor calcium fluxes and calcium compartmentalization in the cultured chorioallantoic membrane cells: (1) fura-2

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27

Stangherlin, Alessandra, and Manuela Zaccolo. "Phosphodiesterases and subcellular compartmentalized cAMP signaling in the cardiovascular system." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 2 (2012): H379—H390. http://dx.doi.org/10.1152/ajpheart.00766.2011.

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Phosphodiesterases are key enzymes in the cAMP signaling cascade. They convert cAMP in its inactive form 5′-AMP and critically regulate the intensity and the duration of cAMP-mediated signals. Multiple isoforms exist that possess different intracellular distributions, different affinities for cAMP, and different catalytic and regulatory properties. This complex repertoire of enzymes provides a multiplicity of ways to modulate cAMP levels, to integrate more signaling pathways, and to respond to the specific needs of the cell within distinct subcellular domains. In this review we summarize key f

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28

Lawrence, Scott A., Steven A. Titus, Jennifer Ferguson, Amy L. Heineman, Shirley M. Taylor, and Richard G. Moran. "Mammalian Mitochondrial and Cytosolic Folylpolyglutamate Synthetase Maintain the Subcellular Compartmentalization of Folates." Journal of Biological Chemistry 289, no. 42 (2014): 29386–96. http://dx.doi.org/10.1074/jbc.m114.593244.

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29

CHU, CHARLEEN T., and JIAN-HUI ZHU. "Subcellular Compartmentalization of P-ERKs in the Lewy Body Disease Substantia Nigra." Annals of the New York Academy of Sciences 991, no. 1 (2006): 288–90. http://dx.doi.org/10.1111/j.1749-6632.2003.tb07486.x.

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30

BIONDA, Clara, Jacques PORTOUKALIAN, Daniel SCHMITT, Claire RODRIGUEZ-LAFRASSE, and Dominique ARDAIL. "Subcellular compartmentalization of ceramide metabolism: MAM (mitochondria-associated membrane) and/or mitochondria?" Biochemical Journal 382, no. 2 (2004): 527–33. http://dx.doi.org/10.1042/bj20031819.

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Recent studies by our group and others have disclosed the presence of ceramides in mitochondria, and the activities of ceramide synthase and reverse ceramidase in mitochondria have also been reported. Since a possible contamination with the ER (endoplasmic reticulum)-related compartment MAM (mitochondria-associated membrane) could not be ruled out in previous studies, we have re-investigated the presence of the enzymes of ceramide metabolism in mitochondria and MAM highly purified from rat liver. In the present paper, we show that purified mitochondria as well as MAM are indeed able to generat

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31

Baudry, Michel, Richard Dubrin, and Gary Lynch. "Subcellular compartmentalization of calcium-dependent and calcium-independent neutral proteases in brain." Synapse 1, no. 6 (1987): 506–11. http://dx.doi.org/10.1002/syn.890010603.

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32

Friedrich, Teresa, Michaela Söhn, Tobias Gutting, et al. "Subcellular compartmentalization of docking protein-1 contributes to progression in colorectal cancer." EBioMedicine 8 (June 2016): 159–72. http://dx.doi.org/10.1016/j.ebiom.2016.05.003.

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33

Linask, K. K., and R. M. Greene. "Subcellular compartmentalization of cAMP-dependent protein kinase regulatory subunits during palate ontogeny." Life Sciences 45, no. 20 (1989): 1863–68. http://dx.doi.org/10.1016/0024-3205(89)90539-0.

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34

Cooper, D. M. F. "Compartmentalization of adenylate cyclase and cAMP signalling." Biochemical Society Transactions 33, no. 6 (2005): 1319–22. http://dx.doi.org/10.1042/bst0331319.

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Concepts of cAMP signalling have changed dramatically from the linear cascades of just a few years ago, with the realization that numerous cellular processes affect this motif. These influences include other signalling pathways – most significantly Ca2+, scaffolding proteins (which are themselves variously regulated) to organize the elements of the pathway, and subcellular targeting of components. An obvious implication of this organization is that global measurements of cAMP may trivialize the complexity of the cAMP signals and obscure the regulation of targets. In this presentation, current

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35

Mintz-Oron, S., S. Meir, S. Malitsky, E. Ruppin, A. Aharoni, and T. Shlomi. "Reconstruction of Arabidopsis metabolic network models accounting for subcellular compartmentalization and tissue-specificity." Proceedings of the National Academy of Sciences 109, no. 1 (2011): 339–44. http://dx.doi.org/10.1073/pnas.1100358109.

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36

Ardail, D., F. Gasnier, F. Lermé, C. Simonot, P. Louisot, and O. Gateau-Roesch. "Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes." Journal of Biological Chemistry 268, no. 34 (1993): 25985–92. http://dx.doi.org/10.1016/s0021-9258(19)74483-4.

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37

M.Green, R., M. Graham, M. R.O'Donovan, J. K. Chipman, and N. J.Hodges. "Subcellular compartmentalization of glutathione: Correlations with parameters of oxidative stress related to genotoxicity." Mutagenesis 21, no. 6 (2006): 383–90. http://dx.doi.org/10.1093/mutage/gel043.

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38

Conrad, Abigail H., William A. Clark, and Gary W. Conrad. "Subcellular compartmentalization of myosin isoforms in embryonic chick heart ventricle myocytes during cytokinesis." Cell Motility and the Cytoskeleton 19, no. 3 (1991): 189–206. http://dx.doi.org/10.1002/cm.970190307.

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39

Rohmann, Kevin N., Barney A. Schlinger, and Colin J. Saldanha. "Subcellular compartmentalization of aromatase is sexually dimorphic in the adult zebra finch brain." Developmental Neurobiology 67, no. 1 (2006): 1–9. http://dx.doi.org/10.1002/dneu.20303.

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40

Rohmann, Kevin N., Barney A. Schlinger, and Colin J. Saldanha. "Subcellular compartmentalization of aromatase is sexually dimorphic in the adult zebra finch brain." Journal of Neurobiology 67, no. 1 (2007): 1–9. http://dx.doi.org/10.1002/neu.20303.

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41

Vollmer, Jean-Yves, Philippe Alix, André Chollet, Kenneth Takeda, and Jean-Luc Galzi. "Subcellular Compartmentalization of Activation and Desensitization of Responses Mediated by NK2 Neurokinin Receptors." Journal of Biological Chemistry 274, no. 53 (1999): 37915–22. http://dx.doi.org/10.1074/jbc.274.53.37915.

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42

Geffard, Alain, Hervé Sartelet, Jeanne Garric, Sylvie Biagianti-Risbourg, Laurence Delahaut, and Olivier Geffard. "Subcellular compartmentalization of cadmium, nickel, and lead in Gammarus fossarum: Comparison of methods." Chemosphere 78, no. 7 (2010): 822–29. http://dx.doi.org/10.1016/j.chemosphere.2009.11.051.

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43

Farré, Jean-Claude, Paul Li, and Suresh Subramani. "BiFC Method Based on Intraorganellar Protein Crowding Detects Oleate-Dependent Peroxisomal Targeting of Pichia pastoris Malate Dehydrogenase." International Journal of Molecular Sciences 22, no. 9 (2021): 4890. http://dx.doi.org/10.3390/ijms22094890.

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The maintenance of intracellular NAD+/NADH homeostasis across multiple, subcellular compartments requires the presence of NADH-shuttling proteins, which circumvent the lack of permeability of organelle membranes to these cofactors. Very little is known regarding these proteins in the methylotrophic yeast, Pichia pastoris. During the study of the subcellular locations of these shuttling proteins, which often have dual subcellular locations, it became necessary to develop new ways to detect the weak peroxisomal locations of some of these proteins. We have developed a novel variation of the tradi

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44

Döring, Marius, Hanna Blees, Nicole Koller, et al. "Modulation of TAP-dependent antigen compartmentalization during human monocyte-to-DC differentiation." Blood Advances 3, no. 6 (2019): 839–50. http://dx.doi.org/10.1182/bloodadvances.2018027268.

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Abstract Dendritic cells (DCs) take up antigen in the periphery, migrate to secondary lymphoid organs, and present processed antigen fragments to adaptive immune cells and thus prime antigen-specific immunity. During local inflammation, recirculating monocytes are recruited from blood to the inflamed tissue, where they differentiate to macrophages and DCs. In this study, we found that monocytes showed high transporter associated with antigen processing (TAP)–dependent peptide compartmentalization and that after antigen pulsing, they were not able to efficiently stimulate antigen-specific T lym

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45

Zheng, Xiaowei, Jorge L. Ruas, Renhai Cao та ін. "Cell-Type-Specific Regulation of Degradation of Hypoxia-Inducible Factor 1α: Role of Subcellular Compartmentalization". Molecular and Cellular Biology 26, № 12 (2006): 4628–41. http://dx.doi.org/10.1128/mcb.02236-05.

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ABSTRACT The hypoxia-inducible factor-1α (HIF-1α) is a transcription factor that mediates adaptive cellular responses to decreased oxygen availability (hypoxia). At normoxia, HIF-1α is targeted by the von Hippel-Lindau tumor suppressor protein (pVHL) for degradation by the ubiquitin-proteasome pathway. In the present study we have observed distinct cell-type-specific differences in the ability of various tested pVHL-interacting subfragments to stabilize HIF-1α and unmask its function at normoxia. These properties correlated with differences in subcellular compartmentalization and degradation o

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46

D'ANGELO, Maximiliano A., Santiago SANGUINETI, Jeffrey M. REECE, Lutz BIRNBAUMER, Héctor N. TORRES, and Mirtha M. FLAWIÁ. "Identification, characterization and subcellular localization of TcPDE1, a novel cAMP-specific phosphodiesterase from Trypanosoma cruzi." Biochemical Journal 378, no. 1 (2004): 63–72. http://dx.doi.org/10.1042/bj20031147.

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Compartmentalization of cAMP phosphodiesterases plays a key role in the regulation of cAMP signalling in mammals. In the present paper, we report the characterization and subcellular localization of TcPDE1, the first cAMP-specific phosphodiesterase to be identified from Trypanosoma cruzi. TcPDE1 is part of a small gene family and encodes a 929-amino-acid protein that can complement a heat-shock-sensitive yeast mutant deficient in phospho-diesterase genes. Recombinant TcPDE1 strongly associates with membranes and cannot be released with NaCl or sodium cholate, suggesting that it is an integral

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47

Kesler, Cristina T., Daniel Gioeli, Mark R. Conaway, Michael J. Weber, and Bryce M. Paschal. "Subcellular Localization Modulates Activation Function 1 Domain Phosphorylation in the Androgen Receptor." Molecular Endocrinology 21, no. 9 (2007): 2071–84. http://dx.doi.org/10.1210/me.2007-0240.

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Abstract Although the steady-state distribution of the androgen receptor (AR) is predominantly nuclear in androgen-treated cells, androgen-bound AR shuttles between the nucleus and the cytoplasm. In the present study we have addressed how nucleocytoplasmic shuttling contributes to the regulation of AR. Nuclear transport signal fusions were used to force AR localization to the nucleus or cytoplasm of prostate cancer cells, and the effect of localization on shuttling, transcription, androgen binding, and phosphorylation was determined. Fusing the simian virus 40 nuclear localization signal or c-

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48

Labarde, Audrey, Lina Jakutyte, Cyrille Billaudeau, et al. "Temporal compartmentalization of viral infection in bacterial cells." Proceedings of the National Academy of Sciences 118, no. 28 (2021): e2018297118. http://dx.doi.org/10.1073/pnas.2018297118.

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Virus infection causes major rearrangements in the subcellular architecture of eukaryotes, but its impact in prokaryotic cells was much less characterized. Here, we show that infection of the bacterium Bacillus subtilis by bacteriophage SPP1 leads to a hijacking of host replication proteins to assemble hybrid viral–bacterial replisomes for SPP1 genome replication. Their biosynthetic activity doubles the cell total DNA content within 15 min. Replisomes operate at several independent locations within a single viral DNA focus positioned asymmetrically in the cell. This large nucleoprotein complex

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49

Zhu, Yi, Jiaqi Liu, Joun Park, Priyamvada Rai, and Rong G. Zhai. "Subcellular compartmentalization of NAD+ and its role in cancer: A sereNADe of metabolic melodies." Pharmacology & Therapeutics 200 (August 2019): 27–41. http://dx.doi.org/10.1016/j.pharmthera.2019.04.002.

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50

Föger, Niko, Silvia Bulfone-Paus, Andrew C. Chan, and Kyeong-Hee Lee. "Subcellular compartmentalization of FADD as a new level of regulation in death receptor signaling." FEBS Journal 276, no. 15 (2009): 4256–65. http://dx.doi.org/10.1111/j.1742-4658.2009.07134.x.

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