Relevant bibliographies by topics / Cytoplasmic and Nuclear Transcription

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Cytoplasmic and Nuclear Transcription'

Author: Grafiati
Published: 4 June 2021
Last updated: 4 February 2022

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Journal articles on the topic "Cytoplasmic and Nuclear Transcription"

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Billin, Andrew N., Alanna L. Eilers, Kathryn L. Coulter, Jennifer S. Logan, and Donald E. Ayer. "MondoA, a Novel Basic Helix-Loop-Helix–Leucine Zipper Transcriptional Activator That Constitutes a Positive Branch of a Max-Like Network." Molecular and Cellular Biology 20, no. 23 (2000): 8845–54. http://dx.doi.org/10.1128/mcb.20.23.8845-8854.2000.

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ABSTRACT Max is a common dimerization partner for a family of transcription factors (Myc, Mad [or Mxi]), and Mnt [or Rox] proteins) that regulate cell growth, proliferation, and apoptosis. We recently characterized a novel Max-like protein, Mlx, which interacts with Mad1 and Mad4. Here we describe the cloning and functional characterization of a new family of basic helix-loop-helix–leucine zipper heterodimeric partners for Mlx termed the Mondo family. MondoA forms homodimers weakly and does not interact with Max or members of the Myc or Mad families. MondoA and Mlx associate in vivo, and surpr
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Tolwinski, Nicholas S., and Eric Wieschaus. "Armadillo nuclear import is regulated by cytoplasmic anchor Axin and nuclear anchor dTCF/Pan." Development 128, no. 11 (2001): 2107–17. http://dx.doi.org/10.1242/dev.128.11.2107.

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Drosophila melanogaster Armadillo plays two distinct roles during development. It is a component of adherens junctions, and functions as a transcriptional activator in response to Wingless signaling. In the current model, Wingless signal causes stabilization of cytoplasmic Armadillo allowing it to enter the nucleus where it can activate transcription. However, the mechanism of nuclear import and export remains to be elucidated. In this study, we show that two gain-of-function alleles of Armadillo activate Wingless signaling by different mechanisms. The S10 allele was previously found to locali
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Oh, Jaewook, and Steven S. Broyles. "Host Cell Nuclear Proteins Are Recruited to Cytoplasmic Vaccinia Virus Replication Complexes." Journal of Virology 79, no. 20 (2005): 12852–60. http://dx.doi.org/10.1128/jvi.79.20.12852-12860.2005.

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ABSTRACT The initiation and termination of vaccinia virus postreplicative transcription have been reported to require cellular proteins, some of which are believed to be nuclear proteins. Vaccinia virus replicates in the cytoplasmic compartment of the cell, raising questions as to whether vaccinia virus has access to nuclear proteins. This was addressed here by following the fate of several nuclear proteins after infection of cells with vaccinia virus. The nuclear transcription factors YY1, SP1, and TATA binding protein were found to colocalize with virus replication complexes in the cytoplasm
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Grunau, Christoph, Susanne Voigt, Ralph Dobler, Damian Dowling, and Klaus Reinhardt. "The Cytoplasm Affects the Epigenome in Drosophila melanogaster." Epigenomes 2, no. 3 (2018): 17. http://dx.doi.org/10.3390/epigenomes2030017.

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Cytoplasmic components and their interactions with the nuclear genome may mediate patterns of phenotypic expression to form a joint inheritance system. However, proximate mechanisms underpinning these interactions remain elusive. To independently assess nuclear genetic and epigenetic cytoplasmic effects, we created a full-factorial design in which representative cytoplasms and nuclear backgrounds from each of two geographically disjunct populations of Drosophila melanogaster were matched together in all four possible combinations. To capture slowly-accumulating epimutations in addition to imme
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Tam, Winnie F., Linda H. Lee, Laura Davis та Ranjan Sen. "Cytoplasmic Sequestration of Rel Proteins by IκBα Requires CRM1-Dependent Nuclear Export". Molecular and Cellular Biology 20, № 6 (2000): 2269–84. http://dx.doi.org/10.1128/mcb.20.6.2269-2284.2000.

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ABSTRACT Rel and IκB protein families form a complex cellular regulatory network. A major regulatory function of IκB proteins is to retain Rel proteins in the cell cytoplasm. In addition, IκB proteins have also been postulated to serve nuclear functions. These include the maintenance of inducible NF-κB-dependent gene transcription, as well as termination of inducible transcription. We show that IκBα shuttles between the nucleus and the cytoplasm, utilizing the nuclear export receptor CRM1. A CRM1-binding export sequence was identified in the N-terminal domain of IκBα but not in that of IκBβ or
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McGrath, James, and Davor Solter. "Nucleocytoplasmic interactions in the mouse embryo." Development 97, Supplement (1986): 277–89. http://dx.doi.org/10.1242/dev.97.supplement.277.

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Fertilized mammalian ova consist of haploid genomes derived from both parents and cytoplasmic components inherited largely from the female parent. These three cellular compartments must successfully interact with each other and with their environment for development to proceed. These interactions require the transposition of nuclear and cytoplasmic products between cellular compartments with resultant alteration of gene transcription and the cytoplasmic expression of preformed or newly synthesized gene products. We have investigated nuclear/cytoplasmic interactions in the mouse embryo via the
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Wimmer, Robert J., Yewei Liu, Tova Neustadt Schachter, David P. Stonko, Bradford E. Peercy, and Martin F. Schneider. "Mathematical modeling reveals modulation of both nuclear influx and efflux of Foxo1 by the IGF-I/PI3K/Akt pathway in skeletal muscle fibers." American Journal of Physiology-Cell Physiology 306, no. 6 (2014): C570—C584. http://dx.doi.org/10.1152/ajpcell.00338.2013.

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Foxo family transcription factors contribute to muscle atrophy by promoting transcription of the ubiquitin ligases muscle-specific RING finger protein and muscle atrophy F-box/atrogin-1. Foxo transcriptional effectiveness is largely determined by its nuclear-cytoplasmic distribution, with unphosphorylated Foxo1 transported into nuclei and phosphorylated Foxo1 transported out of nuclei. We expressed the fluorescent fusion protein Foxo1-green fluorescent protein (GFP) in cultured adult mouse flexor digitorum brevis muscle fibers and tracked the time course of the nuclear-to-cytoplasmic Foxo1-GFP
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Laribee, R. Nicholas, and Ronit Weisman. "Nuclear Functions of TOR: Impact on Transcription and the Epigenome." Genes 11, no. 6 (2020): 641. http://dx.doi.org/10.3390/genes11060641.

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The target of rapamycin (TOR) protein kinase is at the core of growth factor- and nutrient-dependent signaling pathways that are well-known for their regulation of metabolism, growth, and proliferation. However, TOR is also involved in the regulation of gene expression, genomic and epigenomic stability. TOR affects nuclear functions indirectly through its activity in the cytoplasm, but also directly through active nuclear TOR pools. The mechanisms by which TOR regulates its nuclear functions are less well-understood compared with its cytoplasmic activities. TOR is an important pharmacological
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Kumar, K. Prasanna, Kevin M. McBride, Brian K. Weaver, Colin Dingwall, and Nancy C. Reich. "Regulated Nuclear-Cytoplasmic Localization of Interferon Regulatory Factor 3, a Subunit of Double-Stranded RNA-Activated Factor 1." Molecular and Cellular Biology 20, no. 11 (2000): 4159–68. http://dx.doi.org/10.1128/mcb.20.11.4159-4168.2000.

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ABSTRACT Viral double-stranded RNA (dsRNA) generated during the course of infection leads to the activation of a latent transcription factor, dsRNA-activated factor 1 (DRAF1). DRAF1 binds to a DNA target containing the type I interferon-stimulated response element and induces transcription of responsive genes. DRAF1 is a multimeric transcription factor containing the interferon regulatory factor 3 (IRF-3) protein and one of the histone acetyl transferases, CREB binding protein (CBP) or p300 (CBP/p300). In uninfected cells, the IRF-3 component of DRAF1 resides in the cytoplasm. The cytoplasmic
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De Jesús-González, Luis Adrián, Selvin Palacios-Rápalo, José Manuel Reyes-Ruiz, et al. "The Nuclear Pore Complex Is a Key Target of Viral Proteases to Promote Viral Replication." Viruses 13, no. 4 (2021): 706. http://dx.doi.org/10.3390/v13040706.

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Various viruses alter nuclear pore complex (NPC) integrity to access the nuclear content favoring their replication. Alteration of the nuclear pore complex has been observed not only in viruses that replicate in the nucleus but also in viruses with a cytoplasmic replicative cycle. In this last case, the alteration of the NPC can reduce the transport of transcription factors involved in the immune response or mRNA maturation, or inhibit the transport of mRNA from the nucleus to the cytoplasm, favoring the translation of viral mRNAs or allowing access to nuclear factors necessary for viral repli
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Dissertations / Theses on the topic "Cytoplasmic and Nuclear Transcription"

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Vu, Anthony. "Nuclear and Cytoplasmic Roles of the Transcription factor REST." Diss., [La Jolla] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p1469263.

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Thesis (M.S.)--University of California, San Diego, 2009.<br>Title from first page of PDF file (viewed Oct. 7, 2009). Available via ProQuest Digital Dissertations. Includes bibliographical references (p. 58-61).
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Li, Yong. "Cytoplasmic domain of CD44 acts as a nuclear transcription regulator." Karlsruhe : FZKA, 2004. http://bibliothek.fzk.de/zb/berichte/FZKA6917.pdf.

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Holter, Elin. "Modulation of nuclear receptor activity by a unique class of corepressors /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7140-039-7/.

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Osman, Waffa. "Modulation of nuclear receptor function by interacting proteins /." Stockholm : Karolinska institutet, 2007. http://diss.kib.ki.se/2007/978-91-7357-264-4/.

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Ruan, Xuan 1974. "Differential circadian regulation of Bmal1 transcription by orphan nuclear receptors." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=112358.

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In mammals, circadian rhythms are generated by transcriptional-translational feedback loops consisting of a set of clock genes and their protein products. Among them, Bmal1 is a critical clock gene in generating and maintaining circadian rhythms. Moreover, orphan nuclear receptors REV-ERBs and RORs were known to respectively repress and activate Bmal1 transcription. In our study, we further demonstrated that: (1) REV-ERBalpha might be the main regulator in maintaining Bmal1 oscillation in thymus. (2) Rorgamma mRNA is constant in muscle and testis, and rhythmic in liver, while Rorgammat mRNA is
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Li, Yong [Verfasser]. "Cytoplasmic domain of CD44 acts as a nuclear transcription regulator / Forschungszentrum Karlsruhe GmbH, Karlsruhe. Yong Li." Karlsruhe : FZKA, 2004. http://d-nb.info/971463921/34.

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Loinder, Kristina. "Nuclear receptor corepressor N-CoR : role in transcriptional repression /." Linköping : Univ, 2004. http://www.bibl.liu.se/liupubl/disp/disp2004/med869s.pdf.

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Wallén, Åsa. "Some aspects of nuclear receptor function in the CNS : novel roles of Nurr1 and RXR in developing and mature neurons /." Stockholm, 2002.

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Lindquist, Per J. G. "Molecular cloning and characterization of the murine acyl-CoA thioesterase CTE-I /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-878-5/.

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Skogsberg, Josefin. "PPAR delta : its role in cholesterol metabolism /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-604-9.

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Books on the topic "Cytoplasmic and Nuclear Transcription"

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1945-, Fruchart J. C., ed. Peroxisome proliferator activated receptors: From basic science to clinical applications. Kluwer Academic Pub., 2002.

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Yang, Weidong, ed. Nuclear-Cytoplasmic Transport. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-77309-4.

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Gronemeyer, Hinrich. Transcription factors 3: nuclear receptors. Academic Press, 1995.

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Rakesh, Kumar. Nuclear signaling pathways and targeting transcription in cancer. Humana Press, 2014.

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Pontes, Olga, and Hailing Jin, eds. Nuclear Functions in Plant Transcription, Signaling and Development. Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2386-1.

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Kumar, Rakesh, ed. Nuclear Signaling Pathways and Targeting Transcription in Cancer. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-8039-6.

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Nuclear receptors: Current concepts and future challenges. Springer, 2010.

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Furlong, Eileen E. M. Tissue-specific regulation of gene expression by the transcription factors Ying-Yang 1 and nuclear factor 1. University College Dublin, 1996.

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Fenili, Daniela. Same-cell, high-resolution tracking of nuclear and cytoplasmic fluorescent signals in live, transfected cerebellar neurons. National Library of Canada, 2003.

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Retnakaran, Ravi. Identification of RVR, a novel orphan nuclear receptor that acts as a negative regulator of transcription. National Library of Canada, 1994.

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Book chapters on the topic "Cytoplasmic and Nuclear Transcription"

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Levy, D. E., R. Raz, J. E. Durbin, H. Bluyssen, R. Muzaffar, and S. Pisharody. "Cytoplasmic Transcription Factors: Mediators of Cytokine Signaling." In Inflammation: Mechanisms and Therapeutics. Birkhäuser Basel, 1995. http://dx.doi.org/10.1007/978-3-0348-7343-7_6.

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Schmitz, M. Lienhard, and Patrick A. Baeuerle. "Signal Transduction from the Cytoplasm to the Cell Nucleus by NF-κB/Rel Transcription Factors." In Signalling Mechanisms — from Transcription Factors to Oxidative Stress. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79675-3_23.

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Jackson, Dean A. "Thinking Holistically About Gene Transcription." In Advances in Nuclear Architecture. Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9899-3_7.

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Sassone-Corsi, P., S. J. Busch, F. Schlotter, et al. "Nuclear Oncogenes as Transcription Factors." In Chemical Carcinogenesis 2. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3694-9_1.

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Smith, Gary D. "Control of Oocyte Nuclear and Cytoplasmic Maturation." In Assisted Fertilization and Nuclear Transfer in Mammals. Humana Press, 2001. http://dx.doi.org/10.1007/978-1-59259-369-9_3.

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McGrath, James, and Davor Solter. "Nuclear and Cytoplasmic Transfer in Mammalian Embryos." In Manipulation of Mammalian Development. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2143-9_2.

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Chatzifrangkeskou, Maria, and Eric O’Neill. "Nuclear/Cytoplasmic Fractionation to Study Hippo Effectors." In Methods in Molecular Biology. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8910-2_10.

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Albertini, David F., Dineli Wickramasinghe, Susan Messinger, Britta A. Mattson, and Carlos E. Plancha. "Nuclear and Cytoplasmic Changes During Oocyte Maturation." In Preimplantation Embryo Development. Springer New York, 1993. http://dx.doi.org/10.1007/978-1-4613-9317-7_1.

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Peercy, Bradford E., and Martin F. Schneider. "Mathematical Modeling of Nuclear Trafficking of FOXO Transcription Factors." In FOXO Transcription Factors. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8900-3_17.

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Meagher, Richard B., Muthugapatti K. Kandasamy, and Lori King. "Actin Functions in the Cytoplasmic and Nuclear Compartments." In The Plant Cytoskeleton. Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-0987-9_1.

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Conference papers on the topic "Cytoplasmic and Nuclear Transcription"

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Shiraishi, Toshihiko, and Akitoshi Nishijima. "A Study of a Mechanism of Cell Proliferation Promotion of Cultured Osteoblasts by Mechanical Vibration." In ASME 2018 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2018. http://dx.doi.org/10.1115/imece2018-87364.

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This paper describes a mechanism of cell proliferation promotion of cultured osteoblasts by mechanical vibration focusing on β-catenin. 12.5 Hz and 0.5 G mechanical vibration was reported to promote the cell proliferation of cultured osteoblasts in plane culture. That is because the mechanical vibration weakens cell-cell adhesion, promotes to pile up cells, and allows cells to form multilayer structure. However, it has not been clarified why cells continue cell division after their monolayer confluent state. Here we show that mechanical vibration not only weakens cell-cell adhesion bound by β-
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Al-Mehdi, Abu-Bakr, Viktor Pastukh, Darla Reed, Brad Swiger, and Gina Bardwell. "Discrete Roles Of Cytoplasmic And Nuclear Reactive Oxygen Species (ROS) In Hypoxia-Induced Transcriptional Regulation." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5489.

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Graziano, Laura J., Xue Zhang, Yabin Cheng, et al. "Abstract 5031: Melanoma progression involves a profound nuclear to cytoplasmic shift of the transcription factor SUM-6 (specifically upregulated in melanoma gene six)." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-5031.

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Reeves, Anthony P., Eric J. Seibel, Michael G. Meyer, Tatiyana Apanasovich, and Alberto Biancardi. "Nuclear cytoplasmic cell evaluation from 3D optical CT microscope images." In SPIE Medical Imaging, edited by Bram van Ginneken and Carol L. Novak. SPIE, 2012. http://dx.doi.org/10.1117/12.912399.

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Levin, Pavel A., Thiruvengadam Arumugam, David J. McConkey, Shrikanth Reddy, and Craig D. Logsdon. "Abstract 3920: EphA2 transcription is regulated by activation of Ras / MEK2 / cytoplasmic ERK pathway in pancreatic cancer." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3920.

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Koroleva, S. V. "Results of sweet pepper breeding based on the cytoplasmic-nuclear male sterility." In CURRENT STATE, PROBLEMS AND PROSPECTS OF THE DEVELOPMENT OF AGRARIAN SCIENCE. Federal State Budget Scientific Institution “Research Institute of Agriculture of Crimea”, 2019. http://dx.doi.org/10.33952/09.09.2019.79.

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Wehling, L., L. Keegan, J. Schmitt, et al. "Mathematical modeling of YAP and TAZ nuclear/cytoplasmic shuttling in liver cancer cells." In 37. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0040-1722055.

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Jaidevi, K., Ann Mathew, and S. Hemalatha. "Nuclear to cytoplasmic ratio & cellbody analysis of virtual biopsy images for diagnosing diseases." In 2014 International Conference on Circuit, Power and Computing Technologies (ICCPCT). IEEE, 2014. http://dx.doi.org/10.1109/iccpct.2014.7054874.

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Burton, Liza J., and Valerie Odero-Marah. "Abstract 1602: Snail transcription factor regulates nuclear cathepsin L activity." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1602.

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Anibire, Oladipupo O., Oyinloye Jose, Kenyada Williams, Billy R. Ballard, Michael G. Izban, and Dana Marshall. "Abstract PO-233: HPV+ and HPV- HNSCC show similar nrf2 nuclear and cytoplasmic staining patterns." In Abstracts: AACR Virtual Conference: Thirteenth AACR Conference on the Science of Cancer Health Disparities in Racial/Ethnic Minorities and the Medically Underserved; October 2-4, 2020. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7755.disp20-po-233.

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Reports on the topic "Cytoplasmic and Nuclear Transcription"

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Sharp, Zelton D. Nuclear Dynamics of BRCA1-Dependent Transcription Regulation. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada463827.

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Newton, K. J. Molecular analyses of nuclear-cytoplasmic interactions affecting plant growth and yield. Final technical report. Office of Scientific and Technical Information (OSTI), 1998. http://dx.doi.org/10.2172/674901.

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