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Academic literature on the topic 'Nucleolus'

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Published: 4 June 2021
Last updated: 22 February 2023

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Journal articles on the topic "Nucleolus"

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Ukil, Leena, Colin P. De Souza, Hui-Lin Liu, and Stephen A. Osmani. "Nucleolar Separation from Chromosomes during Aspergillus nidulans Mitosis Can Occur Without Spindle Forces." Molecular Biology of the Cell 20, no. 8 (April 15, 2009): 2132–45. http://dx.doi.org/10.1091/mbc.e08-10-1046.

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How the nucleolus is segregated during mitosis is poorly understood and occurs by very different mechanisms during closed and open mitosis. Here we report a new mechanism of nucleolar segregation involving removal of the nucleolar-organizing regions (NORs) from nucleoli during Aspergillus nidulans mitosis. This involves a double nuclear envelope (NE) restriction which generates three NE-associated structures, two daughter nuclei (containing the NORs), and the nucleolus. Therefore, a remnant nucleolar structure can exist in the cytoplasm without NORs. In G1, this parental cytoplasmic nucleolus undergoes sequential disassembly releasing nucleolar proteins to the cytoplasm as nucleoli concomitantly reform in daughter nuclei. By depolymerizing microtubules and mutating spindle assembly checkpoint function, we demonstrate that a cycle of nucleolar “segregation” can occur without a spindle in a process termed spindle-independent mitosis (SIM). During SIM physical separation of the NOR from the nucleolus occurs, and NE modifications promote expulsion of the nucleolus to the cytoplasm. Subsequently, the cytoplasmic nucleolus is disassembled and rebuilt at a new site around the nuclear NOR. The data demonstrate the existence of a mitotic machinery for nucleolar segregation that is normally integrated with mitotic spindle formation but that can function without it.
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Chen, Hongying, Torsten Wurm, Paul Britton, Gavin Brooks, and Julian A. Hiscox. "Interaction of the Coronavirus Nucleoprotein with Nucleolar Antigens and the Host Cell." Journal of Virology 76, no. 10 (May 15, 2002): 5233–50. http://dx.doi.org/10.1128/jvi.76.10.5233-5250.2002.

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ABSTRACT Coronavirus nucleoproteins (N proteins) localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The nucleolus is the site of ribosome biogenesis and sequesters cell cycle regulatory complexes. Two of the major components of the nucleolus are fibrillarin and nucleolin. These proteins are involved in nucleolar assembly and ribosome biogenesis and act as chaperones for the import of proteins into the nucleolus. We have found that fibrillarin is reorganized in primary cells infected with the avian coronavirus infectious bronchitis virus (IBV) and in continuous cell lines that express either IBV or mouse hepatitis virus N protein. Both N protein and a fibrillarin-green fluorescent protein fusion protein colocalized to the perinuclear region and the nucleolus. Pull-down assays demonstrated that IBV N protein interacted with nucleolin and therefore provided a possible explanation as to how coronavirus N proteins localize to the nucleolus. Nucleoli, and proteins that localize to the nucleolus, have been implicated in cell growth-cell cycle regulation. Comparison of cells expressing IBV N protein with controls indicated that cells expressing N protein had delayed cellular growth. This result could not to be attributed to apoptosis. Morphological analysis of these cells indicated that cytokinesis was disrupted, an observation subsequently found in primary cells infected with IBV. Coronaviruses might therefore delay the cell cycle in interphase, where maximum translation of viral mRNAs can occur.
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Maddox-Hyttel, Poul, Bolette Bjerregaard, and Jozef Laurincik. "Meiosis and embryo technology: renaissance of the nucleolus." Reproduction, Fertility and Development 17, no. 2 (2005): 3. http://dx.doi.org/10.1071/rd04108.

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The nucleolus is the site of rRNA and ribosome production. This organelle presents an active fibrillogranular ultrastructure in the oocyte during the growth of the gamete but, at the end of the growth phase, the nucleolus is transformed into an inactive remnant that is dissolved when meiosis is resumed at germinal vesicle breakdown. Upon meiosis, structures resembling the nucleolar remnant, now referred to as nucleolus precursor bodies (NPBs), are established in the pronuclei. These entities harbour the development of fibrillogranular nucleoli and re-establishment of nucleolar function in conjunction with the major activation of the embryonic genome. This so-called nucleologenesis occurs at a species-specific time of development and can be classified into two different models: one where nucleolus development occurs inside the NPBs (e.g. cattle) and one where the nucleolus is formed on the surface of the NPBs (e.g. pigs). A panel of nucleolar proteins with functions during rDNA transcription (topoisomerase I, RNA polymerase I and upstream binding factor) and early (fibrillarin) or late rRNA processing (nucleolin and nucleophosmin) are localised to specific compartments of the oocyte nucleolus and those engaged in late processing are, to some degree, re-used for nucleologenesis in the embryo, whereas the others require de novo embryonic transcription in order to be allocated to the developing nucleolus. In the oocyte, inactivation of the nucleolus coincides with the acquisition of full meiotic competence, a parameter that may be of importance in relation to in vitro oocyte maturation. In embryo, nucleologenesis may be affected by technological manipulations: in vitro embryo production apparently has no impact on this process in cattle, whereas in the pig this technology results in impaired nucleologenesis. In cattle, reconstruction of embryos by nuclear transfer results in profound disturbances in nucleologenesis. In conclusion, the nucleolus is an organelle of great importance for the developmental competence of oocytes and embryos and may serve as a morphological marker for the completion of oocyte growth and normality of activation of the embryonic genome.
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Chen, Hung-Kai, Chi-Yun Pai, Jing-Yi Huang, and Ning-Hsing Yeh. "Human Nopp140, Which Interacts with RNA Polymerase I: Implications for rRNA Gene Transcription and Nucleolar Structural Organization." Molecular and Cellular Biology 19, no. 12 (December 1, 1999): 8536–46. http://dx.doi.org/10.1128/mcb.19.12.8536.

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ABSTRACT Nopp140 is thought to shuttle between nucleolus and cytoplasm. However, the predominant nucleolar localization of Nopp140 homologues from different species suggests that Nopp140 is also involved in events occurring within the nucleolus. In this study, we demonstrated that the largest subunit of RNA polymerase I, RPA194, was coimmunoprecipitated with the human Nopp140 (hNopp140). Such an interaction is mediated through amino acids 204 to 382 of hNopp140. By double immunofluorescence, hNopp140 was colocalized with RNA polymerase I at the rDNA (rRNA genes) transcription active foci in the nucleolus. These results suggest that Nopp140 can interact with RNA polymerase I in vivo. Transfected cells expressing the amino-terminal half of hNopp140, hNopp140N382 (amino acids 1 to 382), displayed altered nucleoli with crescent-shaped structures. This phenotype is reminiscent of the segregated nucleoli induced by actinomycin D treatment, which is known to inhibit rRNA synthesis. Consistently, the hNopp140N382 protein mislocalized the endogenous RNA polymerase I and shut off cellular rRNA gene transcription as revealed by an in situ run-on assay. These dominant negative effects of the mutant hNopp140N382 suggest that Nopp140 plays an essential role in rDNA transcription. Interestingly, ectopic expression of hNopp140 to a very high level caused the formation of a transcriptionally inactive spherical structure occupying the entire nucleolar area which trapped the RNA polymerase I, fibrillarin, and hNopp140 but excluded the nucleolin. The mislocalizations of these nucleolar proteins after hNopp140 overexpression imply that Nopp140 may also play roles in maintenance of nucleolar integrity.
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Wang, Jianyue, and Feixiong Zhang. "Nucleolus disassembly and distribution of segregated nucleolar material in prophase of root-tip meristematic cells in Triticum aestivum L." Archives of Biological Sciences 67, no. 2 (2015): 405–10. http://dx.doi.org/10.2298/abs140810007w.

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This paper presents details of the process of nucleolar disassembly, studied by conventional transmission electron microscopy (TEM) in wheat root cells. In early prophase, chromatin condensation and irregular nucleolar morphology are observed, with many small particles appearing around the nucleolus. In middle prophase, the nucleolus radiates outwards; in late prophase, the fine structure of the nucleolus disappears and nucleolar material diffuses away. Using ?en bloc? silver-staining to distinguish between nucleoli and chromatin, we observed that the dispersed nucleolar material aggregates around the chromatin, forming a sheath-like perichromosomal structure that coats the chromosomes in late prophase.
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Dundr, M., G. H. Leno, N. Lewis, D. Rekosh, M. L. Hammarskjoid, and M. O. Olson. "Location of the HIV-1 Rev protein during mitosis: inactivation of the nuclear export signal alters the pathway for postmitotic reentry into nucleoli." Journal of Cell Science 109, no. 9 (September 1, 1996): 2239–51. http://dx.doi.org/10.1242/jcs.109.9.2239.

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The HIV-1 Rev protein localizes predominantly to the nucleolus of HIV-1-infected or Rev-expressing cells. The subcellular location of Rev during mitotic nucleolar disintegration was examined at various stages of mitosis in synchronized Rev-expressing CMT3 cells. During early prophase Rev was predominantly located in disintegrating nucleoli and began to accumulate at the peripheral regions of chromosomes in late prophase, eventually distributing uniformly on all chromosomes in prometaphase. In anaphase Rev remained associated with the perichromosomal regions, but significant amounts of Rev were also seen in numerous nucleolus-derived foci. The movement of Rev from disintegrating nucleoli to perichromosomal regions and foci was similar to that of nonribosomal nucleolar proteins, including fibrillarin, nucleolin, protein B23 and p52 of the granular component. During telophase Rev remained associated with perichromosomal regions and mitotic foci until the nuclear envelope started to reform. When nuclear envelope formation was complete in late telophase, nonribosomal nucleolar proteins were present in prenucleolar bodies (PNBs) which were eventually incorporated into nucleoli; at the same time, Rev was excluded from nuclei. In contrast, a trans-dominant negative Rev protein containing an inactive nuclear export signal reentered nuclei by the nonribosomal nucleolar protein pathway in late telophase, associating with PNBs and reformed nucleoli. Rev protein reentry into postmitotic nuclei was delayed until early G1 phase, but before the arrival of ribosomal protein S6. Thus, Rev behaves like a nonribosomal nucleolar protein through mitosis until early telophase; however, its nuclear reentry seems to require reestablishment of both a nuclear import system and active nucleoli.
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Dundr, Miroslav, Tom Misteli, and Mark O. J. Olson. "The Dynamics of Postmitotic Reassembly of the Nucleolus." Journal of Cell Biology 150, no. 3 (August 7, 2000): 433–46. http://dx.doi.org/10.1083/jcb.150.3.433.

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Mammalian cell nucleoli disassemble at the onset of M-phase and reassemble during telophase. Recent studies showed that partially processed preribosomal RNA (pre-rRNA) is preserved in association with processing components in the perichromosomal regions (PRs) and in particles called nucleolus-derived foci (NDF) during mitosis. Here, the dynamics of nucleolar reassembly were examined for the first time in living cells expressing fusions of the processing-related proteins fibrillarin, nucleolin, or B23 with green fluorescent protein (GFP). During telophase the NDF disappeared with a concomitant appearance of material in the reforming nuclei. Prenucleolar bodies (PNBs) appeared in nuclei in early telophase and gradually disappeared as nucleoli formed, strongly suggesting the transfer of PNB components to newly forming nucleoli. Fluorescence recovery after photobleaching (FRAP) showed that fibrillarin-GFP reassociates with the NDF and PNBs at rapid and similar rates. The reentry of processing complexes into telophase nuclei is suggested by the presence of pre-rRNA sequences in PNBs. Entry of specific proteins into the nucleolus approximately correlated with the timing of processing events. The mitotically preserved processing complexes may be essential for regulating the distribution of components to reassembling daughter cell nucleoli.
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Intine, Robert V., Miroslav Dundr, Alex Vassilev, Elena Schwartz, Yingmin Zhao, Yingxin Zhao, Melvin L. DePamphilis, and Richard J. Maraia. "Nonphosphorylated Human La Antigen Interacts with Nucleolin at Nucleolar Sites Involved in rRNA Biogenesis." Molecular and Cellular Biology 24, no. 24 (December 15, 2004): 10894–904. http://dx.doi.org/10.1128/mcb.24.24.10894-10904.2004.

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ABSTRACT La is a RNA-binding protein implicated in multiple pathways related to the production of tRNAs, ribosomal proteins, and other components of the translational machinery (D. J. Kenan and J. D. Keene, Nat. Struct. Mol. Biol. 11 :303-305, 2004). While most La is phosphorylated and resides in the nucleoplasm, a fraction is in the nucleolus, the site of ribosome production, although the determinants of this localization are incompletely known. In addition to its conserved N-terminal domain, human La harbors a C-terminal domain that contains an atypical RNA recognition motif and a short basic motif (SBM) adjacent to phosphoserine-366. We report that nonphosphorylated La (npLa) is concentrated in nucleolar sites that correspond to the dense fibrillar component that harbors nascent pol I transcripts as well as fibrillarin and nucleolin, which function in early phases of rRNA maturation. Affinity purification and native immunoprecipitation of La and fluorescence resonance energy transfer in the nucleolus reveal close association with nucleolin. Moreover, La lacking the SBM does not localize to nucleoli. Lastly, La exhibits SBM-dependent, phosphorylation-sensitive interaction with nucleolin in a yeast two-hybrid assay. The data suggest that interaction with nucleolin is, at least in part, responsible for nucleolar accumulation of La and that npLa may be involved in ribosome biogenesis.
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Kill, I. R. "Localisation of the Ki-67 antigen within the nucleolus. Evidence for a fibrillarin-deficient region of the dense fibrillar component." Journal of Cell Science 109, no. 6 (June 1, 1996): 1253–63. http://dx.doi.org/10.1242/jcs.109.6.1253.

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The Ki-67 antigen is detected in proliferating cells in all phases of the cell division cycle. Throughout most of interphase, the Ki-67 antigen is localised within the nucleous. To learn more about the relationship between the Ki-67 antigen and the nucleolus, we have compared the distribution of Ki-67 antibodies with that of a panel of antibodies reacting with nucleolar components by confocal laser scanning microscopy of normal human dermal fibroblasts in interphase stained in a double indirect immunofluorescence assay. During early G1, the Ki-67 antigen is detected at a large number of discrete foci throughout the nucleoplasm, extending to the nuclear envelope. During S-phase and G2, the antigen is located in the nucleolus. Double indirect immunofluorescence studies have revealed that during early to mid G1 the Ki-67 antigen is associated with reforming nucleoli within discrete domains which are distinct from domains containing two of the major nucleolar antigens fibrillarin and RNA polymerase I. Within mature nucleoli the Ki-67 antigen is absent from regions containing RNA polymerase I and displays only partial co-localisation within domains containing either fibrillarin or B23/nucleophosmin. Following disruption of nucleolar structure, induced by treatment of cells with the drug 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole or with actinomycin D, the Ki-67 antigen translocates to nucleoplasmic foci which are associated with neither fibrillarin nor RNA polymerase I. However, in treated cells the Ki-67 Ag remains associated with, but not co-localised to, regions containing B23/nucleophosmin. Our observations suggest that the Ki-67 antigen associates with a fibrillarin-deficient region of the dense fibrillar component of the nucleolus. Integrity of this region is lost following either nucleolar dispersal or nucleolar segregation.
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Pontvianne, Frederic, Isabel Matía, Julien Douet, Sylvette Tourmente, Francisco J. Medina, Manuel Echeverria, and Julio Sáez-Vásquez. "Characterization of AtNUC-L1 Reveals a Central Role of Nucleolin in Nucleolus Organization and Silencing of AtNUC-L2 Gene in Arabidopsis." Molecular Biology of the Cell 18, no. 2 (February 2007): 369–79. http://dx.doi.org/10.1091/mbc.e06-08-0751.

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Nucleolin is one of the most abundant protein in the nucleolus and is a multifunctional protein involved in different steps of ribosome biogenesis. In contrast to animals and yeast, the genome of the model plant Arabidopsis thaliana encodes two nucleolin-like proteins, AtNUC-L1 and AtNUC-L2. However, only the AtNUC-L1 gene is ubiquitously expressed in normal growth conditions. Disruption of this AtNUC-L1 gene leads to severe plant growth and development defects. AtNUC-L1 is localized in the nucleolus, mainly in the dense fibrillar component. Absence of this protein in Atnuc-L1 plants induces nucleolar disorganization, nucleolus organizer region decondensation, and affects the accumulation levels of pre-rRNA precursors. Remarkably, in Atnuc-L1 plants the AtNUC-L2 gene is activated, suggesting that AtNUC-L2 might rescue, at least partially, the loss of AtNUC-L1. This work is the first description of a higher eukaryotic organism with a disrupted nucleolin-like gene and defines a new role for nucleolin in nucleolus structure and rDNA chromatin organization.
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Dissertations / Theses on the topic "Nucleolus"

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Jellbauer, Stephan. "The nucleolus." Diss., lmu, 2009. http://nbn-resolving.de/urn:nbn:de:bvb:19-101704.

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Inder, Kerry, and n/a. "The Functional Role of NRAP in the Nucleolus." Griffith University. School of Biomolecular and Biomedical Science, 2006. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20070201.133347.

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The nucleolus is the site for rRNA synthesis, a process requiring the recruitment of many proteins involved in ribosomal biogenesis. Nrap is a novel nucleolar protein found to be present in all eukaryotes. Preliminary characterisation of Nrap suggested it was likely to participate in ribosome biogenesis but as with many other nucleolar proteins, the functional role of Nrap is largely unknown. In this study, the role of mammalian Nrap in the nucleolus and in ribosome biogenesis was explored. Initially, a number of tools were generated to investigate Nrap function. This involved raising and purifying a polyclonal antibody against the N-terminal region of Nrap. The anti-Nrap antibody was found to detect two Nrap bands in mouse fibroblast cells, possibly corresponding to the two mouse Nrap isoforms, and . In addition, mammalian expression vectors containing the full Nrap sequence as well as deletion constructs were created. The subcellular localisation of each construct was observed by fluorescent microscopy. It was revealed that recombinant Nrap did not localise to the nucleolus, possibly because it was exported to undergo degradation by the 26S proteasome. Two putative NLSs were found to be responsible for directing Nrap to the nucleus but a region accountable for nucleolar localisation was not identified. The data indicated that multiple domains working together are likely to direct Nrap to the nucleolus. Nrap was also observed to co-localise with nucleolar proteins B23 and p19ARF. Moreover, it was shown by reciprocal immunoprecipitation that these three nucleolar proteins existed in a complex in unsynchronised mouse fibroblast cells. Recent reports demonstrated a complex relationship between B23 and p19ARF although the functional significance remained unclear. Nrap's in vivo association with B23 and p19ARF indicated a specific functional role in the nucleolus. Nrap knockdown using siRNA significantly increased B23 protein levels in a dose-dependent manner and down-regulated p19ARF protein levels at higher siRNA concentration. Preliminary studies also implicated Nrap in cell proliferation through these novel interactions. Both endogenous and recombinant Nrap were found to be highly unstable suggesting that Nrap might regulate B23 and p19ARF through its own tightly regulated stability. Finally, the role of Nrap in rRNA processing was investigated by northern blot analysis. Nrap knockdown was found to affect the levels of 45S, 32S and 28S rRNAs. The changes found may be a consequence of the concurrent perturbation in the levels of B23 and p19ARF caused by Nrap knockdown. As the results were not consistent with previous reports, it was likely that changes to rRNA processing could be contributed to Nrap loss of function. This study demonstrated for the first time a functional role of Nrap in rRNA processing possibly through its association with B23 and p19ARF.
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Inder, Kerry. "The Functional Role of NRAP in the Nucleolus." Thesis, Griffith University, 2006. http://hdl.handle.net/10072/367738.

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The nucleolus is the site for rRNA synthesis, a process requiring the recruitment of many proteins involved in ribosomal biogenesis. Nrap is a novel nucleolar protein found to be present in all eukaryotes. Preliminary characterisation of Nrap suggested it was likely to participate in ribosome biogenesis but as with many other nucleolar proteins, the functional role of Nrap is largely unknown. In this study, the role of mammalian Nrap in the nucleolus and in ribosome biogenesis was explored. Initially, a number of tools were generated to investigate Nrap function. This involved raising and purifying a polyclonal antibody against the N-terminal region of Nrap. The anti-Nrap antibody was found to detect two Nrap bands in mouse fibroblast cells, possibly corresponding to the two mouse Nrap isoforms, and . In addition, mammalian expression vectors containing the full Nrap sequence as well as deletion constructs were created. The subcellular localisation of each construct was observed by fluorescent microscopy. It was revealed that recombinant Nrap did not localise to the nucleolus, possibly because it was exported to undergo degradation by the 26S proteasome. Two putative NLSs were found to be responsible for directing Nrap to the nucleus but a region accountable for nucleolar localisation was not identified. The data indicated that multiple domains working together are likely to direct Nrap to the nucleolus. Nrap was also observed to co-localise with nucleolar proteins B23 and p19ARF. Moreover, it was shown by reciprocal immunoprecipitation that these three nucleolar proteins existed in a complex in unsynchronised mouse fibroblast cells. Recent reports demonstrated a complex relationship between B23 and p19ARF although the functional significance remained unclear. Nrap's in vivo association with B23 and p19ARF indicated a specific functional role in the nucleolus. Nrap knockdown using siRNA significantly increased B23 protein levels in a dose-dependent manner and down-regulated p19ARF protein levels at higher siRNA concentration. Preliminary studies also implicated Nrap in cell proliferation through these novel interactions. Both endogenous and recombinant Nrap were found to be highly unstable suggesting that Nrap might regulate B23 and p19ARF through its own tightly regulated stability. Finally, the role of Nrap in rRNA processing was investigated by northern blot analysis. Nrap knockdown was found to affect the levels of 45S, 32S and 28S rRNAs. The changes found may be a consequence of the concurrent perturbation in the levels of B23 and p19ARF caused by Nrap knockdown. As the results were not consistent with previous reports, it was likely that changes to rRNA processing could be contributed to Nrap loss of function. This study demonstrated for the first time a functional role of Nrap in rRNA processing possibly through its association with B23 and p19ARF.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Biomedical Sciences
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Moore, Duncan Alan. "FUS, RNA and the nucleolus." Thesis, University of Sussex, 2016. http://sro.sussex.ac.uk/id/eprint/65760/.

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Fused-in-sarcoma (FUS) is an RNA binding protein, thought to be involved in a wide variety of cellular processes, and mutations in FUS are known to be causative for amyotrophic lateral sclerosis (ALS). The mechanism of pathogenesis for ALS has not been established but it has been proposed that dysfunction in cellular functions involving RNA could be responsible. Investigations into a FUS-ALS patient cell line showed sensitivity to the transcriptional inhibitor camptothecin (CPT) and demonstrated constitutively fragmented nucleoli, a phenotype that has been associated with rRNA dysfunction, as well as a possible defect in ribosomal RNA (rRNA) maturation. In addition a reversible relocalisation of FUS to the nucleolus in response to inhibition of RNA polymerase II was observed in all cell lines examined. This relocalisation appeared to be dependent on the activity of phosphodiesterase 8 (PDE8) and on the presence of rRNA, as pre-inhibition of RNAP I (which produces rRNA) prevented relocalisation of FUS. However treatment of both RNAP I and RNAP II at the same time resulted in FUS relocalisation and the protein remaining in the nucleolus for hours if inhibition was maintained - long after RNA would be depleted at the site were RNAP I inhibited in isolation. These findings suggest that FUS may have a role in protecting pre-rRNA transcripts from degradation during transcriptional stress.
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McKeown, Peter. "Chromatin components of the Arabidopsis nucleolus." Thesis, University of East Anglia, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.441526.

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Leung, Anthony Kar Lun. "Proteomics and dynamics of the human nucleolus." Thesis, University of Dundee, 2003. https://discovery.dundee.ac.uk/en/studentTheses/46f8836d-a114-4320-b1a8-70622068c68e.

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The nucleolus is the most prominent structure within the eukaryotic cell nucleus and it was established to be the site where the majority of ribosomal RNAs (5.8S, 18S and 28S) are transcribed, processed and assembled with ribosomal proteins to form ribosomal subunits. The sole role of ribosome biogenesis, however, cannot explain the specific nucleolar localisations of tumour suppressors, cell cycle-regulatory factors and viral proteins. Therefore, together with my colleagues in the laboratory of Prof. Angus Lamond, we carried out a proteomic approach with an aim to identify the core components of the human nucleolus isolated from HeLa cell nuclei. My role in this project includes verification of the newly identified components, database construction archiving the primary data and providing links to other related information in the public domain, and subsequent bioinformatics and microscopic analyses. So far, 400 proteins were identified in which -30% represents novel or uncharacterised proteins, partly reflecting the current poor status in the human genome annotation, but also reflecting the unknown complexity of the nucleolus. To facilitate the understanding of the functions of these novel proteins, I used deposited data of their gene activities and homologues across the species to identify in silico those novel proteins that are likely to be involved in ribosomal biogenesis. Like the nucleus, the nucleolus itself is subcompartmentalised into different domains, namely, the fibrillar centre, the dense fibrillar components and the granular components and these structures are disassembled and reassembled during mitosis in human cells. In order to understand the intricate mechanism behind these mitotic dynamics, I have generated a panel of 24 HeLa cell lines stably expressing one or more nucleolar marker to study the inter-relationships between these subnucleolar domains as well as their relationships with the chromosomes. The results suggest that (1) a core subunit of the RNA polymerase I dissociates from the chromosomes between prophase and metaphase and (2) the breakdown and reassembly are dependent on the dissociation and the recruitment of RNA polymerase I to the chromosomes respectively.As part of the follow-up to the nucleolar proteome identified, the study of one uncharacterised factor NHPX led to the discovery of a novel nucleolar targeting pathway that is observed in both primary and transformed cell lines. Although NHPX co-localises with the dense fibrillar component marker fibrillarin, NHPX transiently transits through the splicing speckles prior to the nucleolar accumulation whilst fibrillarin accumulates within the nucleolus immediately after the nuclear entry. The NHPX progression is dependent on pre-mRNA transcription and may link multiple RNA metabolic pathways that occur in distinct subnuclear domains.
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Peruquetti, Rita Luiza [UNESP]. "Caracterização do ciclo nucleolar e da formação do corpo cromatóide na espermatogênese de alguns vertebrados." Universidade Estadual Paulista (UNESP), 2009. http://hdl.handle.net/11449/102725.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
O corpo cromatóide (CB) é uma organela citoplasmática que, aparentemente, possui um papel no estoque de RNA e proteínas para a diferenciação final dos espermatozóides. Existem algumas teorias que tentam explicar a origem do material que compõe essa organela. Uma dessas teorias, proposta por alguns autores, sugere que o CB se origine a partir de material nucleolar, que se fragmenta nas etapas iniciais da espermatogênese e, em seguida, migra para o citoplasma. O objetivo do presente estudo foi acompanhar o ciclo nucleolar por meio de análises citoquímicas – hematoxilina-eosina (HE); azul de toluidina (AT); variante da concentração crítica de eletrólitos (CEC); reação de Feulgen; impregnação por íons prata (AgNOR); citogenéticas – impregnação por íons prata (AgNOR), e análises ultra-estruturais – microscopia eletrônica de transmissão (MET), para verificar a relação da fragmentação do material nucleolar com a formação do corpo cromatóide (CB), em algumas espécies de vertebrados: Tilapia rendalli (Teleostei, Cichlidae); Dendropsophus minutus (Amphibia, Anura); Phrynops geoffroanus (Reptilia, Testudines) e coelho albino da raça Nova Zelândia – Oryctolagus cuniculus (Mammalia, Lagomorpha). Por meio das análises citoquímicas foi possível observar que ocorre uma fragmentação do material nucleolar no início da prófase I, em todas as espécies analisadas, e uma posterior reorganização do nucléolo no núcleo de espermátides iniciais, com uma área significantemente menor do que a área do nucléolo das espermatogônias. Três fenômenos podem contribuir para essa diferença significante entre as áreas nucleolar de espermatogônias e espermátides: a) Modificação no estado funcional da célula; b) Diminuição no número de RONs nas espermátides; c) Migração de material nucleolar fragmentado...
The chromatoid body (CB) is a cytoplasmic organelle that has a function related to RNA and protein accumulation and ⁄ or storage for later germ-cell differentiation. Many theories have been postulated in order to explain the origins of the CB material. One of the most accepted theory describes that it originates from a nucleolar material, where it was fragmented in the early spermatogenesis, and finally, this fragmented nucleolar material migrates to cytoplasm. The aims of the present study were: 1) monitoring the nucleolar material distribution by means of cytochemical techniques (hematoxylin–eosin (HE), toluidine blue (TB), modified Critical Electrolyte Concentration for detecting RNA (CEC), silver-ion impregnation (AgNOR) and Feulgen reaction), and by ultrastructural analysis (Transmission Electron Microscopy – TEM); and 2) comparing the nucleolar material distribution with the formation of CB in some vertebrate species: Tilapia rendalli (Teleostei, Cichlidae); Dendropsophus minutus (Amphibia, Anura); Phrynops geoffroanus (Reptilia, Testudines); and Oryctolagus cuniculus (Mammalia, Lagomorpha). For all analyzed species, the cytochemical techniques showed that the nucleolar fragmentation occurred during the beginning of prophase I, and the nucleolus reorganization occurred in the early spermatids nucleus. Statistical tests evidenced that area of the early spermatids nucleolus were smaller than the spermatogonia nucleolus area. Three phenomena can contribute for the statistical difference between the spermatogonia nucleolar area and the early spermatids nucleolar area: a) Modification of cell activity; b) Decrease of the number of NORs in the spermatids; c) Migration of the fragmented nucleolar material from the nucleus to the cytoplasm. This nucleolar material will participate in the CB formation process. The ultrastructural analysis showed an ...(Complete abstract click electronic access below)
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Jacob, Mathieu. "Functional Remodelling of the Nucleolus by Long Noncoding RNA." Thesis, Université d'Ottawa / University of Ottawa, 2013. http://hdl.handle.net/10393/30288.

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The nucleolus is a plurifunctional organelle in which structure and function are intimately linked. Though it is primarily known as the site of ribosomal biogenesis, the nucleolus is also capable of orchestrating the immobilization of a broad range of proteins under specific environmental conditions. This process, known as nucleolar sequestration, contributes to cell viability under stress. Despite the importance of this post-translational regulatory pathway, very little is known about the mechanisms that govern it. Here, we show that heat shock and acidosis, two physiological stimuli associated with nucleolar sequestration, induce the expression of long noncoding RNA (lncRNA) from stimulus-specific loci of the ribosomal intergenic spacer (IGS). These lncRNAs, in turn, immobilize proteins encoding a nucleolar detention sequence (NoDS) within a compartment of the nucleolus termed the detention centre (DC). The DC is a spatially and dynamically distinct region, characterized by an 8-anilino-1-naphthalenesulfonate (ANS)-positive hydrophobic signature. Its formation is accompanied by a redistribution of nucleolar factors and an arrest in ribosomal biogenesis. Silencing of regulatory IGS lncRNA prevents the creation of this structure and allows the nucleolus to retain its tripartite organization and transcriptional activity. Signal termination causes a decrease in IGS transcript levels and a return to the active nucleolar conformation. We propose that the induction of IGS lncRNA, by environmental signals, operates as a molecular switch that regulates the structure and function of the nucleolus.
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Morral, Martínez Clara 1989. "The Nucleolus : a connection between cell fate and tumorigenesis in colorectal cancer." Doctoral thesis, Universitat Pompeu Fabra, 2017. http://hdl.handle.net/10803/663807.

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El càncer de colon es caracteritza per presentar una composició cel·lular heterogènia en la qual només un subgrup de cèl·lules retenen la capacitat de contribuir en el manteniment i creixement del tumor. L‘investigació duta a terme en aquesta tesis es focalitza en estudiar aquelles funcions biològiques que estan específicament enriquides en aquesta subpoblació tumoral comparat amb altres cèl·lules cancerígenes que no tenen potencial tumoral. A partir de dades obtingudes en analitzar l’expressió genètica de cèl·lules mare normals i tumorals, hem descobert que l’activitat nucleolar està específicament sobre-activada en aquestes dues poblacions. Hem validat aquestes dades utilitzant diferents models in vivo i in vitro que ens permeten reproduir la biologia intestinal. Hem descobert que l’activitat nucleolar està regulada de forma heterogènia en els tumors de colon. Concretament, són les cèl·lules mare del tumor que presenten una major activació d’aquesta funció biològica. Utilitzant tècniques d’edició del genoma (CRISPR-Cas9) hem pogut generar cèl·lules tumorals de colon que expressen la proteïna RNA Polymerasa I fusionada a una molècula fluorescent (EGFP). D’aquesta manera hem pogut aïllar dels tumors de colon cèl·lules tumorals que presenten una elevada activitat nucleolar. Hem descobert que aquestes cèl·lules tenen una elevada capacitat tumoral, mentre que altres cèl·lules tumorals amb baixa activitat nucleolar no són capaces de retenir aquest potencial cancerigen. Finalment també hem obtingut evidències de que aquesta activitat nucleolar podria estar regulada per la via de senyalització de WNT i que el oncogen MYC podria jugar un paper molt important en aquest escenari. Els resultats obtinguts durant aquesta tesis proveeixen nova informació per al que fa a les funcions biològiques que regulen el potencial tumoral de les cèl·lules de càncer de colon. Això en permetrà entendre millor la malaltia i poder desenvolupar noves teràpies més efectives.
Colorectal cancers (CRCs) are amalgams of phenotypically distinct tumor cell populations in which only a subset of cells retain the capacity to sustain tumor growth and propagate the disease. The research in this thesis has focus on the biological functions specifically enriched in this population compared with their differentiated and non-tumorigenic counterparts. Data mining of the expression profiles of normal and cancer stem cells suggested that nucleolar function was enhanced in both types of stem cells. We have validated these in silico observations using different in vitro and in vivo models that allow us to reproduce the intestinal biology and disease. We have discovered that nucleolar activity is heterogeneously regulated in colorectal cancer (CRC) and that high levels of this activity correlate with the undifferentiated state of tumor cells. By means of CRISPR-Cas9 technology we have generated colorectal cancer organoids expressing endogenous RNA Polymerase I (RNA POL I) fused to a EGFP reporter protein. Analysis of tumor cells purified from patient derived xenografts (PDX) expressing high levels of RNA Pol I demonstrated that these cells display elevated rDNA transcriptional activity as well as tumorigenic potential. On the contrary, tumor cells with low levels of RNA Pol I represent a differentiated population with dismal tumor capacity. Furthermore, we also put forward evidence that nucleolar activity is WNT regulated and that the WNT target MYC may be essential in this scenario. Taken together, our data provides new insights on the biology behind the differential tumorigenic behavior and fate of tumor cells in CRCs. Importantly, it also contributes to better understanding cell heterogeneity and may provide the basis for the development of new therapeutic strategies to tackle this disease.
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Galliot, Sonia. "A la recherche de nouvelles AgNORs: une famille de protéines nucléolaires conservées et marqueurs potentiels du cancers." Doctoral thesis, Universite Libre de Bruxelles, 2010. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/210190.

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Comme le nucléole joue un rôle fondamental dans l’expression des protéines, via la synthèse des ARN ribosomiques, il n’est donc pas surprenant que des études aient révélé un lien étroit, entre des dysfonctionnements nucléolaires et l’origine de certaines maladies humaines. La découverte, il y a plusieurs années, d’un taux anormalement élevé de protéines nucléolaires dites argyrophiles ou AgNORs, dans les cellules tumorales, a permis d’envisager leur utilisation comme outil diagnostique ou pronostique du cancer. Détectées, de manière in vitro grâce à leur affinité pour l’argent, l’identification de quelques protéines AgNORs n’a pourtant pas permis d’établir une caractéristique commune à toutes les protéines argyrophiles détectées dans les extraits nucléolaires. Ainsi, bien que le test colorimétrique AgNOR soit utilisé dans de nombreux laboratoires académiques, l’absence d’identification de protéines AgNORs spécifiques du processus de cancérisation, a limité son utilisation en laboratoire clinique. Comme certaines limites technologiques et expérimentales ont limité leur caractérisation chez l’humain, nous avons donc décidé de reprendre les recherches sur ce sujet et de le réactualiser grâce aux avancées technologiques et scientifiques. Les protéines AgNORs étant étroitement liées à la biogenèse des ribosomes, nous avons donc décidé d’amorcer nos recherches chez la levure Saccharomyces cerevisiae, dans laquelle, la voie de biosynthèse des ribosomes a été particulièrement bien décrite. Devant l’intérêt biologique et médical de ces protéines, l’objectif de ce projet a donc été triple :

1-identifier des protéines AgNORs chez la levure

2-caractériser les propriétés physico-fonctionnelles et physico-chimiques de ces protéines AgNORs.

3-utiliser ces caractéristiques physico-chimiques pour rechercher de nouvelles AgNORs humaines, spécifiques de processus de cancérisation et potentiellement utilisables comme marqueurs tumoraux./The nucleolus is a subnuclear compartment that organized around ribosomal gene (rDNA) repeats NORs, which encode for ribosomal RNA. A peculiar group of acidic proteins which are highly argyrophilic are also localized at the same sites as NORs, thus allowing NORs to be very clearly and rapidly visualized by silver nitrate staining procedures. However, if three human argyrophilic proteins, UBF, C23 (nucleolin) and B23 (nucleophosmin), have been associated for staining of NOR, the exact number of AgNOR proteins and their intrinsic biochemical feature are unclear. Here, we have performed an heterologous screen in a genetically tractable eukaryotic organism (budding yeast) for the identification of novel AgNOR proteins and in vitro characterized an intrinsic feature that underlies silver binding and offers a strong predictive value for the identification of novel human AgNOR proteins.
Doctorat en Sciences
info:eu-repo/semantics/nonPublished

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Books on the topic "Nucleolus"

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Németh, Attila, ed. The Nucleolus. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3792-9.

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Olson, Mark O. J., ed. The Nucleolus. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4614-0514-6.

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service), SpringerLink (Online, ed. The Nucleolus. New York, NY: Springer Science+Business Media, LLC, 2011.

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O'Day, Danton H., and Andrew Catalano, eds. Proteins of the Nucleolus. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5818-6.

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Chelidze, P. V. Ulʹtrastruktura i funkt͡s︡ii i͡a︡dryshka interfaznoĭ kletki. Tbilisi: "Met͡s︡niereba", 1985.

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The nucleolus and ribosome biogenesis. Wien: Springer-Verlag, 1985.

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Hadjiolov, Asen A. The Nucleolus and Ribosome Biogenesis. Vienna: Springer Vienna, 1985. http://dx.doi.org/10.1007/978-3-7091-8742-5.

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Thiry, Marc. The nucleolus during the cell cycle. New York: Springer, 1996.

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Thiry, Marc. The nucleolus during the cell cycle. New York: Springer, 1996.

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Suhonen, Jouni. From Nucleons to Nucleus. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-48861-3.

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Book chapters on the topic "Nucleolus"

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Capinera, John L., Marjorie A. Hoy, Paul W. Paré, Mohamed A. Farag, John T. Trumble, Murray B. Isman, Byron J. Adams, et al. "Nucleolus." In Encyclopedia of Entomology, 2622. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6359-6_2264.

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Fang, Qizhi. "Nucleolus." In Encyclopedia of Algorithms, 1419–22. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-2864-4_260.

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Pavelka, Margit, and Jürgen Roth. "Nucleolus." In Functional Ultrastructure, 10–11. Vienna: Springer Vienna, 2010. http://dx.doi.org/10.1007/978-3-211-99390-3_6.

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Fang, Qizhi. "Nucleolus." In Encyclopedia of Algorithms, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27848-8_260-2.

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Fang, Qizhi. "Nucleolus." In Encyclopedia of Algorithms, 581–84. Boston, MA: Springer US, 2008. http://dx.doi.org/10.1007/978-0-387-30162-4_260.

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Gooch, Jan W. "Nucleolus." In Encyclopedic Dictionary of Polymers, 911. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_14357.

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Hutten, Saskia, Belinda J. Westman, François-Michel Boisvert, Silvana van Koningsbruggen, and Angus I. Lamond. "The Nucleolus." In Genome Organization and Function in the Cell Nucleus, 279–307. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527639991.ch12.

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Tijs, Stef. "The nucleolus." In Introduction to Game Theory, 102–5. Gurgaon: Hindustan Book Agency, 2003. http://dx.doi.org/10.1007/978-93-86279-17-0_16.

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Peters, Hans. "The Nucleolus." In Springer Texts in Business and Economics, 343–59. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46950-7_19.

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van Sluis, Marjolein, Chelly van Vuuren, and Brian McStay. "The Relationship Between Human Nucleolar Organizer Regions and Nucleoli, Probed by 3D-ImmunoFISH." In The Nucleolus, 3–14. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3792-9_1.

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Conference papers on the topic "Nucleolus"

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Deng, Xiaotie, Qizhi Fang, and Xiaoxun Sun. "Finding nucleolus of flow game." In the seventeenth annual ACM-SIAM symposium. New York, New York, USA: ACM Press, 2006. http://dx.doi.org/10.1145/1109557.1109572.

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Elkind, Edith, and Dmitrii Pasechnik. "Computing the nucleolus of weighted voting games." In Proceedings of the Twentieth Annual ACM-SIAM Symposium on Discrete Algorithms. Philadelphia, PA: Society for Industrial and Applied Mathematics, 2009. http://dx.doi.org/10.1137/1.9781611973068.37.

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Goradia, Hrishikesh J., and Jose M. Vidal. "A Distributed Algorithm for Finding Nucleolus-Stable Payoff Divisions." In 2007 IEEE/WIC/ACM International Conference on Intelligent Agent Technology (IAT'07). IEEE, 2007. http://dx.doi.org/10.1109/iat.2007.99.

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Samia, Dardouri, Bouallegue Ridha, and Anne Wei. "Resource allocation using Nucleolus Value in downlink LTE networks." In 2016 IEEE Symposium on Computers and Communication (ISCC). IEEE, 2016. http://dx.doi.org/10.1109/iscc.2016.7543748.

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Kobayashi, Noriaki, Yuji Iwahori, Takashi Iwamoto, Jun Ueda, Boonserm Kijsirikul, and Aili Wang. "Classification of Benign or Malignant Cell Nuclei using Nucleolus." In 2019 8th International Congress on Advanced Applied Informatics (IIAI-AAI). IEEE, 2019. http://dx.doi.org/10.1109/iiai-aai.2019.00123.

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Chen, Min, Shengyong Chen, and Qiu Guan. "Hybrid Contour Model for Segmentation of Cell Nucleolus and Membranes." In 2009 2nd International Conference on Biomedical Engineering and Informatics. IEEE, 2009. http://dx.doi.org/10.1109/bmei.2009.5305309.

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Du, Fengqing, Aiqiang Pan, Hongbo Ren, and Qiong Wu. "Estimating Nucleolus for Fair Profit Allocation in Distributed Energy Network." In 2021 4th International Conference on Energy, Electrical and Power Engineering (CEEPE). IEEE, 2021. http://dx.doi.org/10.1109/ceepe51765.2021.9475773.

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Gustavo Atkinson Amorim, João, Vinícius Moreno Sanches, Tainee Bottamedi, André Victória Matias, Marco Antônio Martins Cavaco, Alexandre Sherlley Onofre, Fabiana B. Botelho Onofre, and Aldo Von Wangenheim. "Nucleus Detection in Cervical Samples Stained With AgNOR." In Computer on the Beach. Itajaí: Universidade do Vale do Itajaí, 2022. http://dx.doi.org/10.14210/cotb.v13.p045-050.

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ABSTRACTCervical cancer is a public health problem, where the treatment hasa better chance of success if detected early. This paper explores oneway of to analyze argyrophilic nucleolus organizer regions (AgNOR)stained slide using deep learning approaches of object detection fordetecting the different categories of nucleus. Our results show thata balanced dataset between the explored categories was essential,also that a ResNet-50 as backbone of Fast RCNN shows an AP of61.8% and 42.5% to detect nucleus and out of focus nucleus.
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Li, Tianwen, Feng Ma, and Weiyi Liu. "Bargaining set, kernel and nucleolus for multi-choice games with coalition structure." In 2013 25th Chinese Control and Decision Conference (CCDC). IEEE, 2013. http://dx.doi.org/10.1109/ccdc.2013.6561113.

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Murali, M., P. S. Divya, M. S. Kumari, and M. Sydulu. "Distribution of loss cost using proportional nucleolus method in competitive power markets." In 2013 International Conference on Energy Efficient Technologies for Sustainability (ICEETS). IEEE, 2013. http://dx.doi.org/10.1109/iceets.2013.6533531.

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Reports on the topic "Nucleolus"

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Peng, Jamy C. Local chromatin structure of heterochromatin regulates repeated DNA stability, nucleolus structure, and genome integrity. Office of Scientific and Technical Information (OSTI), January 2007. http://dx.doi.org/10.2172/913167.

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Meissner, U. G. Chiral perturbation theory with nucleons. Office of Scientific and Technical Information (OSTI), September 1991. http://dx.doi.org/10.2172/10107296.

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Meissner, U. G. Chiral perturbation theory with nucleons. Office of Scientific and Technical Information (OSTI), September 1991. http://dx.doi.org/10.2172/6095581.

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Borowiec, James A. Regulation of MDM2 Activity by Nucleolin. Fort Belvoir, VA: Defense Technical Information Center, June 2005. http://dx.doi.org/10.21236/ada439277.

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Borowiec, James A. Regulation of MDM2 Activity by Nucleolin. Fort Belvoir, VA: Defense Technical Information Center, June 2007. http://dx.doi.org/10.21236/ada472086.

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Thornton, S. T., and R. M. Sealock. Electromagnetic interactions with nuclei and nucleons. Office of Scientific and Technical Information (OSTI), November 1990. http://dx.doi.org/10.2172/6311946.

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Thornton, S. T., and R. M. Sealock. Electromagnetic interactions with nucleons and nuclei. Office of Scientific and Technical Information (OSTI), October 1991. http://dx.doi.org/10.2172/5748013.

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Baker, Oliver K. Electromagnetic Studies of Mesons, Nucleons, and Nuclei. Office of Scientific and Technical Information (OSTI), August 2013. http://dx.doi.org/10.2172/1091181.

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Kyle, Gary. Experimental Studies of Quark-Gluon Structure of Nucleons and Nuclei. Office of Scientific and Technical Information (OSTI), December 2004. http://dx.doi.org/10.2172/835226.

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Liu, Hongxiang. Mechanism of Splicing of Unusual Intron in Human Proliferating Cell Nucleolor Pl2O. Fort Belvoir, VA: Defense Technical Information Center, December 1997. http://dx.doi.org/10.21236/ada340957.

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