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Nucleolus

About: Nucleolus is a research topic. Over the lifetime, 5873 publications have been published within this topic receiving 232435 citations. The topic is also known as: GO:0005730 & cell nucleolus.


Papers
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Journal ArticleDOI
TL;DR: The increased ribonuclease activity produced by sonic oscillation, Triton X-100, and p-chloromercuribenzoate, as well as the different response to these agents of nuclear fractions from normal rats and from rats treated with thioacetamide or actinomycin D, shows that there may be more than one mechanism of latency of nuclear and nucleolar ribonucleases.

74 citations

Journal ArticleDOI
TL;DR: Changes in the intracellular localization of RECQL4 in response to oxidative stress are demonstrated and an interaction betweenRECQL4 and PARP-1 is identified, a nuclear enzyme that promotes genomic integrity through its involvement in DNA repair and signaling pathways.

74 citations

Journal ArticleDOI
TL;DR: The hypothesis that DRB inhibits the synthesis of mRNA is proposed; as a consequence, some of the preribosomal proteins that normally coat the 32S rRNA portion of the 45S precursor RNA become limiting, and this defective portion is then subject to degradation by nucleases.
Abstract: A number of chemicals, mostly adenosine analogues, cause the nucleolus of the chick embryo fibroblast to lose material and unravel over a period of several hours into beaded strands termed nucleolar necklaces (NN). The results of analyses of the fibroblasts, treated with the NN-forming chemical dichlororibobenzimidazole (DRB), suggests that the following biochemical alterations occur: DRB almost completely prevents the increase in both messenger RNA (mRNA) and heterogeneous nuclear RNA. It interferes with ribosome synthesis by decreasing the rate of 45S ribosomal RNA (rRNA) accumulation by 50%, slowing the rate of 18S rRNA appearance by 50%, and causing an extensive degradation (80%) of the 32S and 28S rRNA-containing preribisomes. Most of this preribosome degration probably occurs at or before the 32S rRNA preribosome stage. The degradation of these preribosomes appears to be due to the formation of defective 45S rRNA preribosomes rather than to a direct DRB interference with preribosome processing enzyme action. DRB inhibits total cellular RNA synthesis in less than 15 min, suggesting a direct interference with RNA synthesis. DRB also inhibits the uptake of nucleosides into the cell. DRB in the concentrations used does not appear to directly interfere with the translation of mRNA (i.e., protein synthesis). Other NN-forming adenoside analogues and high concentrations of adenosine (2 mM) cause biochemical alterations similar to those produced by DRB. To explain the preribosome degradation, we propose the hypothesis that DRB inhibits the synthesis of mRNA; as a consequence, some of the preribosomal proteins that normally coat the 32S rRNA portion of the 45S precursor RNA become limiting, and this defective portion is then subject to degradation by nucleases.

74 citations

Journal ArticleDOI
TL;DR: Radioimmunoprecipitation analysis of [35S]methionine-labelled purified virions and Western blot analysis of the antigens prepared from the infected mammalian and mosquito cells showed that the MAb was directed against the DEN-4 virus core protein.
Abstract: A mouse monoclonal antibody (MAb) to dengue 4 (DEN-4) virus reacted with the antigen in the nucleus as well as in the cytoplasm of DEN-4-infected mammalian and mosquito cells, as demonstrated by the peroxidase-antiperoxidase staining method. The intranuclear antigen appeared to accumulate at the nucleoli, forming spots, whereas the cytoplasmic antigen appeared to be localized mainly in large perinuclear foci in the infected cells. The MAb-reactive antigen was produced in the presence of actinomycin D, which caused the accumulation in the nucleus to be altered to a dispersed pattern. Radioimmunoprecipitation analysis of [35S]methionine-labelled purified virions and Western blot analysis of the antigens prepared from the infected mammalian and mosquito cells showed that the MAb was directed against the DEN-4 virus core protein (Mr 15.5K). These results indicated that the DEN-4 virus core protein was partially transported, soon after its synthesis in the cytoplasm, into the nucleus and accumulated at the nucleoli.

74 citations

Book
01 Jul 1996
TL;DR: This review presents and discusses recent progress in the understanding of nucleolar architecture and its relationship to nucleolar functions, and critically evaluates the data and proposes a new model of structure-function relationships within the Nucleolus.
Abstract: There is growing evidence that the cell nucleus like the cytoplasm is organized into different functional domains. The best-characterized intranuclear domain is the Nucleolus. This review presents and discusses recent progress in the understanding of nucleolar architecture and its relationship to nucleolar functions. Both the morphology and the composition of the various nucleolar components are analysed during the cell cycle in different eucaryotic organisms. Since controversy is still present in this field, the authors critically evaluate the data and propose a new model of structure-function relationships within the Nucleolus. This review is designed for researchers who need general information on the morphology and functions of the Nucleolus.

74 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023145
2022209
2021143
2020125
2019139
2018121