In vivo interaction of nucleophosmin/B23 and protein C23 during cell cycle progression in HeLa cells.
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Summary
The findings suggest some possibilities for further elucidation of the actions of nucleophosmin/B23 and protein C23 in cell cycle progression and cell growth.
- Type
- article
- Published
- 1999-09-20
- Cited by
- 53
- References
- 39
- OpenAlex
- https://openalex.org/W2117488991
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:9527268
Keywords
Nucleophosmin, Prometaphase, Mitosis, Cell biology, Cytokinesis
References
- Translocation of nucleolar phosphoprotein B23 (37 kDa/pI 5.1) induced by selective inhibitors of ribosome synthesis.
- The Nucleolus and Ribosome Biogenesis
- Nuclear localization of the ubiquitin-activating enzyme, E1, is cell-cycle-dependent.
- The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion.
- The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid leukemia produces a novel fusion gene, NPM-MLF1.
- The nucleolar structure.
- Amino acid sequence of protein B23 phosphorylation site.
- Nucleolar targeting signal of Rex protein of human T-cell leukemia virus type I specifically binds to nucleolar shuttle protein B-23.
- Relief of YY1-induced transcriptional repression by protein-protein interaction with the nucleolar phosphoprotein B23.
- Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells.
- Identification of the nuclear and nucleolar localization signals of the protein p120. Interaction with translocation protein B23.
- The major phosphorylation site of nucleophosmin (B23) is phosphorylated by a nuclear kinase II.
- Identification of a prominent nuclear protein associated with proliferation of normal and malignant B cells.
- Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element
- Comparison of proteins of ribosomal subunits and nucleolar preribosomal particles from Novikoff hepatoma ascites cells by two-dimensional polyacrylamide gel electrophoresis.
- Immunolocalization of phosphoprotein B23 in proliferating and non‐proliferating hela cells
- Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth.
- A new class of reversible cell cycle inhibitors.
- Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase.
- Casein kinase II accumulation in the nucleolus and its role in nucleolar phosphorylation.
Cited by
- Proteomic Analyses of HIV-1 Infected T-cells and the Functional Characterization of Cyclophilin B During HIV-1 Infection
- Characterization of Nucleophosmin (B23) as a Myc Target by Scanning Chromatin Immunoprecipitation*
- Utility of peptide-protein affinity complexes in proteomics: identification of interaction partners of a tumor suppressor peptide.
- The Nucleolus Takes Control of Protein Trafficking Under Cellular Stress
- Comprehensive Proteomic Analysis of Interphase and Mitotic 14-3-3-binding Proteins*
- Type 1 Protein Phosphatase Controls Biological Processes in Cultured Human Osteoblastic Cells
- Nucleolin provides a link between RNA polymerase I transcription and pre-ribosome assembly
- Involvement of nPKC-MAPK pathway in the decrease of nucleophosmin/B23 during megakaryocytic differentiation of human myelogenous leukemia K562 cells.
- Nucleophosmin/B23, a multifunctional protein that can regulate apoptosis
- Nucleolin
- Proteomic, cellular, and network analyses reveal new DUSP3 interactions with nucleolar proteins in HeLa cells.
- Nucleolin modulates the subcellular localization of GDNF-inducible zinc finger protein 1 and its roles in transcription and cell proliferation.
- VHR/DUSP3 phosphatase: structure, function and regulation
- The nucleoplasmin homolog NLP mediates centromere clustering and anchoring to the nucleolus.
- The nucleolus: an emerging target for cancer therapy.
- Nucleophosmin Serves as a Rate-Limiting Nuclear Export Chaperone for the Mammalian Ribosome
- Nucleophosmin and Nucleolin Regulate K-Ras Plasma Membrane Interactions and MAPK Signal Transduction*
- Phosphorylated Nucleolin Interacts with Translationally Controlled Tumor Protein during Mitosis and with Oct4 during Interphase in ES Cells
- Enhancement of Adeno-Associated Virus Infection by Mobilizing Capsids into and Out of the Nucleolus
- Depletion of nucleophosmin leads to distortion of nucleolar and nuclear structures in HeLa cells
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