Literatura académica sobre el tema "Novel nucleolar protein"
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Artículos de revistas sobre el tema "Novel nucleolar protein"
Savino, T. M., R. Bastos, E. Jansen y D. Hernandez-Verdun. "The nucleolar antigen Nop52, the human homologue of the yeast ribosomal RNA processing RRP1, is recruited at late stages of nucleologenesis". Journal of Cell Science 112, n.º 12 (15 de junio de 1999): 1889–900. http://dx.doi.org/10.1242/jcs.112.12.1889.
Texto completoPendle, Alison F., Gillian P. Clark, Reinier Boon, Dominika Lewandowska, Yun Wah Lam, Jens Andersen, Matthias Mann, Angus I. Lamond, John W. S. Brown y Peter J. Shaw. "Proteomic Analysis of the Arabidopsis Nucleolus Suggests Novel Nucleolar Functions". Molecular Biology of the Cell 16, n.º 1 (enero de 2005): 260–69. http://dx.doi.org/10.1091/mbc.e04-09-0791.
Texto completoFujimura, Akiko, Yuki Hayashi, Kazashi Kato, Yuichiro Kogure, Mutsuro Kameyama, Haruka Shimamoto, Hiroaki Daitoku, Akiyoshi Fukamizu, Toru Hirota y Keiji Kimura. "Identification of a novel nucleolar protein complex required for mitotic chromosome segregation through centromeric accumulation of Aurora B". Nucleic Acids Research 48, n.º 12 (1 de junio de 2020): 6583–96. http://dx.doi.org/10.1093/nar/gkaa449.
Texto completoSmith, Corey L., Timothy D. Matheson, Daniel J. Trombly, Xiaoming Sun, Eric Campeau, Xuemei Han, John R. Yates y Paul D. Kaufman. "A separable domain of the p150 subunit of human chromatin assembly factor-1 promotes protein and chromosome associations with nucleoli". Molecular Biology of the Cell 25, n.º 18 (15 de septiembre de 2014): 2866–81. http://dx.doi.org/10.1091/mbc.e14-05-1029.
Texto completoWestendorf, Joanne M., Konstantin N. Konstantinov, Steven Wormsley, Mei-Di Shu, Naoko Matsumoto-Taniura, Fabienne Pirollet, F. George Klier, Larry Gerace y Susan J. Baserga. "M Phase Phosphoprotein 10 Is a Human U3 Small Nucleolar Ribonucleoprotein Component". Molecular Biology of the Cell 9, n.º 2 (febrero de 1998): 437–49. http://dx.doi.org/10.1091/mbc.9.2.437.
Texto completoEilbracht, Jens, Michaela Reichenzeller, Michaela Hergt, Martina Schnölzer, Hans Heid, Michael Stöhr, Werner W. Franke y Marion S. Schmidt-Zachmann. "NO66, a Highly Conserved Dual Location Protein in the Nucleolus and in a Special Type of Synchronously Replicating Chromatin". Molecular Biology of the Cell 15, n.º 4 (abril de 2004): 1816–32. http://dx.doi.org/10.1091/mbc.e03-08-0623.
Texto completoPark, J. H., B. C. Jensen, C. T. Kifer y M. Parsons. "A novel nucleolar G-protein conserved in eukaryotes". Journal of Cell Science 114, n.º 1 (1 de enero de 2001): 173–85. http://dx.doi.org/10.1242/jcs.114.1.173.
Texto completoKadowaki, T., R. Schneiter, M. Hitomi y A. M. Tartakoff. "Mutations in nucleolar proteins lead to nucleolar accumulation of polyA+ RNA in Saccharomyces cerevisiae." Molecular Biology of the Cell 6, n.º 9 (septiembre de 1995): 1103–10. http://dx.doi.org/10.1091/mbc.6.9.1103.
Texto completoDamianov, Andrey, Michael Kann, William S. Lane y Albrecht Bindereif. "Human RBM28 protein is a specific nucleolar component of the spliceosomal snRNPs". Biological Chemistry 387, n.º 10/11 (1 de octubre de 2006): 1455–60. http://dx.doi.org/10.1515/bc.2006.182.
Texto completoBrown, Isabella N., M. Carmen Lafita-Navarro y Maralice Conacci-Sorrell. "Regulation of Nucleolar Activity by MYC". Cells 11, n.º 3 (7 de febrero de 2022): 574. http://dx.doi.org/10.3390/cells11030574.
Texto completoTesis sobre el tema "Novel nucleolar protein"
Utama, B. "Isolation and characterization of Nrap, a novel nucleolar protein /". [St. Lucia, Qld.], 2001. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe16281.pdf.
Texto completoInder, Kerry y 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.
Texto completoInder, Kerry. "The Functional Role of NRAP in the Nucleolus". Thesis, Griffith University, 2006. http://hdl.handle.net/10072/367738.
Texto completoThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Biomedical Sciences
Full Text
Ho, Joseph Tsung-yo. "Bridging cell growth and proliferation : identification and characterization of binding partners for pescadillo, a novel nucleolar protein involved in tumorigenesis and DNA damage /". Thesis, Connect to this title online; UW restricted, 2004. http://hdl.handle.net/1773/10659.
Texto completoBai, Qi Yun y 白其昀. "Expression of a novel highly phosphorylated human nucleolar protein pl30 is proliferation-associated: identification of the cDNAS, Alterations during cell-cycle and correlation to the nucleologenesis". Thesis, 1995. http://ndltd.ncl.edu.tw/handle/24607301009942442654.
Texto completoTsai, Wen-Hai y 蔡文海. "Biochemical and Molecular Biological Characterizations of Nucleolin and a Novel PHD-finger Protein". Thesis, 1999. http://ndltd.ncl.edu.tw/handle/93349080846838181301.
Texto completo國立臺灣大學
分子醫學研究所
87
Maintenance of chromosome integrity is a fundamental requirement in all-living organisms. Genes are expressed in a temporal or tissue-specific manner or activated in response to extracellular stimuli. Gene expression can be tightly controlled at several levels, including transcriptional, post-transcriptional (mRNA processing and transport), translational (protein synthesis) and post-translational levels (glycosylation or phosphorylation etc.). For most genes transcriptional controls are paramount. The initiation of transcription in eukaryotes is a highly and tightly controlled process. Genes exist at some time in an inert state that was tightly packaged with histones in to chromatin. Before transcription can occur, this inert structure must be decondensed so that transcriptional control sequences are made available to regulatory proteins. Once decondensation of chromatin has occurred, the scene is set for the second activation steps: the interaction of regulatory proteins, commonly referred to as transcription factors or trans-acting factors, with specific DNA sequences. Such interactions of these bound factors with general transcription factors mediate gene transcription. Protein-protein interaction and posttranslational modifications are important for regulating activities of these trans-acting factors. There are two models for the initiation of transcription by RNA pol II : the stepwise assembly model and the holoenzyme model. The conventional model (stepwise assembly model) for ordered transcriptional initiation by RNA pol II is characterized by a distinct series of events : (1) recognition of core promoter elements by TFIID, (2) recognition of the TFIID-promoter complex by TFIIB and TFIIA, (3) recruitment of the TFIIF/pol II complex, (4) binding of TFIIE and TFIIH to complete the preinitiation complex, (5) promoter melting and formation of an "open" initiation complex, (6) synthesis of the nascent mRNA transcript, (7) release of pol II contact with the promoter ("promoter clearance"), and (8) elongation of the RNA transcript. Recently, the discovery that a subset of the GTFs (General Transcription Factor) exists in a preassembled form in an RNA pol II holoenzyme, suggests that the majority of the initiation machinery can bind to a promoter in a single step (RNA pol II holoenzyme model). The assembly of the GTFs is subject to regulation by activator and repressor proteins. Activators can recruit GTFs to a promoter, thereby accelerating the assembly process, whereas repressor proteins can inhibit transcription by blocking the assembly of GTFs. The mechanism of activator can function during multiple stages of transcription. These include (1) removal of repressor molecules from promoter DNA, (2) recruitment of GTFs and pol II to a promoter, (3) induction of conformation changes in the preinitiation complex, (4) induction of covalent modification of proteins in the preinitiation complex, and (5) stimulation of promoter clearance and elongation. These steps involve direct interactions between activators and GTFs. The condensation of eukaryotic DNA in chromatin functions not only to constrain the genome within the boundaries of the cell nucleus but also to suppress gene activity in a general manner. PHD-finger domain, a zinc finger-like motif, has a unique Cys4-His-Cys3 pattern, spanning approximately 50-80 residues. Generally the PHD-fingers are protein-protein interaction domains or that they recognize a set of similar nuclear targets related to chromatin structure and chromatin regulation, such as the differentially modified tails of the nucleosomal histones. We used the alpha-1 acid glycoprotein (AGP) gene as a model for studying transcriptional regulation. AGP is an acute responsive, liver-specific gene. Its expression is regulated by both positive and negative trans-acting factors. At least five cis elements have been identified within the 180-bp region of AGP promoter. Four of these sites, A, C, D and E are recognized by AGP/EBP or AGB/EBP-like factors in liver nuclear extracts. A, C, D and E regions are positive regulatory elements enhancing the expression of AGP gene while B motif is negative regulatory element repressing the expression of AGP gene. There are two parts in this thesis : (1) Biochemical purification and characterization of the negative transcription factors for AGP gene expression. The purified factor has been identified as nucleolin by amino acid analysis. Furthermore, we show that nucleolin can function as a transcription repressor for the AGP gene. (2) Identification, molecular cloning and biological characterization of a novel PHD-finger protein DPKAP (DNA-PK Activating Protein). DPKAP interacts with DNA-PK physically and functionally. DPKAP stimulates the DNA-PK kinase activity in vitro. Genetic evidence strongly suggests for the crucial role of DNA-PK in DNA double-strand break (DSB) repair and V(D)J recombination. However, the precise regulatory mechanism of DNA-PK in these processes remains to be elucidated. The potential in vivo functions of DPKAP on DNA DSB repair and V(D)J recombination remain to be investigated.
Capítulos de libros sobre el tema "Novel nucleolar protein"
Asea, Alexzander, Appukuttan R. Pradeep y Punit Kaur. "Nucleolin: A Novel Intracellular Transporter of HSPA1A". En Heat Shock Proteins, 115–24. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4740-1_8.
Texto completoA Becker-Kojić, Zorica, José Manuel García-Verdugo, Anne-Kathrin Schott, Vicente Herranz-Pérez, Ivan Zipančić y Vicente Hernández-Rabaza. "Membrane-to-Nucleus Signaling in Human Blood Progenitor Cells Reveals an Efficient GM-Free Reprogramming to Pluripotency". En Stem Cell Research [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.108950.
Texto completoActas de conferencias sobre el tema "Novel nucleolar protein"
Demokan, Semra, Alice Y. Chuang, Kavita M. Pattani, David Sidransky, Wayne Koch y Joseph A. Califano. "Abstract 666: Validation of nucleolar protein 4 as a novel methylated tumor suppressor gene in head and neck cancer." En Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-666.
Texto completoChiara, Brignole, Veronica Bensa, Genny Del Zotto, Silvia Bruno, Nuno A. Fonseca, Ana F. Cruz, Daniela Di Paolo et al. "Abstract A101: Nucleolin: A novel cell surface protein for neuroblastoma targeted therapy". En Abstracts: AACR-NCI-EORTC International Conference on Molecular Targets and Cancer Therapeutics; October 26-30, 2019; Boston, MA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1535-7163.targ-19-a101.
Texto completoWu, Guanhui, Buket Onel y Danzhou Yang. "Abstract 1474: Identifying novel chromatin binding sites of nucleolin protein in cancer cells". En Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1474.
Texto completoInformes sobre el tema "Novel nucleolar protein"
Paik, Jason C. The Role of a Novel Nucleolar Protein in Regulation of E2F1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, septiembre de 2009. http://dx.doi.org/10.21236/ada525619.
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