Relevant bibliographies by topics / UAP56

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  1. Journal articles
  2. Dissertations / Theses
  3. Conference papers

Academic literature on the topic 'UAP56'

Author: Grafiati
Published: 4 June 2021
Last updated: 2 February 2022

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Journal articles on the topic "UAP56"

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Taniguchi, Ichiro, and Mutsuhito Ohno. "ATP-Dependent Recruitment of Export Factor Aly/REF onto Intronless mRNAs by RNA Helicase UAP56." Molecular and Cellular Biology 28, no. 2 (2007): 601–8. http://dx.doi.org/10.1128/mcb.01341-07.

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ABSTRACT Loading of export factors onto mRNAs is a key step in gene expression. In vertebrates, splicing plays a role in this process. Specific protein complexes, exon junction complex and transcription/export complex, are loaded onto mRNAs in a splicing-dependent manner, and adaptor proteins such as Aly/REF in the complexes in turn recruit mRNA exporter TAP-p15 onto the RNA. By contrast, how export factors are recruited onto intronless mRNAs is largely unknown. We previously showed that Aly/REF is preferentially associated with intronless mRNAs in the nucleus. Here we show that Aly/REF could
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Xiong, Fuyin, Yanli Lin, Zhengbin Han, et al. "Plk1-mediated phosphorylation of UAP56 regulates the stability of UAP56." Molecular Biology Reports 39, no. 2 (2011): 1935–42. http://dx.doi.org/10.1007/s11033-011-0940-x.

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Kronemann, Daniel, Stacy R. Hagemeier, Dan Cygnar, Stacia Phillips, and Wade A. Bresnahan. "Binding of the Human Cytomegalovirus (HCMV) Tegument Protein UL69 to UAP56/URH49 Is Not Required for Efficient Replication of HCMV." Journal of Virology 84, no. 18 (2010): 9649–54. http://dx.doi.org/10.1128/jvi.00669-10.

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ABSTRACT The human cytomegalovirus (HCMV) tegument protein UL69 is important for efficient viral replication at low multiplicities of infection. Several molecular mechanisms by which UL69 contributes to HCMV replication have been proposed, including UL69's ability to interact with the mRNA export factors UAP56 and URH49 to facilitate the shuttling of viral mRNAs from the nuclei of infected cells. Using a UL69 viral mutant that is unable to bind UAP56 and URH49, we demonstrated that UL69's interaction with UAP56 or URH49 does not contribute to the growth phenotype associated with the UL69 delet
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Yamazaki, Tomohiro, Naoko Fujiwara, Hiroko Yukinaga, et al. "The Closely Related RNA helicases, UAP56 and URH49, Preferentially Form Distinct mRNA Export Machineries and Coordinately Regulate Mitotic Progression." Molecular Biology of the Cell 21, no. 16 (2010): 2953–65. http://dx.doi.org/10.1091/mbc.e09-10-0913.

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Nuclear export of mRNA is an essential process for eukaryotic gene expression. The TREX complex couples gene expression from transcription and splicing to mRNA export. Sub2, a core component of the TREX complex in yeast, has diversified in humans to two closely related RNA helicases, UAP56 and URH49. Here, we show that URH49 forms a novel URH49–CIP29 complex, termed the AREX (alternative mRNA export) complex, whereas UAP56 forms the human TREX complex. The mRNAs regulated by these helicases are different at the genome-wide level. The two sets of target mRNAs contain distinct subsets of key mit
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Gatfield, David, and Elisa Izaurralde. "REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export." Journal of Cell Biology 159, no. 4 (2002): 579–88. http://dx.doi.org/10.1083/jcb.200207128.

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The metazoan proteins UAP56, REF1, and NXF1 are thought to bind sequentially to mRNA to promote its export to the cytoplasm: UAP56 is thought to recruit REF1 to nascent mRNA; REF1 acts as an adaptor protein mediating the association of NXF1 with mRNA, whereas NXF1 translocates the mRNA across the nuclear pore complex. REF1 is a component of the exon–exon junction complex (EJC); thus, the EJC is thought to play a role in the export of spliced mRNA. NXF1 and UAP56 are essential for mRNA export. An essential role for metazoan REF1 or the additional EJC proteins in this process has not been establ
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Colgan, Kevin J., James R. Boyne, and Adrian Whitehouse. "Uncoupling of hTREX demonstrates that UAP56 and hTHO-complex recruitment onto herpesvirus saimiri intronless transcripts is required for replication." Journal of General Virology 90, no. 6 (2009): 1455–60. http://dx.doi.org/10.1099/vir.0.010124-0.

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Herpesvirus saimiri (HVS) ORF57 nucleocytoplasmic shuttle protein binds viral RNA and interacts with the cellular nuclear export adaptor protein, Aly, to access the TAP-mediated nuclear export pathway. This enables the efficient nuclear export of HVS intronless mRNAs. Herein, we extend these studies and demonstrate that ORF57 recruits several members of hTREX, namely Aly, UAP56 and hTHO-complex proteins, onto the viral mRNAs to assemble an export-competent ribonucleoprotein particle. Moreover, using a transdominant form of Aly which inhibits UAP56 and hTHO-complex association with viral intron
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Lischka, Peter, Zsolt Toth, Marco Thomas, Regina Mueller, and Thomas Stamminger. "The UL69 Transactivator Protein of Human Cytomegalovirus Interacts with DEXD/H-Box RNA Helicase UAP56 To Promote Cytoplasmic Accumulation of Unspliced RNA." Molecular and Cellular Biology 26, no. 5 (2006): 1631–43. http://dx.doi.org/10.1128/mcb.26.5.1631-1643.2006.

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ABSTRACT The UL69 gene product of human cytomegalovirus belongs to a family of regulatory proteins conserved among all herpesviruses that have in part been characterized as posttranscriptional transactivators participating in the nuclear export of RNA. Recent experiments suggested that pUL69 also acts as a posttranscriptional activator since it was demonstrated that nucleocytoplasmic shuttling via a CRM1-independent nuclear export signal is a prerequisite for its stimulatory effect on gene expression. Based on these findings we initiated studies to investigate the role of pUL69 in mRNA export
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Thomas, Marco, Eric Sonntag, Regina Müller, et al. "pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine Methyltransferase 6 via a Domain That Is Crucial for mRNA Export and Efficient Viral Replication." Journal of Virology 89, no. 18 (2015): 9601–15. http://dx.doi.org/10.1128/jvi.01399-15.

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ABSTRACTThe regulatory protein pUL69 of human cytomegalovirus acts as a viral mRNA export factor, facilitating the cytoplasmic accumulation of unspliced RNA via interaction with the cellular mRNA export factor UAP56. Here we provide evidence for a posttranslational modification of pUL69 via arginine methylation within the functionally important N terminus. First, we demonstrated a specific immunoprecipitation of full-length pUL69 as well as pUL69aa1-146 by a mono/dimethylarginine-specific antibody. Second, we observed a specific electrophoretic mobility shift upon overexpression of the catalyt
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Wang, Ke, Lantian Wang, Jianshu Wang, Suli Chen, Min Shi, and Hong Cheng. "Intronless mRNAs transit through nuclear speckles to gain export competence." Journal of Cell Biology 217, no. 11 (2018): 3912–29. http://dx.doi.org/10.1083/jcb.201801184.

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Nuclear speckles (NSs) serve as splicing factor storage sites. In this study, we unexpectedly found that many endogenous intronless mRNAs, which do not undergo splicing, associate with NSs. These associations do not require transcription, polyadenylation, or the polyA tail. Rather, exonic splicing enhancers present in intronless mRNAs and their binding partners, SR proteins, promote intronless mRNA localization to NSs. Significantly, speckle targeting of mRNAs promotes the recruitment of the TREX export complex and their TREX-dependent nuclear export. Furthermore, TREX, which accumulates in NS
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Lin, Haifan. "Capturing the Cloud: UAP56 in Nuage Assembly and Function." Cell 151, no. 4 (2012): 699–701. http://dx.doi.org/10.1016/j.cell.2012.10.026.

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Dissertations / Theses on the topic "UAP56"

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Kapadia, Fehmida. "Analyses of the thymidylate synthase promoter and an RNA helicase required for mRNA export." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1117635126.

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Thesis (Ph. D.)--Ohio State University, 2005.<br>Title from first page of PDF file. Document formatted into pages; contains xvii, 179 p.; also includes graphics. Includes bibliographical references (p. 155-179). Available online via OhioLINK's ETD Center
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Zhang, Meng. "UAP56: A Dead Box Protein Required for Pre-mRNA Splicing: A Dissertation." eScholarship@UMMS, 1999. http://escholarship.umassmed.edu/gsbs_diss/173.

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Splicing of mRNA precursors (pre-mRNA) comprises a series of ATP-dependent steps, the first of which is the stable binding of U2 snRNP at the pre-mRNA branchpoint. The basis of ATP use in splicing is not well understood. Several yeast splicing factors belong to DEAD/H box family of RNA-dependent ATPase, and are implicated in dynamic RNA structure rearrangement during spliceosome assembly. In mammals, however, such information is conspicuously lacking. In fact, none of the known mammalian splicing factors has characteristics for ATP hydrolysis. In an attempt to identify mammalian splicing facto
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Zhang, Fan. "A Novel Role of UAP56 in piRNA Mediated Transposon Silencing: A Dissertation." eScholarship@UMMS, 2013. http://escholarship.umassmed.edu/gsbs_diss/685.

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Transposon silencing is required to maintain genome stability. The non-coding piRNAs effectively suppress of transposon activity during germline development. In the Drosophila female germline, long precursors of piRNAs are transcribed from discrete heterochromatic clusters and then processed into primary piRNAs in the perinuclear nuage. However, the detailed mechanism of piRNA biogenesis, specifically how the nuclear and cytoplasmic processes are connected, is not well understood. The nuclear DEAD box protein UAP56 has been previously implicated in protein-coding gene transcript splicing and e
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藤田, 賢一. "DEADbox型RNAヘリカーゼUAP56とURH49による複合体リモデリングを介したmRNA輸送機構に関する研究". Kyoto University, 2020. http://hdl.handle.net/2433/253469.

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Lin, Jared. "CHARACTERIZING THE ROLE OF N TERMINUS OF INFLUENZA A NUCLEOPROTEIN FOR LOCATION AND VIRAL RNP ACTIVITY." CSUSB ScholarWorks, 2018. https://scholarworks.lib.csusb.edu/etd/694.

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The influenza viral ribonucleoprotein complexes (vRNPs) are responsible for viral RNA synthesis. Each vRNP is comprised of one vRNA segment, the viral RNA dependent RNA polymerase complex (RdRP), and multiple copies of nucleoprotein (NP). NP serves as scaffold in formation of vRNPs, but also regulates vRNP activity. The N-terminus of NP contains a nonconventional nuclear localization signal (NLS1) essential for initial vRNP nuclear import, but also interacts with host RNA helicases to enhance viral RNA replication in the nucleus. NP contains at least one additional NLS sequence, with bioinform
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Thomas, Marco. "Molecular characterization of UAP56- and pUL69-protein interactions with respect to their impact on nuclear mRNA export during human cytomegalovirus infection." kostenfrei, 2009. http://d-nb.info/994815441/34.

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Zhang, Gen. "TREX Function in piRNA Biogenesis and Transposon Silencing." eScholarship@UMMS, 2019. https://escholarship.umassmed.edu/gsbs_diss/1056.

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The Piwi interacting RNA pathway (piRNA) transcriptionally and post-transcriptionally silences transposons in the germline to maintain host genome integrity and faithful transmission of the genetic materials. In Drosophilaovaries, maternally loaded piRNAs kick-start piRNA biogenesis and convert precursor transcripts into piRNAs to replenish the piRNA pool during oogenesis. piRNA clusters are the genomic source of piRNA precursors, which are determined by the HP1 homolog Rhino and accessary factors. Rhino specifically binds to piRNA cluster chromatin. I was intrigued by how Rhino localizes to p
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Pryor, Anne M. "Growth-regulated expression and G0-specific turnover of the mRNA that encodes AH49, a mammalian protein highly related to the mRNA export protein UAP56." Connect to this title online, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1069259604.

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Thesis (Ph. D.)--Ohio State University, 2003.<br>Title from first page of PDF file. Document formatted into pages; contains xii, 187 p.; also includes graphics (some col.) Includes bibliographical references (p. 175-187). Available online via OhioLINK's ETD Center
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山崎, 智弘. "DEAD box型RNAヘリカーゼUAP56とURH49が形成するmRNA核外輸送経路に関する研究". 京都大学 (Kyoto University), 2010. http://hdl.handle.net/2433/126748.

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Giede-Jeppe, Antje [Verfasser]. "Generierung und Charakterisierung rekombinanter Cytomegaloviren mit Mutation der UAP56-Bindungsstelle sowie RNA-Bindungsdomäne des viralen mRNA-Exportfaktors pUL69 / vorgelegt von Antje Giede-Jeppe." 2011. http://d-nb.info/1013100506/34.

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Conference papers on the topic "UAP56"

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Carvalho, Renato S., Thales C. Nepomuceno, Michael Sweet, Alvaro N. Monteiro, and Marcelo A. Carvalho. "Abstract 1117: Characterization of BAT1 (UAP56) interaction with BARD1." 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.am10-1117.

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