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            <name>Title</name>
            <description>A name given to the resource</description>
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                <text>Coronavirus</text>
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            <name>Description</name>
            <description>An account of the resource</description>
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                <text>Dominio científico: Coronavirus</text>
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    <description>A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.</description>
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          <name>Title</name>
          <description>A name given to the resource</description>
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              <text>Molecular Characterizations of Subcellular Localization Signals in the Nucleocapsid Protein of Porcine Epidemic Diarrhea Virus</text>
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          <name>Creator</name>
          <description>An entity primarily responsible for making the resource</description>
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              <text>Da Shi, Maojie Lv, Jianfei Chen, Hongyan Shi, Sha Zhang, Xin Zhang, Li Feng</text>
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          <name>Description</name>
          <description>An account of the resource</description>
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              <text>The nucleolus is a dynamic subnuclear structure, which is crucial to the normal operation of the eukaryotic cell. The porcine epidemic diarrhea virus (PEDV), coronavirus nucleocapsid (N) protein, plays important roles in the process of virus replication and cellular infection. Virus infection and transfection showed that N protein was predominately localized in the cytoplasm, but also found in the nucleolus in Vero E6 cells. Furthermore, by utilizing fusion proteins with green fluorescent protein (GFP), deletion mutations or site-directed mutagenesis of PEDV N protein, coupled with live cell imaging and confocal microscopy, it was revealed that, a region spanning amino acids (aa), 71–90 in region 1 of the N protein was sufficient for nucleolar localization and R87 and R89 were critical for its function. We also identified two nuclear export signals (NES, aa221–236, and 325–364), however, only the nuclear export signal (aa325–364) was found to be functional in the context of the full-length N protein. Finally, the activity of this nuclear export signal (NES) was inhibited by the antibiotic Lepomycin B, suggesting that N is exported by a chromosome region maintenance 1-related export pathway.</text>
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          <name>Date</name>
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              <text>2014</text>
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          <name>Subject</name>
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              <text>CHROMOSOME region maintenance 1, Nucleocapsid protein, porcine epidemic diarrhea virus, subcellular localization signals</text>
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          <name>Identifier</name>
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              <text>DOI: 10.3390/v6031253</text>
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          <name>Source</name>
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              <text>Viruses</text>
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          <name>Publisher</name>
          <description>An entity responsible for making the resource available</description>
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              <text>MDPI AG</text>
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          <name>Coverage</name>
          <description>The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant</description>
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              <text>Microbiology</text>
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          <name>Language</name>
          <description>A language of the resource</description>
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            <elementText elementTextId="4576">
              <text>EN</text>
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