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      <src>https://www.socictopen.socict.org/files/original/a94e792ab540457e522195ecaabeca3b.pdf</src>
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          <element elementId="50">
            <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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    <name>Text</name>
    <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>Dublin Core</name>
      <description>The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.</description>
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        <element elementId="50">
          <name>Title</name>
          <description>A name given to the resource</description>
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              <text>Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.</text>
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          <name>Creator</name>
          <description>An entity primarily responsible for making the resource</description>
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              <text>Jian Shang, Yu-Shun Wan, Chang Liu, Boyd Yount, Kendra Gully, Yang Yang, Ashley Auerbach, Guiqing Peng, Ralph Baric, Fang Li</text>
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          <name>Description</name>
          <description>An account of the resource</description>
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              <text>Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse hepatitis coronavirus (MHV) is the only known coronavirus that uses the N-terminal domain (NTD) of its spike to recognize a protein receptor, CEACAM1a. Here we determined the cryo-EM structure of MHV spike complexed with mouse CEACAM1a. The trimeric spike contains three receptor-binding S1 heads sitting on top of a trimeric membrane-fusion S2 stalk. Three receptor molecules bind to the sides of the spike trimer, where three NTDs are located. Receptor binding induces structural changes in the spike, weakening the interactions between S1 and S2. Using protease sensitivity and negative-stain EM analyses, we further showed that after protease treatment of the spike, receptor binding facilitated the dissociation of S1 from S2, allowing S2 to transition from pre-fusion to post-fusion conformation. Together these results reveal a new role of receptor binding in MHV entry: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes. Our study provides new mechanistic insight into coronavirus entry and highlights the diverse entry mechanisms used by different viruses.</text>
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          <name>Date</name>
          <description>A point or period of time associated with an event in the lifecycle of the resource</description>
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              <text>2020</text>
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          <name>Identifier</name>
          <description>An unambiguous reference to the resource within a given context</description>
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              <text>DOI: 10.1371/journal.ppat.1008392</text>
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          <name>Source</name>
          <description>A related resource from which the described resource is derived</description>
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              <text>PLoS Pathogens</text>
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          <name>Publisher</name>
          <description>An entity responsible for making the resource available</description>
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              <text>Public Library of Science (PLoS)</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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            <elementText elementTextId="14944">
              <text>Biology (General), Immunologic diseases. Allergy</text>
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          <name>Language</name>
          <description>A language of the resource</description>
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            <elementText elementTextId="14945">
              <text>EN</text>
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