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                <text>DOI: 10.5213/inj.2020edi.001</text>
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                <text>International Neurourology Journal</text>
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                <text>Diseases of the genitourinary system. Urology</text>
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            <description>A language of the resource</description>
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                  <text>Dominio científico: Coronavirus</text>
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                <text>We have to write and share valid and reliable information on COVID-19</text>
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            <description>An entity primarily responsible for making the resource</description>
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                <text>Su May Liew, Ee Ming Khoo, Wee Kooi Cheah, Kalaiarasu Peariasamy, Pik-Pin Goh, Hishamshah M. Ibrahim</text>
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                <text>Te world has been grappling with the outbreak of COVID-19 for the past few months. Te coronavirus, which was frst reported in Wuhan, China has now spread to 82 countries and infected more than 95000 individuals.  As of March 5, 2020, there have been 55 confrmed cases of COVID-19 in Malaysia.</text>
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                <text>Malaysian Family Physician</text>
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                <text>Medicine</text>
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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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                <text>Sharing Our Experience of Operating an Endoscopy Unit in the Midst of a COVID-19 Outbreak</text>
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                <text>Jimin Han, Eun Young Kim</text>
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                <text>DOI: 10.5946/ce.2020.076</text>
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                <text>Clinical Endoscopy</text>
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            <description>An entity responsible for making the resource available</description>
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                <text>Hoon Jai Chun</text>
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                <text>Internal medicine, Diseases of the digestive system. Gastroenterology</text>
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            <description>A language of the resource</description>
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              <name>Title</name>
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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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                <text>Dynamically-driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain.</text>
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            <name>Creator</name>
            <description>An entity primarily responsible for making the resource</description>
            <elementTextContainer>
              <elementText elementTextId="2457">
                <text>Jiahai Shi, Nanyu Han, Liangzhong Lim, Shixiong Lua, J Sivaraman, Lushan Wang, Yuguang Mu, Jianxing Song</text>
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          <element elementId="41">
            <name>Description</name>
            <description>An account of the resource</description>
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              <elementText elementTextId="2458">
                <text>Despite utilizing the same chymotrypsin fold to host the catalytic machinery, coronavirus 3C-like proteases (3CLpro) noticeably differ from picornavirus 3C proteases in acquiring an extra helical domain in evolution. Previously, the extra domain was demonstrated to regulate the catalysis of the SARS-CoV 3CLpro by controlling its dimerization. Here, we studied N214A, another mutant with only a doubled dissociation constant but significantly abolished activity. Unexpectedly, N214A still adopts the dimeric structure almost identical to that of the wild-type (WT) enzyme. Thus, we conducted 30-ns molecular dynamics (MD) simulations for N214A, WT, and R298A which we previously characterized to be a monomer with the collapsed catalytic machinery. Remarkably, three proteases display distinctive dynamical behaviors. While in WT, the catalytic machinery stably retains in the activated state; in R298A it remains largely collapsed in the inactivated state, thus implying that two states are not only structurally very distinguishable but also dynamically well separated. Surprisingly, in N214A the catalytic dyad becomes dynamically unstable and many residues constituting the catalytic machinery jump to sample the conformations highly resembling those of R298A. Therefore, the N214A mutation appears to trigger the dramatic change of the enzyme dynamics in the context of the dimeric form which ultimately inactivates the catalytic machinery. The present MD simulations represent the longest reported so far for the SARS-CoV 3CLpro, unveiling that its catalysis is critically dependent on the dynamics, which can be amazingly modulated by the extra domain. Consequently, mediating the dynamics may offer a potential avenue to inhibit the SARS-CoV 3CLpro.</text>
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                <text>2011</text>
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                <text>DOI: 10.1371/journal.pcbi.1001084</text>
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                <text>PLoS Computational Biology</text>
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                <text>Public Library of Science (PLoS)</text>
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                <text>Biology (General)</text>
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            <description>A language of the resource</description>
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              <name>Title</name>
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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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                <elementText elementTextId="2">
                  <text>Dominio científico: Coronavirus</text>
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              </elementTextContainer>
            </element>
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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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      <elementSet elementSetId="1">
        <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">
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                <text>In vitro reconstitution of SARS-coronavirus mRNA cap methylation.</text>
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            <name>Creator</name>
            <description>An entity primarily responsible for making the resource</description>
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              <elementText elementTextId="2448">
                <text>Mickaël Bouvet, Claire Debarnot, Isabelle Imbert, Barbara Selisko, Eric J. Snijder, Bruno Canard, Etienne Decroly</text>
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            <description>An account of the resource</description>
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                <text>SARS-coronavirus (SARS-CoV) genome expression depends on the synthesis of a set of mRNAs, which presumably are capped at their 5' end and direct the synthesis of all viral proteins in the infected cell. Sixteen viral non-structural proteins (nsp1 to nsp16) constitute an unusually large replicase complex, which includes two methyltransferases putatively involved in viral mRNA cap formation. The S-adenosyl-L-methionine (AdoMet)-dependent (guanine-N7)-methyltransferase (N7-MTase) activity was recently attributed to nsp14, whereas nsp16 has been predicted to be the AdoMet-dependent (nucleoside-2'O)-methyltransferase. Here, we have reconstituted complete SARS-CoV mRNA cap methylation in vitro. We show that mRNA cap methylation requires a third viral protein, nsp10, which acts as an essential trigger to complete RNA cap-1 formation. The obligate sequence of methylation events is initiated by nsp14, which first methylates capped RNA transcripts to generate cap-0 (7Me)GpppA-RNAs. The latter are then selectively 2'O-methylated by the 2'O-MTase nsp16 in complex with its activator nsp10 to give rise to cap-1 (7Me)GpppA(2'OMe)-RNAs. Furthermore, sensitive in vitro inhibition assays of both activities show that aurintricarboxylic acid, active in SARS-CoV infected cells, targets both MTases with IC(50) values in the micromolar range, providing a validated basis for anti-coronavirus drug design.</text>
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                <text>2010</text>
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                <text>DOI: 10.1371/journal.ppat.1000863</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>
            <elementTextContainer>
              <elementText elementTextId="2454">
                <text>Biology (General), Immunologic diseases. Allergy</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="44">
            <name>Language</name>
            <description>A language of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="2455">
                <text>EN</text>
              </elementText>
            </elementTextContainer>
          </element>
        </elementContainer>
      </elementSet>
    </elementSetContainer>
  </item>
</itemContainer>
