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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>Dublin Core</name>
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          <name>Title</name>
          <description>A name given to the resource</description>
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              <text>Proteomic analysis of purified coronavirus infectious bronchitis virus particles</text>
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          <name>Creator</name>
          <description>An entity primarily responsible for making the resource</description>
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              <text>Shu Dingming, Li Linlin, Zhang Chengwen, Ren Xiangpeng, Xue Chunyi, Kong Qingming, Bi Yingzuo, Cao Yongchang</text>
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              <text>Abstract Background Infectious bronchitis virus (IBV) is the coronavirus of domestic chickens causing major economic losses to the poultry industry. Because of the complexity of the IBV life cycle and the small number of viral structural proteins, important virus-host relationships likely remain to be discovered. Toward this goal, we performed two-dimensional gel electrophoresis fractionation coupled to mass spectrometry identification approaches to perform a comprehensive proteomic analysis of purified IBV particles. Results Apart from the virus-encoded structural proteins, we detected 60 host proteins in the purified virions which can be grouped into several functional categories including intracellular trafficking proteins (20%), molecular chaperone (18%), macromolcular biosynthesis proteins (17%), cytoskeletal proteins (15%), signal transport proteins (15%), protein degradation (8%), chromosome associated proteins (2%), ribosomal proteins (2%), and other function proteins (3%). Interestingly, 21 of the total host proteins have not been reported to be present in virions of other virus families, such as major vault protein, TENP protein, ovalbumin, and scavenger receptor protein. Following identification of the host proteins by proteomic methods, the presence of 4 proteins in the purified IBV preparation was verified by western blotting and immunogold labeling detection. Conclusions The results present the first standard proteomic profile of IBV and may facilitate the understanding of the pathogenic mechanisms.</text>
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          <name>Date</name>
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              <text>2010</text>
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          <name>Identifier</name>
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              <text>DOI: 10.1186/1477-5956-8-29</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>Proteome Science</text>
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          <name>Publisher</name>
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              <text>BMC</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="18119">
              <text>Cytology</text>
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          <name>Language</name>
          <description>A language of the resource</description>
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              <text>EN</text>
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