
<mods xmlns="http://www.loc.gov/mods/v3" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-4.xsd">
  <titleInfo>
    <title>Characterization of the major nuclear localization signal of the Borna disease virus phosphoprotein</title>
  </titleInfo>
  <name type="personal">
    <namePart type="family">Schwemmle</namePart>
    <namePart type="given">Martin</namePart>
    <role>
      <roleTerm type="text">author</roleTerm>
    </role>
  </name>
  <name type="personal">
    <namePart type="family">Jehle</namePart>
    <namePart type="given">Christian</namePart>
    <role>
      <roleTerm type="text">author</roleTerm>
    </role>
  </name>
  <name type="personal">
    <namePart type="family">Shoemaker</namePart>
    <namePart type="given">Trevor</namePart>
    <role>
      <roleTerm type="text">author</roleTerm>
    </role>
  </name>
  <name ID="wil2001" type="personal">
    <namePart type="family">Lipkin</namePart>
    <namePart type="given">W. Ian</namePart>
    <role>
      <roleTerm type="text">author</roleTerm>
    </role>
  </name>
  <name ID="originator_1" type="corporate">
    <namePart>Columbia University. Center for Infection and Immunity</namePart>
    <role>
      <roleTerm type="text">originator</roleTerm>
    </role>
  </name>
  <typeOfResource>text</typeOfResource>
  <genre>Articles</genre>
  <originInfo>
    <dateIssued encoding="w3cdtf" keyDate="yes">1999</dateIssued>
  </originInfo>
  <language>
    <languageTerm type="text">English</languageTerm>
  </language>
  <abstract>Borna disease virus (BDV) replicates and transcribes its negative-sense RNA genome in the nucleus. The BDV phosphoprotein (P) is localized in the nucleus of infected cells and cells transfected with P expression constructs. To identify the nuclear localization signal (NLS) of P, COS- 7 cells were transfected with wild-type or mutant forms of P fused with green fluorescent protein (GFP). Whereas GFP alone was exclusively cytoplasmic, P or P-GFP were nuclear. Analysis of carboxy- and amino- terminal truncation mutants of P indicated that amino acids (aa) 20-37 are sufficient to promote efficient nuclear accumulation of the fusion protein. Residual nuclear import of GFP was observed with portions of P including aa 33-134 or aa 134-201, suggesting the presence of additional NLS motifs. The major NLS of P appears to be bipartite. It consists of two basic aa domains, R22RER25 and R30PRKIPR36, separated by four non-basic aa, S26GSP29.</abstract>
  <subject>
    <topic>Epidemiology</topic>
  </subject>
  <subject>
    <topic>Virology</topic>
  </subject>
  <relatedItem type="host">
    <titleInfo>
      <title>Journal of general virology</title>
    </titleInfo>
    <part>
      <detail type="volume">
        <number>80</number>
      </detail>
      <detail type="issue">
        <number>1</number>
      </detail>
      <extent unit="page">
        <start>97</start>
        <end>100</end>
      </extent>
      <date>1999</date>
    </part>
    <identifier type="issn">0022-1317</identifier>
  </relatedItem>
  <identifier type="hdl">http://hdl.handle.net/10022/AC:P:9988</identifier>
  <location>
    <physicalLocation authority="marcorg">NNC</physicalLocation>
  </location>
  <accessCondition type="use and reproduction">
    <copyrightNotice>Copyright © 1999 by the Society for General Microbiology</copyrightNotice>
  </accessCondition>
  <recordInfo>
    <recordContentSource authority="marcorg">NNC</recordContentSource>
    <recordCreationDate encoding="w3cdtf">2011-03-17 20:04:22 UTC</recordCreationDate>
    <recordChangeDate encoding="w3cdtf">2011-03-17 20:20:12 UTC</recordChangeDate>
    <recordIdentifier>3114</recordIdentifier>
    <languageOfCataloging>
      <languageTerm authority="iso639-2b">eng</languageTerm>
    </languageOfCataloging>
  </recordInfo>
</mods>
