<?xml version="1.0" encoding="UTF-8"?>
<?xml-stylesheet type="text/xsl" href="/oai-pmh.xsl"?>
<OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd">
  <responseDate>2026-09-23T06:10:23Z</responseDate>
  <request identifier="oai:www.ideals.illinois.edu:2142/87067" metadataPrefix="etdms" verb="GetRecord">https://www.ideals.illinois.edu/oai-pmh</request>
  <GetRecord>
    <record>
      <header>
        <identifier>oai:www.ideals.illinois.edu:2142/87067</identifier>
        <datestamp>2023-07-11</datestamp>
        <setSpec>col_2142_5131</setSpec>
        <setSpec>col_2142_16357</setSpec>
        <setSpec>com_2142_5130</setSpec>
        <setSpec>com_2142_16356</setSpec>
        <setSpec>com_2142_8913</setSpec>
        <setSpec>com_2142_8903</setSpec>
      </header>
      <metadata>
        <thesis xmlns="http://www.ndltd.org/standards/metadata/etdms/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.ndltd.org/standards/metadata/etdms/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdms11.xsd http://purl.org/dc/elements/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdmsdc.xsd">
          <dc:contributor>Bush, Daniel R.</dc:contributor>
          <dc:creator>Lu, Mei-Yeh Jade</dc:creator>
          <dc:date>2015-09-28T15:23:00Z</dc:date>
          <dc:date>2015-09-28T15:23:00Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1998</dc:date>
          <dc:date>1998</dc:date>
          <dc:description>"To explore other functionally-important domains, the AtSUC1 cDNA was randomly mutagenized and transformed yeast were screened on sucrose- or maltose-limited media for growth. Three point mutations were identified---H65Q, G334S, and L461P. Significantly, they all displayed enhanced sucrose transport rate. H65Q and G334S also increased maltose transport activity. In the predicted ""6-loop-6"" topology of the symporter, these residues all face extracellularly, suggesting their involvement in substrate binding. To investigate this hypothesis, the symporter-expressing COS-1 cells were analyzed by epitope-tagging and immunofluorescence. The results showed that both N- and C-termini, as well as the central loop, are located on the cytoplasmic side of the membrane."</dc:description>
          <dc:description>Made available in DSpace on 2015-09-28T15:23:00Z (GMT). No. of bitstreams: 2
license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5)
9912310.pdf: 3930939 bytes, checksum: f8e18bca2968d3dbadd6522ee8d7681a (MD5)
  Previous issue date: 1998</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 88348
Lift date: Forever
Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:description>124 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/87067</dc:identifier>
          <dc:identifier>(MiAaPQ)AAI9912310</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:subject>Biology, Cell</dc:subject>
          <dc:title>Molecular Cloning and Structure-Function Analysis of the Plant Proton-Sucrose Symporter</dc:title>
          <dc:type>text</dc:type>
          <degree>
            <department>Plant Biology</department>
            <discipline>Plant Biology</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
          </degree>
        </thesis>
      </metadata>
    </record>
  </GetRecord>
</OAI-PMH>
