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    <creators>
      <item>
        <name>
          <family>Cho</family>
          <given>Won Jin</given>
        </name>
      </item>
      <item>
        <name>
          <family>Lee</family>
          <given>Jin-Sook</given>
        </name>
      </item>
      <item>
        <name>
          <family>Zhang</family>
          <given>Lei</given>
        </name>
      </item>
      <item>
        <name>
          <family>Ren</family>
          <given>Gang</given>
        </name>
      </item>
      <item>
        <name>
          <family>Shin</family>
          <given>Leah</given>
        </name>
      </item>
      <item>
        <name>
          <family>Manke</family>
          <given>Charles W</given>
        </name>
      </item>
      <item>
        <name>
          <family>Potoff</family>
          <given>Jeffrey</given>
        </name>
      </item>
      <item>
        <name>
          <family>Kotaria</family>
          <given>Nato</given>
        </name>
        <id>N_KOTARIA@YAHOO.COM</id>
      </item>
      <item>
        <name>
          <family>Zhvania</family>
          <given>Mzia G</given>
        </name>
        <id>mzia_zhvania@iliauni.edu.ge</id>
      </item>
      <item>
        <name>
          <family>Jena</family>
          <given>Bhanu P</given>
        </name>
        <id>bjena@med.wayne.edu</id>
      </item>
    </creators>
    <title>Membrane-directed molecular assembly
of the neuronal SNARE complex
Won</title>
    <ispublished>pub</ispublished>
    <subjects>
      <item>QP</item>
    </subjects>
    <divisions>
      <item>ins10</item>
    </divisions>
    <full_text_status>public</full_text_status>
    <abstract>Since the discovery and implication of N-ethylmaleimide-sensitive factor (NSF)-attachment protein receptor (SNARE) proteins in membrane
fusion almost two decades ago, there have been significant efforts to understand their involvement at the molecular level. In the
current study, we report for the first time the molecular interaction between full-length recombinant t-SNAREs and v-SNARE present in
opposing liposomes, leading to the assembly of a t-/v-SNARE ring complex. Using high-resolution electron microscopy, the electron
density maps and 3D topography of the membrane-directed SNARE ring complex was determined at nanometre resolution. Similar to
the t-/v-SNARE ring complex formed when 50 nm v-SNARE liposomes meet a t-SNARE-reconstituted planer membrane, SNARE rings
are also formed when 50 nm diameter isolated synaptic vesicles (SVs) meet a t-SNARE-reconstituted planer lipid membrane.
Furthermore, the mathematical prediction of the SNARE ring complex size with reasonable accuracy, and the possible mechanism of
membrane-directed t-/v-SNARE ring complex assembly, was determined from the study. Therefore in the present study, using both
lipososome-reconstituted recombinant t-/v-SNARE proteins, and native v-SNARE present in isolated SV membrane, the membranedirected
molecular assembly of the neuronal SNARE complex was determined for the first time and its size mathematically predicted.
These results provide a new molecular understanding of the universal machinery and mechanism of membrane fusion in cells, having
fundamental implications in human health and disease.</abstract>
    <date>2011</date>
    <publication>Journal of Cellular and Molecular Medicine</publication>
    <volume>15</volume>
    <number>1</number>
    <publisher>Wiley</publisher>
    <pagerange>31-37</pagerange>
    <refereed>TRUE</refereed>
    <issn>1582-4934</issn>
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