<?xml version="1.0" encoding="UTF-8"?>
<collection xmlns="http://www.loc.gov/MARC21/slim">
 <record>
  <leader>     caa a22        4500</leader>
  <controlfield tag="001">475846524</controlfield>
  <controlfield tag="003">CHVBK</controlfield>
  <controlfield tag="005">20180406123915.0</controlfield>
  <controlfield tag="007">cr unu---uuuuu</controlfield>
  <controlfield tag="008">170329e20001001xx      s     000 0 eng  </controlfield>
  <datafield tag="024" ind1="7" ind2="0">
   <subfield code="a">10.1007/PL00000635</subfield>
   <subfield code="2">doi</subfield>
  </datafield>
  <datafield tag="035" ind1=" " ind2=" ">
   <subfield code="a">(NATIONALLICENCE)springer-10.1007/PL00000635</subfield>
  </datafield>
  <datafield tag="245" ind1="0" ind2="4">
   <subfield code="a">The role of glycosylation in ionotropic glutamate receptor ligand binding, function, and trafficking</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[S. Standley, M. Baudry]</subfield>
  </datafield>
  <datafield tag="520" ind1="3" ind2=" ">
   <subfield code="a">Abstract.: Members of the ionotropic glutarnate receptor (iGluR) family have between 4 and 12 consensus asparagine (N)-linked glycosylation sites. They are localized on the extracellular N-termini, and the loop between the penultimate and last transmembrane domains. These regions also contain the essential elements for formation of the ligand binding site. N-linked glycosylation does not appear to be essential for formation of the ligand binding site per se, but there are demonstrated interactions between glycosylation state and ligand binding affinity, receptor physiology, susceptibility to allosteric modulation and, in some cases, trafficking. There is no indication of a general role for N-linked glycosylation in iGluRs; instead the effects of glycosylation vary among glutamate receptor subtypes and splice variants, with specific effects on structure or function with different subunits.</subfield>
  </datafield>
  <datafield tag="540" ind1=" " ind2=" ">
   <subfield code="a">Birkhäuser Verlag Basel,, 2000</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">Key words. Glutamate</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">receptors</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">glycosylation</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">ionotropic</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">asparagine-linked</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Standley</subfield>
   <subfield code="D">S.</subfield>
   <subfield code="u">Laboratory of Neurochemistry, Bldg. 36, Rm. 51308, NIDCD, National Institute of Health, Bethesda (Maryland 20892, USA), US</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="700" ind1="1" ind2=" ">
   <subfield code="a">Baudry</subfield>
   <subfield code="D">M.</subfield>
   <subfield code="u">Neuroscience Program, University of Southern California, Los Angeles (California, 90089-2520, USA), US</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="856" ind1="4" ind2="0">
   <subfield code="u">https://doi.org/10.1007/PL00000635</subfield>
   <subfield code="q">text/html</subfield>
   <subfield code="z">Onlinezugriff via DOI</subfield>
  </datafield>
  <datafield tag="908" ind1=" " ind2=" ">
   <subfield code="D">1</subfield>
   <subfield code="a">research-article</subfield>
   <subfield code="2">jats</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">856</subfield>
   <subfield code="E">40</subfield>
   <subfield code="u">https://doi.org/10.1007/PL00000635</subfield>
   <subfield code="q">text/html</subfield>
   <subfield code="z">Onlinezugriff via DOI</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Standley</subfield>
   <subfield code="D">S.</subfield>
   <subfield code="u">Laboratory of Neurochemistry, Bldg. 36, Rm. 51308, NIDCD, National Institute of Health, Bethesda (Maryland 20892, USA), US</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="950" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="P">700</subfield>
   <subfield code="E">1-</subfield>
   <subfield code="a">Baudry</subfield>
   <subfield code="D">M.</subfield>
   <subfield code="u">Neuroscience Program, University of Southern California, Los Angeles (California, 90089-2520, USA), US</subfield>
   <subfield code="4">aut</subfield>
  </datafield>
  <datafield tag="900" ind1=" " ind2="7">
   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
   <subfield code="2">nationallicence</subfield>
  </datafield>
  <datafield tag="898" ind1=" " ind2=" ">
   <subfield code="a">BK010053</subfield>
   <subfield code="b">XK010053</subfield>
   <subfield code="c">XK010000</subfield>
  </datafield>
  <datafield tag="949" ind1=" " ind2=" ">
   <subfield code="B">NATIONALLICENCE</subfield>
   <subfield code="F">NATIONALLICENCE</subfield>
   <subfield code="b">NL-springer</subfield>
  </datafield>
 </record>
</collection>
