Acylation of proteins — a new type of modification of membrane glycoproteins
Identifieur interne : 000416 ( Istex/Curation ); précédent : 000415; suivant : 000417Acylation of proteins — a new type of modification of membrane glycoproteins
Auteurs : Michael F. G. Schmidt [Allemagne]Source :
- Trends in Biochemical Sciences [ 0968-0004 ] ; 1982.
English descriptors
- Teeft :
- Acyl chains, Acylated, Acylated glycoproteins, Acylated peptides, Acylation, Acylation site, Bilayer, Biol, Bishr omary, Cell surface, Cellular membrane glycoproteins, Common feature, Fatty, Fatty acid, Fatty acid attachment sites, Fatty acids, Glycoprotein, Hydroxyamino acids, Intracellular transport, Lipid, Lipid bilayer, Membrane, Membrane fusion, Membrane proteins, Natl acad, Plasma membrane, Protein acylation, Schmidt, Sendai virus, Sindbis virus, Transferrin receptor, Viral, Viral glycoproteins, Viral lipid bilayer.
Abstract
Abstract: Fatty acids are covalently attached to many membrane glycoproteins during their biosynthesis.
Url:
DOI: 10.1016/0968-0004(82)90263-8
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<affiliation wicri:level="1"><mods:affiliation>Michael F. G. Schmidt is at the Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, 6300 Giessen, FRG</mods:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Michael F. G. Schmidt is at the Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, 6300 Giessen</wicri:regionArea>
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<sourceDesc><biblStruct><analytic><title level="a">Acylation of proteins — a new type of modification of membrane glycoproteins</title>
<author><name sortKey="Schmidt, Michael F G" sort="Schmidt, Michael F G" uniqKey="Schmidt M" first="Michael F. G." last="Schmidt">Michael F. G. Schmidt</name>
<affiliation wicri:level="1"><mods:affiliation>Michael F. G. Schmidt is at the Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, 6300 Giessen, FRG</mods:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Michael F. G. Schmidt is at the Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, 6300 Giessen</wicri:regionArea>
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<series><title level="j">Trends in Biochemical Sciences</title>
<title level="j" type="abbrev">TIBS</title>
<idno type="ISSN">0968-0004</idno>
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<date type="published" when="1982">1982</date>
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<profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acyl chains</term>
<term>Acylated</term>
<term>Acylated glycoproteins</term>
<term>Acylated peptides</term>
<term>Acylation</term>
<term>Acylation site</term>
<term>Bilayer</term>
<term>Biol</term>
<term>Bishr omary</term>
<term>Cell surface</term>
<term>Cellular membrane glycoproteins</term>
<term>Common feature</term>
<term>Fatty</term>
<term>Fatty acid</term>
<term>Fatty acid attachment sites</term>
<term>Fatty acids</term>
<term>Glycoprotein</term>
<term>Hydroxyamino acids</term>
<term>Intracellular transport</term>
<term>Lipid</term>
<term>Lipid bilayer</term>
<term>Membrane</term>
<term>Membrane fusion</term>
<term>Membrane proteins</term>
<term>Natl acad</term>
<term>Plasma membrane</term>
<term>Protein acylation</term>
<term>Schmidt</term>
<term>Sendai virus</term>
<term>Sindbis virus</term>
<term>Transferrin receptor</term>
<term>Viral</term>
<term>Viral glycoproteins</term>
<term>Viral lipid bilayer</term>
</keywords>
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<langUsage><language ident="en">en</language>
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<front><div type="abstract" xml:lang="en">Abstract: Fatty acids are covalently attached to many membrane glycoproteins during their biosynthesis.</div>
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