Acylation of proteins — a new type of modification of membrane glycoproteins
Identifieur interne : 001689 ( Main/Exploration ); précédent : 001688; suivant : 001690Acylation 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
Affiliations:
Links toward previous steps (curation, corpus...)
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- to stream Istex, to step Curation: 000416
- to stream Istex, to step Checkpoint: 000805
- to stream Main, to step Merge: 001718
- to stream Main, to step Curation: 001689
Le document en format XML
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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"><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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<wicri:noRegion>6300 Giessen</wicri:noRegion>
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<series><title level="j">Trends in Biochemical Sciences</title>
<title level="j" type="abbrev">TIBS</title>
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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>
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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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