Acylation of proteins — a new type of modification of membrane glycoproteins
Identifieur interne : 000436 ( Istex/Corpus ); précédent : 000435; suivant : 000437Acylation of proteins — a new type of modification of membrane glycoproteins
Auteurs : Michael F. G. SchmidtSource :
- 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
Links to Exploration step
ISTEX:B77797923262C40CA68E1981889F6DF97DFD9B9BLe document en format XML
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Schmidt is at the Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, 6300 Giessen, FRG</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:B77797923262C40CA68E1981889F6DF97DFD9B9B</idno><date when="1982" year="1982">1982</date><idno type="doi">10.1016/0968-0004(82)90263-8</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-7X6DVJXP-D/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000436</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000436</idno></publicationStmt><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><mods:affiliation>Michael F. G. Schmidt is at the Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, 6300 Giessen, FRG</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Trends in Biochemical Sciences</title><title level="j" type="abbrev">TIBS</title><idno type="ISSN">0968-0004</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1982">1982</date><biblScope unit="volume">7</biblScope><biblScope unit="issue">9</biblScope><biblScope unit="page" from="322">322</biblScope><biblScope unit="page" to="324">324</biblScope></imprint><idno type="ISSN">0968-0004</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0968-0004</idno></seriesStmt></fileDesc><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></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Fatty acids are covalently attached to many membrane glycoproteins during their biosynthesis.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>glycoprotein</json:string><json:string>acylation</json:string><json:string>acylated</json:string><json:string>fatty acids</json:string><json:string>lipid</json:string><json:string>viral</json:string><json:string>fatty acid</json:string><json:string>viral glycoproteins</json:string><json:string>biol</json:string><json:string>bilayer</json:string><json:string>schmidt</json:string><json:string>acyl chains</json:string><json:string>membrane fusion</json:string><json:string>sindbis virus</json:string><json:string>intracellular transport</json:string><json:string>acylated peptides</json:string><json:string>acylated glycoproteins</json:string><json:string>lipid bilayer</json:string><json:string>natl acad</json:string><json:string>membrane</json:string><json:string>fatty</json:string><json:string>acylation site</json:string><json:string>protein acylation</json:string><json:string>sendai virus</json:string><json:string>fatty acid attachment sites</json:string><json:string>common feature</json:string><json:string>membrane proteins</json:string><json:string>bishr omary</json:string><json:string>hydroxyamino acids</json:string><json:string>cell surface</json:string><json:string>plasma membrane</json:string><json:string>transferrin receptor</json:string><json:string>cellular membrane glycoproteins</json:string><json:string>viral lipid bilayer</json:string></teeft></keywords><author><json:item><name>Michael F.G. 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