Publikation: Structure and function of the porin channel
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
DOI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
The outer membrane bilayer of gram-negative bacteria, which encapsulates completely the plasma membrane, seems to act as a protection system against noxious macromolecules like proteases and bile-salt micelles [1]. The external monolayer is composed of lipopolysaccharides with a variable carbohydrate composition. Long oligosaccharide chains protect the cells against recognition by the complement system [2, 3] and hydrophobic substances [4]. The other monolayer facing the periplasmic space is mainly composed of phospholipid.
This protection system should nevertheless allow free access of small biomolecules like mono- and disaccharides, nucleosides, and amino acids to the cytoplasmic membrane. The proteins allowing for rapid diffusion of these molecules across the outer membrane are called porins [5]. The "general diffusion porins" form aqueous channels with an exclusion limit of typically 600 Da and extremes of 5000 Da. Due to their high copy number they form the major integral protein component of the outer membrane and turn it into a molecular sieve. A single cell of E. coli has been estimated to possess approximately 105 OmpF porin molecules [6].
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
WELTE, Wolfram, Uwe NESTEL, Thomas WACKER, Kay DIEDERICHS, 1995. Structure and function of the porin channel. In: Kidney International. 1995, 48(4), pp. 930-940. ISSN 0085-2538. eISSN 1523-1755. Available under: doi: 10.1038/ki.1995.374BibTex
@article{Welte1995Struc-20890, year={1995}, doi={10.1038/ki.1995.374}, title={Structure and function of the porin channel}, number={4}, volume={48}, issn={0085-2538}, journal={Kidney International}, pages={930--940}, author={Welte, Wolfram and Nestel, Uwe and Wacker, Thomas and Diederichs, Kay} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/20890"> <dc:creator>Nestel, Uwe</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-11-20T07:58:33Z</dc:date> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:creator>Welte, Wolfram</dc:creator> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <dcterms:title>Structure and function of the porin channel</dcterms:title> <dcterms:issued>1995</dcterms:issued> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20890/2/Welte_208907.pdf"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dcterms:bibliographicCitation>Kidney International ; 48 (1995), 4. - S. 930-940</dcterms:bibliographicCitation> <dc:language>eng</dc:language> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/20890"/> <dc:rights>terms-of-use</dc:rights> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-11-20T07:58:33Z</dcterms:available> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Nestel, Uwe</dc:contributor> <dcterms:abstract xml:lang="eng">The outer membrane bilayer of gram-negative bacteria, which encapsulates completely the plasma membrane, seems to act as a protection system against noxious macromolecules like proteases and bile-salt micelles [1]. The external monolayer is composed of lipopolysaccharides with a variable carbohydrate composition. Long oligosaccharide chains protect the cells against recognition by the complement system [2, 3] and hydrophobic substances [4]. The other monolayer facing the periplasmic space is mainly composed of phospholipid.<br /><br />This protection system should nevertheless allow free access of small biomolecules like mono- and disaccharides, nucleosides, and amino acids to the cytoplasmic membrane. The proteins allowing for rapid diffusion of these molecules across the outer membrane are called porins [5]. The "general diffusion porins" form aqueous channels with an exclusion limit of typically 600 Da and extremes of 5000 Da. Due to their high copy number they form the major integral protein component of the outer membrane and turn it into a molecular sieve. A single cell of E. coli has been estimated to possess approximately 105 OmpF porin molecules [6].</dcterms:abstract> <dc:contributor>Diederichs, Kay</dc:contributor> <dc:creator>Diederichs, Kay</dc:creator> <dc:contributor>Welte, Wolfram</dc:contributor> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20890/2/Welte_208907.pdf"/> <dc:creator>Wacker, Thomas</dc:creator> <dc:contributor>Wacker, Thomas</dc:contributor> </rdf:Description> </rdf:RDF>