Identification of Proteins Interacting with Ubiquitin Chains

Lade...
Vorschaubild
Dateien
Zu diesem Dokument gibt es keine Dateien.
Datum
2017
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Angewandte Chemie International Edition. 2017, 56(49), pp. 15764-15768. ISSN 1433-7851. eISSN 1521-3773. Available under: doi: 10.1002/anie.201705898
Zusammenfassung

Ubiquitylation, the modification of proteins with ubiquitin (Ub), is one of the most versatile post-translational modifications in eukaryotic cells. Since Ub also serves as its own substrate, proteins can be modified by numerous different Ub chains, in which the individual moieties are linked via one or several of the seven lysines of Ub. Homogeneous Ub chains, in which the moieties are sequentially linked via the same residue, have been most extensively studied. However, due to their restricted availability, the functions of Ub chains linked via K27, K29, or K33 are poorly understood. We have developed an approach that, for the first time, allows the generation of all seven homogeneous Ub chains in large quantities. The potential of our approach is demonstrated by the identification of previously unknown interaction partners of K27-, K29-, and K33-linked Ub chains by affinity-based proteomics.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
540 Chemie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690ZHAO, Xiaohui, Joachim LUTZ, Eva HÖLLMÜLLER, Martin SCHEFFNER, Andreas MARX, Florian STENGEL, 2017. Identification of Proteins Interacting with Ubiquitin Chains. In: Angewandte Chemie International Edition. 2017, 56(49), pp. 15764-15768. ISSN 1433-7851. eISSN 1521-3773. Available under: doi: 10.1002/anie.201705898
BibTex
@article{Zhao2017-12-04Ident-40972,
  year={2017},
  doi={10.1002/anie.201705898},
  title={Identification of Proteins Interacting with Ubiquitin Chains},
  number={49},
  volume={56},
  issn={1433-7851},
  journal={Angewandte Chemie International Edition},
  pages={15764--15768},
  author={Zhao, Xiaohui and Lutz, Joachim and Höllmüller, Eva and Scheffner, Martin and Marx, Andreas and Stengel, Florian}
}
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/123456789/40972">
    <dcterms:abstract xml:lang="eng">Ubiquitylation, the modification of proteins with ubiquitin (Ub), is one of the most versatile post-translational modifications in eukaryotic cells. Since Ub also serves as its own substrate, proteins can be modified by numerous different Ub chains, in which the individual moieties are linked via one or several of the seven lysines of Ub. Homogeneous Ub chains, in which the moieties are sequentially linked via the same residue, have been most extensively studied. However, due to their restricted availability, the functions of Ub chains linked via K27, K29, or K33 are poorly understood. We have developed an approach that, for the first time, allows the generation of all seven homogeneous Ub chains in large quantities. The potential of our approach is demonstrated by the identification of previously unknown interaction partners of K27-, K29-, and K33-linked Ub chains by affinity-based proteomics.</dcterms:abstract>
    <dc:contributor>Zhao, Xiaohui</dc:contributor>
    <dc:language>eng</dc:language>
    <dc:creator>Zhao, Xiaohui</dc:creator>
    <dc:contributor>Lutz, Joachim</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Scheffner, Martin</dc:creator>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/40972"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-12-20T07:33:17Z</dc:date>
    <dc:rights>terms-of-use</dc:rights>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/40972/1/Zhao_2-1s3q0thmu7ow86.pdf"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:issued>2017-12-04</dcterms:issued>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/40972/1/Zhao_2-1s3q0thmu7ow86.pdf"/>
    <dc:contributor>Stengel, Florian</dc:contributor>
    <dcterms:title>Identification of Proteins Interacting with Ubiquitin Chains</dcterms:title>
    <dc:contributor>Höllmüller, Eva</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:contributor>Scheffner, Martin</dc:contributor>
    <dc:creator>Höllmüller, Eva</dc:creator>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:contributor>Marx, Andreas</dc:contributor>
    <dc:creator>Stengel, Florian</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Lutz, Joachim</dc:creator>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-12-20T07:33:17Z</dcterms:available>
    <dc:creator>Marx, Andreas</dc:creator>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Ja
Diese Publikation teilen