Publikation:

Ribosome-associated chaperones as key players in proteostasis

Vorschaubild

Dateien

Deuerling_213999.pdf
Deuerling_213999.pdfGröße: 926.59 KBDownloads: 913

Datum

2012

Autor:innen

Preissler, Steffen

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

URI (zitierfähiger Link)
http://nbn-resolving.de/urn:nbn:de:bsz:352-213999
DOI (zitierfähiger Link)
https://doi.org/10.1016/j.tibs.2012.03.002
ArXiv-ID

Internationale Patentnummer

Link zur Lizenz
Urheberrechtlich geschützt

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green

Sammlungen

Biologie: Publikationen
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Trends in Biochemical Sciences. 2012, 37(7), pp. 274-283. ISSN 0968-0004. eISSN 1362-4326. Available under: doi: 10.1016/j.tibs.2012.03.002

Zusammenfassung

De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperones. Besides cytosolic and organelle-specific chaperones, cells have evolved ribosome-associated chaperones that support early folding events and prevent misfolding and aggregation. This class of chaperones includes the bacterial trigger factor (TF), the archaeal and eukaryotic nascent polypeptide-associated complex (NAC) and specialized eukaryotic heat shock protein (Hsp) 70/40 chaperones. This review focuses on the cellular activities of ribosome-associated chaperones and highlights new findings indicating additional functions beyond de novo folding. These activities include the assembly of oligomeric complexes, such as ribosomes, modulation of translation and targeting of proteins.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690PREISSLER, Steffen, Elke DEUERLING, 2012. Ribosome-associated chaperones as key players in proteostasis. In: Trends in Biochemical Sciences. 2012, 37(7), pp. 274-283. ISSN 0968-0004. eISSN 1362-4326. Available under: doi: 10.1016/j.tibs.2012.03.002
BibTex
@article{Preissler2012-07Ribos-21399,
  year={2012},
  doi={10.1016/j.tibs.2012.03.002},
  title={Ribosome-associated chaperones as key players in proteostasis},
  number={7},
  volume={37},
  issn={0968-0004},
  journal={Trends in Biochemical Sciences},
  pages={274--283},
  author={Preissler, Steffen and Deuerling, Elke}
}
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/123456789/21399">
    <dcterms:abstract xml:lang="eng">De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperones. Besides cytosolic and organelle-specific chaperones, cells have evolved ribosome-associated chaperones that support early folding events and prevent misfolding and aggregation. This class of chaperones includes the bacterial trigger factor (TF), the archaeal and eukaryotic nascent polypeptide-associated complex (NAC) and specialized eukaryotic heat shock protein (Hsp) 70/40 chaperones. This review focuses on the cellular activities of ribosome-associated chaperones and highlights new findings indicating additional functions beyond de novo folding. These activities include the assembly of oligomeric complexes, such as ribosomes, modulation of translation and targeting of proteins.</dcterms:abstract>
    <dc:language>eng</dc:language>
    <dc:contributor>Deuerling, Elke</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/21399/2/Deuerling_213999.pdf"/>
    <dcterms:title>Ribosome-associated chaperones as key players in proteostasis</dcterms:title>
    <dc:contributor>Preissler, Steffen</dc:contributor>
    <dc:creator>Deuerling, Elke</dc:creator>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-02-05T10:13:25Z</dc:date>
    <dcterms:issued>2012-07</dcterms:issued>
    <dcterms:bibliographicCitation>Trends in Biochemical Sciences ; 37 (2012), 7. - S. 274-283</dcterms:bibliographicCitation>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/21399/2/Deuerling_213999.pdf"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/21399"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Preissler, Steffen</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-02-05T10:13:25Z</dcterms:available>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:rights>terms-of-use</dc:rights>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
  </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
Diese Publikation teilen