Trigger factor flexibility

Gamerdinger, Martin; Deuerling, Elke

Trigger factor flexibility

Dateien

Gamerdinger_284743.pdfGröße: 74.58 KBDownloads: 279

Datum

2014

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Science. 2014, 344(6184), pp. 590-591. ISSN 0036-8075. eISSN 1095-9203. Available under: doi: 10.1126/science.1254064

Zusammenfassung

Molecular chaperones are found in all cells and are essential for maintaining a functional proteome. The main function of chaperones is to promote correct protein folding by protecting non-native proteins from folding along pathways that lead to protein misfolding and aggregation. To fulfill this task, chaperones must recognize a non-native protein, transiently bind to it, and then release it at precisely the right time to allow the substrate to proceed with its folding course. Many but not all chaperones use adenosine 5'-triphosphate (ATP) to control the dynamic substrate binding and release cycle (1). On page 597 of this issue, Saio et al. (2) unravel the structural basis and underlying mechanism of action of the ATP-independent chaperone trigger factor (TF).

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

GAMERDINGER, Martin, Elke DEUERLING, 2014. Trigger factor flexibility. In: Science. 2014, 344(6184), pp. 590-591. ISSN 0036-8075. eISSN 1095-9203. Available under: doi: 10.1126/science.1254064

BibTex

@article{Gamerdinger2014-05-09Trigg-28474,
  year={2014},
  doi={10.1126/science.1254064},
  title={Trigger factor flexibility},
  number={6184},
  volume={344},
  issn={0036-8075},
  journal={Science},
  pages={590--591},
  author={Gamerdinger, Martin 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/123456789/28474">
    <dc:creator>Deuerling, Elke</dc:creator>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/28474"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2014-07-21T07:21:47Z</dcterms:available>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dcterms:title>Trigger factor flexibility</dcterms:title>
    <dc:contributor>Deuerling, Elke</dc:contributor>
    <dc:contributor>Gamerdinger, Martin</dc:contributor>
    <dc:rights>terms-of-use</dc:rights>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/28474/2/Gamerdinger_284743.pdf"/>
    <dcterms:bibliographicCitation>Science ; 344 (2014), 6184. - S. 590-591</dcterms:bibliographicCitation>
    <dcterms:issued>2014-05-09</dcterms:issued>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Gamerdinger, Martin</dc:creator>
    <dc:language>eng</dc:language>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/28474/2/Gamerdinger_284743.pdf"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2014-07-21T07:21:47Z</dc:date>
    <dcterms:abstract xml:lang="eng">Molecular chaperones are found in all cells and are essential for maintaining a functional proteome. The main function of chaperones is to promote correct protein folding by protecting non-native proteins from folding along pathways that lead to protein misfolding and aggregation. To fulfill this task, chaperones must recognize a non-native protein, transiently bind to it, and then release it at precisely the right time to allow the substrate to proceed with its folding course. Many but not all chaperones use adenosine 5'-triphosphate (ATP) to control the dynamic substrate binding and release cycle (1). On page 597 of this issue, Saio et al. (2) unravel the structural basis and underlying mechanism of action of the ATP-independent chaperone trigger factor (TF).</dcterms:abstract>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Ja