Chaperone-assisted folding of newly synthesized proteins in the cytosol

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DEUERLING, Elke, Bernd BUKAU, 2004. Chaperone-assisted folding of newly synthesized proteins in the cytosol. In: Critical Reviews in Biochemistry and Molecular Biology. 39(5-6), pp. 261-277. ISSN 1040-9238. eISSN 1549-7798

@article{Deuerling2004Chape-7309, title={Chaperone-assisted folding of newly synthesized proteins in the cytosol}, year={2004}, doi={10.1080/10409230490892496}, number={5-6}, volume={39}, issn={1040-9238}, journal={Critical Reviews in Biochemistry and Molecular Biology}, pages={261--277}, author={Deuerling, Elke and Bukau, Bernd} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/7309"> <dc:creator>Bukau, Bernd</dc:creator> <dcterms:issued>2004</dcterms:issued> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dcterms:bibliographicCitation>First publ. in: Critical Reviews in Biochemistry and Molecular Biology 39 (2004), pp. 261 277</dcterms:bibliographicCitation> <dcterms:abstract xml:lang="eng">The way in which a newly synthesized polypeptide chain folds into its unique three-dimensional structure remains one of the fundamental questions in molecular biology. Protein folding in the cell is a problematic process and, in many cases, requires the assistance of a network of molecular chaperones to support productive protein folding in vivo. During protein biosynthesis, ribosome-associated chaperones guide the folding of the nascent polypeptide emerging from the ribosomal tunnel. In this review we summarize the basic principles of the protein-folding process and the involved chaperones, and focus on the role of ribosome-associated chaperones. Our discussion emphasizes the bacterial Trigger Factor, which is the best studied chaperone of this type. Recent advances have determined the atomic structure of the Trigger Factor, providing new, exciting insights into the role of ribosome-associated chaperones in co-translational protein folding.</dcterms:abstract> <dc:contributor>Deuerling, Elke</dc:contributor> <dc:contributor>Bukau, Bernd</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:25Z</dcterms:available> <dc:language>eng</dc:language> <dc:format>application/pdf</dc:format> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:25Z</dc:date> <dcterms:title>Chaperone-assisted folding of newly synthesized proteins in the cytosol</dcterms:title> <dc:creator>Deuerling, Elke</dc:creator> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7309"/> </rdf:Description> </rdf:RDF>

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