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dc.contributor.authorGasser, Brigitte
dc.contributor.authorSaloheimo, Markku
dc.contributor.authorRinas, Ursula
dc.contributor.authorDragosits, Martin
dc.contributor.authorRodríguez-Carmona, Escarlata
dc.contributor.authorBaumann, Kristin
dc.contributor.authorGiuliani, Maria
dc.contributor.authorParrilli, Ermenegilda
dc.contributor.authorBranduardi, Paola
dc.contributor.authorLang, Christine
dc.contributor.authorPorro, Danilo
dc.contributor.authorFerrer, Pau
dc.contributor.authorTutino, Maria Luisa
dc.contributor.authorMattanovich, Diethard
dc.contributor.authorVillaverde, Antonio
dc.date.accessioned2009-01-19T15:22:12Z
dc.date.available2009-01-19T15:22:12Z
dc.date.issued2008
dc.identifier.citationProtein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview. 2008, 7:11 Microb. Cell Fact.en
dc.identifier.issn1475-2859
dc.identifier.pmid18394160
dc.identifier.doi10.1186/1475-2859-7-11
dc.identifier.urihttp://hdl.handle.net/10033/47714
dc.description.abstractABSTRACT: Different species of microorganisms including yeasts, filamentous fungi and bacteria have been used in the past 25 years for the controlled production of foreign proteins of scientific, pharmacological or industrial interest. A major obstacle for protein production processes and a limit to overall success has been the abundance of misfolded polypeptides, which fail to reach their native conformation. The presence of misfolded or folding-reluctant protein species causes considerable stress in host cells. The characterization of such adverse conditions and the elicited cell responses have permitted to better understand the physiology and molecular biology of conformational stress. Therefore, microbial cell factories for recombinant protein production are depicted here as a source of knowledge that has considerably helped to picture the extremely rich landscape of in vivo protein folding, and the main cellular players of this complex process are described for the most important cell factories used for biotechnological purposes.
dc.language.isoenen
dc.relation.urlhttp://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=18394160en
dc.titleProtein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview.en
dc.typeArticleen
dc.contributor.departmentUniversity of Natural Resources and Applied Life Sciences Vienna, Department of Biotechnology, Vienna, Austria. diethard.mattanovich@boku.ac.at.en
dc.identifier.journalMicrobial cell factoriesen
refterms.dateFOA2018-06-13T03:57:14Z
html.description.abstractABSTRACT: Different species of microorganisms including yeasts, filamentous fungi and bacteria have been used in the past 25 years for the controlled production of foreign proteins of scientific, pharmacological or industrial interest. A major obstacle for protein production processes and a limit to overall success has been the abundance of misfolded polypeptides, which fail to reach their native conformation. The presence of misfolded or folding-reluctant protein species causes considerable stress in host cells. The characterization of such adverse conditions and the elicited cell responses have permitted to better understand the physiology and molecular biology of conformational stress. Therefore, microbial cell factories for recombinant protein production are depicted here as a source of knowledge that has considerably helped to picture the extremely rich landscape of in vivo protein folding, and the main cellular players of this complex process are described for the most important cell factories used for biotechnological purposes.


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