About: Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli
Creator	De Marco, Ario
Source	Medline; PMC
abstract	Bacteria are simple and cost effective hosts for producing recombinant proteins. However, their physiological features may limit their use for obtaining in native form proteins of some specific structural classes, such as for instance polypeptides that undergo extensive post-translational modifications. To some extent, also the production of proteins that depending on disulfide bridges for their stability has been considered difficult in E. coli. Both eukaryotic and prokaryotic organisms keep their cytoplasm reduced and, consequently, disulfide bond formation is impaired in this subcellular compartment. Disulfide bridges can stabilize protein structure and are often present in high abundance in secreted proteins. In eukaryotic cells such bonds are formed in the oxidizing environment of endoplasmic reticulum during the export process. Bacteria do not possess a similar specialized subcellular compartment, but they have both export systems and enzymatic activities aimed at the formation and at the quality control of disulfide bonds in the oxidizing periplasm. This article reviews the available strategies for exploiting the physiological mechanisms of bactera to produce properly folded disulfide-bonded proteins.
has issue date	2009-05-14(xsd:dateTime)
bibo:doi	10.1186/1475-2859-8-26
bibo:pmid	19442264
has license	cc-by
sha1sum (hex)	7c0a15a70be63f9707358fb640e01b464e54dfd0
schema:url	https://doi.org/10.1186/1475-2859-8-26
resource representing a document's title	Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli
has PubMed Central identifier	PMC2689190
has PubMed identifier	19442264
schema:publication	Microb Cell Fact
resource representing a document's body	covid:7c0a15a70be63f9707358fb640e01b464e54dfd0#body_text
is schema:about of	named entity 'CELL' named entity 'recombinant proteins' named entity 'Escherichia coli' named entity 'DISULFIDE BOND' named entity 'ESCHERICHIA COLI' named entity 'MICROBIAL' named entity 'CLASSES' named entity 'LIMIT' named entity 'PRODUCTION' named entity 'STABILITY' named entity 'THEIR' named entity 'BRIDGES' named entity 'TO SOME EXTENT' named entity 'INSTANCE' named entity 'POLYPEPTIDES' named entity 'FEATURES' named entity 'CONSIDERED' named entity 'PHYSIOLOGICAL' named entity 'BACTERIA ' named entity 'USE' named entity 'COST' named entity 'DIFFICULT' named entity 'DISULFIDE' named entity 'FACTORIES' named entity 'SUCCESSFUL' named entity 'DEPENDENT' named entity 'PROTEINS' named entity 'STRATEGIES' named entity 'E. COLI' named entity 'POST-TRANSLATIONAL MODIFICATIONS' named entity 'EFFECTIVE' named entity 'EXTENSIVE' named entity 'SIMPLE' named entity 'SPECIFIC' named entity 'RECOMBINANT EXPRESSION' named entity 'PRODUCING' named entity 'HOSTS' named entity 'NATIVE FORM' named entity 'STRUCTURAL' named entity 'RECOMBINANT PROTEINS' named entity 'PROTEINS' named entity 'specific' named entity 'physiological' named entity 'structural' named entity 'post-translational modifications' named entity 'polypeptides' named entity 'recombinant' named entity 'stress response' named entity 'signal sequences' named entity 'isomerase' named entity 'tandem repeats' named entity 'culture medium' named entity 'L-arginine' named entity 'N-terminal signal peptide' named entity 'oxidized' named entity 'active site' named entity 'protein' named entity 'MMP-2' named entity 'antibody' named entity 'polypeptides' named entity 'cytoplasm' named entity 'thioredoxin' named entity 'DsbB' named entity 'molecular chaperones' named entity 'disulfide bonds' named entity 'scFvs' named entity 'oxidation' named entity 'antibody' named entity 'cleavage' named entity 'Sumo' named entity 'molecular evolution' named entity 'secreted proteins' named entity 'chaperone' named entity 'inducer' named entity 'periplasm' named entity 'recombinant antibodies' named entity 'target protein' named entity 'proinsulin' named entity 'hydrophobic interactions' named entity 'cytolysin' named entity 'denatured'

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