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dc.contributor.authorHeras, Begona
dc.contributor.authorShouldice, Stephen R
dc.contributor.authorTotsika, Makrina
dc.contributor.authorScanlon, Martin J
dc.contributor.authorSchembri, Mark A
dc.contributor.authorMartin, Jennifer L
dc.date.accessioned2017-09-22T03:48:52Z
dc.date.available2017-09-22T03:48:52Z
dc.date.issued2009
dc.identifier.issn1740-1526
dc.identifier.doi10.1038/nrmicro2087
dc.identifier.urihttp://hdl.handle.net/10072/347146
dc.description.abstractIf DNA is the information of life, then proteins are the machines of life — but they must be assembled and correctly folded to function. A key step in the protein-folding pathway is the introduction of disulphide bonds between cysteine residues in a process called oxidative protein folding. Many bacteria use an oxidative protein-folding machinery to assemble proteins that are essential for cell integrity and to produce virulence factors. Although our current knowledge of this machinery stems largely from Escherichia coli K-12, this view must now be adjusted to encompass the wider range of disulphide catalytic systems present in bacteria.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofpagefrom215
dc.relation.ispartofpageto225
dc.relation.ispartofissue3
dc.relation.ispartofjournalNature Reviews Microbiology
dc.relation.ispartofvolume7
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchMicrobiology not elsewhere classified
dc.subject.fieldofresearchMedical microbiology
dc.subject.fieldofresearchcode3107
dc.subject.fieldofresearchcode310799
dc.subject.fieldofresearchcode3207
dc.titleDSB proteins and bacterial pathogenicity
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorMartin, Jennifer


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