Linked Life Data

15667282

Source:http://linkedlifedata.com/resource/pubmed/id/15667282

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2005-1-25
pubmed:abstractText
Controlled targeting and transport of redox enzymes to and across the bacterial cytoplasmic membrane is essential for bacterial respiration. A subset of bacterial redox enzymes is exported as folded proteins on the Tat (twin-arginine transport) pathway. Protein export is the point-of-no-return for passenger proteins on the Tat pathway and it is crucial that complex, cofactor-containing enzymes are fully assembled before export is attempted. Using the Escherichia coli trimethylamine N-oxide reductase system as a model, we discuss here the molecular processes governing assembly and export of Tat-dependent enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0300-5127
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
124-6
pubmed:dateRevised
2008-7-11
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Chaperones involved in assembly and export of N-oxide reductases.
pubmed:affiliation
School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, England, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't