Linked Life Data

3530497

Source:http://linkedlifedata.com/resource/pubmed/id/3530497

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1986-10-30
pubmed:abstractText
Sensitivity to proteolytic degradation was used to monitor folding of polypeptides in vivo. A correlation between competence for export and lack of stable tertiary structure was established by comparing the kinetics of folding of mutated precursor maltose-binding protein that carries a defective leader peptide with the kinetics of folding of wild-type precursor that is competent for export. It is proposed that during export a kinetic competition exists between productive translocation and folding of precursor intracellularly into a stable conformation that is not compatible with transfer.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
921-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:3530497-ATP-Binding Cassette Transporters, pubmed-meshheading:3530497-Bacterial Proteins, pubmed-meshheading:3530497-Biological Transport, pubmed-meshheading:3530497-Carrier Proteins, pubmed-meshheading:3530497-Cell Compartmentation, pubmed-meshheading:3530497-Endopeptidase K, pubmed-meshheading:3530497-Endopeptidases, pubmed-meshheading:3530497-Escherichia coli, pubmed-meshheading:3530497-Escherichia coli Proteins, pubmed-meshheading:3530497-Kinetics, pubmed-meshheading:3530497-Maltose-Binding Proteins, pubmed-meshheading:3530497-Membrane Proteins, pubmed-meshheading:3530497-Monosaccharide Transport Proteins, pubmed-meshheading:3530497-Protein Conformation, pubmed-meshheading:3530497-Protein Processing, Post-Translational, pubmed-meshheading:3530497-Structure-Activity Relationship
pubmed:year
1986
pubmed:articleTitle
Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't