Linked Life Data

1864385

Source:http://linkedlifedata.com/resource/pubmed/id/1864385

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1991-9-9
pubmed:abstractText
Synthetic mRNAs were produced using either the complete coding sequence of a human preproendothelin-1 cDNA clone or a truncated form in which the portion encoding the first 17 amino acids, representing a putative signal peptide for insertion into the endoplasmic reticulum, was replaced with a methionine codon. The mRNAs were translated in vitro in the presence or in the absence of microsomal membranes. Protection from trypsin digestion demonstrated that the full-length polypeptide, but not the truncated form, could be inserted into the membranes. Sequence analysis revealed that membrane insertion is accompanied by removal of the first 17 amino acids. These results indicate that the first 17 amino acids of human preproendothelin-1 are a functional signal peptide which allows the protein to enter the secretory pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
286
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
91-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
The signal peptide of human preproendothelin-1.
pubmed:affiliation
Istituto Biosintesi Vegetali, Consiglio Nazionale delle Richerche, Milano, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't