Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-12-7
pubmed:abstractText
We have shown that a family of high-molecular-mass proteins can be detected in lysates of parasitized erythrocytes using antibodies specific for a Plasmodium yoelii rhoptry protein. When these polypeptides are biosynthetically labeled in the presence of brefeldin A or at 15 degrees C, their electrophoretic mobility on polyacrylamide gels is decreased. Removal of the drug restores the size of the polypeptides to that in the absence of the drug. These results indicate that the proteins undergo a processing event, most probably a proteolytic cleavage, which is inhibited by brefeldin A and low temperature. The data suggest that the proteins are moved by secretory transport from the endoplasmic reticulum through a functional Golgi to the rhoptry organelles.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-4894
pubmed:author
pubmed:issnType
Print
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
270-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Plasmodium yoelii: brefeldin A-sensitive processing of proteins targeted to the rhoptries.
pubmed:affiliation
Division of Parasitology, National Institute for Medical Research, Mill Hill, London, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't