Linked Life Data

616704

Source:http://linkedlifedata.com/resource/pubmed/id/616704

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11-12
pubmed:dateCreated
1978-12-2
pubmed:abstractText
A variety of proteins, including viral precursor polypeptides, were bound to a solid support and used in a sensitive assay for proteolytic enzymes in HeLa cells. A trypsin-like endoprotease, present on ribosomes of HeLa cells, loses activity after picornavirus infection. The decline follows synthesis and processing of a viral protein. Inhibition of cellfree activity of HeLa protease occurs when protein trypsin inhibitors or double-stranded RNA are added. After the mid-point of infection, protease activity with enhanced specificity for viral substrates is detected. The new protease has a pH optimum and heat stability different from endogenous host enzymes, and is synthesized following infection. A viral mutant was isolated which produces a temperature-sensitive protease. The results indicate that a poliovirus gene product participates enzymatically in the final cleavages of some polioviral proteins. A model for the regulation of poliovirus replication based on specific proteolysis is presented.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-5318
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1565-73
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Protein cleavage in virus-infected cells.
pubmed:publicationType
Journal Article