Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1988-6-6
pubmed:abstractText
The role of eukaryotic initiation factor (eIF)4B in translation is somewhat uncertain, although it appears to stimulate a variety of activities of eIF-4A and eIF-4F. Using the model RNA-dependent ATP hydrolysis assay, the ability of eIF-4B to stimulate eIF-4A and eIF-4F was investigated. The most dramatic effect of eIF-4B is to increase the affinity of eIF-4A for RNA; no effect is seen on the affinity of eIF-4A for ATP. This is not the case for eIF-4F where stimulation occurs primarily through an increase in Vmax and not a change in the affinity for RNA. The finding that eIF-4A and eIF-4B can bind to an mRNA (lacking in secondary structure), with essentially the same degree of effectiveness and affinity as would occur for natural mRNAs in the presence of eIF-4A, eIF-4B, and eIF-4F, suggests a possible role for eIF-4A and eIF-4B in both cap-independent and internal initiation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6016-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Biochemical evidence supporting a mechanism for cap-independent and internal initiation of eukaryotic mRNA.
pubmed:affiliation
Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.