Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1991-12-26
pubmed:abstractText
A cellular 57-kDa protein (p57) that binds specifically to the internal translation initiation site in the 5' untranslated region of foot-and-mouth disease virus RNA was detected in cell extracts of different mammalian species by UV cross-linking. The protein binds to two distinct sites of the translation control region which have as the only common sequence a UUUC motif. The first binding site consists of a conserved hairpin structure, whereas the second binding site contains an essential pyrimidine-rich region without obvious secondary structure. Competition experiments indicate that the complexes with the two binding sites were formed by a single p57 species. The protein binds also to the 5' untranslated region of other picornaviruses. Results from footprint analyses with foot-and-mouth disease RNA suggest the participation of additional cellular factors in the translation initiation complex.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2077688, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2153239, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2155820, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2157900, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2165605, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2168956, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2169432, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2174810, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2303031, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2450348, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2533575, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2538648, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2548167, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2550319, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2554308, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2725581, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2838971, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2839690, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2839775, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-3010307, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-3033601, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-3837842, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-4604997, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-6089122, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-6091052, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-627214, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-6323749, http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-7388032
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6486-94
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:1658355-Animals, pubmed-meshheading:1658355-Aphthovirus, pubmed-meshheading:1658355-Base Sequence, pubmed-meshheading:1658355-Binding, Competitive, pubmed-meshheading:1658355-Binding Sites, pubmed-meshheading:1658355-Cell Line, pubmed-meshheading:1658355-Cross-Linking Reagents, pubmed-meshheading:1658355-HeLa Cells, pubmed-meshheading:1658355-Humans, pubmed-meshheading:1658355-Kinetics, pubmed-meshheading:1658355-Liver, pubmed-meshheading:1658355-Models, Structural, pubmed-meshheading:1658355-Molecular Sequence Data, pubmed-meshheading:1658355-Molecular Weight, pubmed-meshheading:1658355-Nucleic Acid Conformation, pubmed-meshheading:1658355-Peptide Chain Initiation, Translational, pubmed-meshheading:1658355-Picornaviridae, pubmed-meshheading:1658355-Plasmids, pubmed-meshheading:1658355-Poliovirus, pubmed-meshheading:1658355-RNA, Viral, pubmed-meshheading:1658355-RNA-Binding Proteins, pubmed-meshheading:1658355-Rabbits, pubmed-meshheading:1658355-Rats, pubmed-meshheading:1658355-Restriction Mapping, pubmed-meshheading:1658355-Reticulocytes, pubmed-meshheading:1658355-Transcription, Genetic, pubmed-meshheading:1658355-Ultraviolet Rays
pubmed:year
1991
pubmed:articleTitle
Interaction of a cellular 57-kilodalton protein with the internal translation initiation site of foot-and-mouth disease virus.
pubmed:affiliation
Zentrum für Molekulare Biologie Heidelberg, University of Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't