rdf:type |
|
lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1991-12-26
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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.
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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,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1658355-2839775,
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
0022-538X
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
65
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6486-94
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pubmed:dateRevised |
2009-11-18
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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
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pubmed:year |
1991
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pubmed:articleTitle |
Interaction of a cellular 57-kilodalton protein with the internal translation initiation site of foot-and-mouth disease virus.
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pubmed:affiliation |
Zentrum für Molekulare Biologie Heidelberg, University of Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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