pubmed-article:20459669 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20459669 | lifeskim:mentions | umls-concept:C0085177 | lld:lifeskim |
pubmed-article:20459669 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
pubmed-article:20459669 | lifeskim:mentions | umls-concept:C1414371 | lld:lifeskim |
pubmed-article:20459669 | lifeskim:mentions | umls-concept:C0035380 | lld:lifeskim |
pubmed-article:20459669 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
pubmed-article:20459669 | lifeskim:mentions | umls-concept:C0121925 | lld:lifeskim |
pubmed-article:20459669 | pubmed:dateCreated | 2010-5-20 | lld:pubmed |
pubmed-article:20459669 | pubmed:abstractText | Lemay et al recently reported that the RNA binding protein HuR directly interacts with the ribonuclease H (RNase H) domain of HIV-1 reverse transcriptase (RT) and influences the efficiency of viral reverse transcription (Lemay et al., 2008, Retrovirology 5:47). HuR is a member of the embryonic lethal abnormal vision protein family and contains 3 RNA recognition motifs (RRMs) that bind AU-rich elements (AREs). To define the structural determinants of the HuR-RT interaction and to elucidate the mechanism(s) by which HuR influences HIV-1 reverse transcription activity in vitro, we cloned and purified full-length HuR as well as three additional protein constructs that contained the N-terminal and internal RRMs, the internal and C-terminal RRMs, or the C-terminal RRM only. | lld:pubmed |
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pubmed-article:20459669 | pubmed:language | eng | lld:pubmed |
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pubmed-article:20459669 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:20459669 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20459669 | pubmed:issn | 1742-4690 | lld:pubmed |
pubmed-article:20459669 | pubmed:author | pubmed-author:Sluis-CremerN... | lld:pubmed |
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pubmed-article:20459669 | pubmed:author | pubmed-author:DharmasenaSan... | lld:pubmed |
pubmed-article:20459669 | pubmed:author | pubmed-author:HuberKellyK | lld:pubmed |
pubmed-article:20459669 | pubmed:author | pubmed-author:ConcelJasonJ | lld:pubmed |
pubmed-article:20459669 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20459669 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:20459669 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20459669 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20459669 | pubmed:pagination | 40 | lld:pubmed |
pubmed-article:20459669 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:20459669 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20459669 | pubmed:articleTitle | The RNA binding protein HuR does not interact directly with HIV-1 reverse transcriptase and does not affect reverse transcription in vitro. | lld:pubmed |
pubmed-article:20459669 | pubmed:affiliation | Department of Structural Biology, Division of Infectious Diseases, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA. jia12@pitt.edu | lld:pubmed |
pubmed-article:20459669 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20459669 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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