| pubmed-article:17259217 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17259217 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
| pubmed-article:17259217 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:17259217 | lifeskim:mentions | umls-concept:C0733755 | lld:lifeskim |
| pubmed-article:17259217 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:17259217 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:17259217 | pubmed:dateCreated | 2007-3-29 | lld:pubmed |
| pubmed-article:17259217 | pubmed:abstractText | Many eukaryotic and viral mRNAs, in which the first transcribed nucleotide is an adenosine, are decorated with a cap-1 structure, (7Me)G5'-ppp5'-A(2'OMe). The positive-sense RNA genomes of flaviviruses (Dengue, West Nile virus) for example show strict conservation of the adenosine. We set out to produce GpppA- and (7Me)GpppA-capped RNA oligonucleotides for non-radioactive mRNA cap methyltransferase assays and, in perspective, for studies of enzyme specificity in relation to substrate length as well as for co-crystallization studies. This study reports the use of a bacteriophage T7 DNA primase fragment to synthesize GpppAC(n) and (7Me)GpppAC(n) (1 < or = n < or = 9) in a one-step enzymatic reaction, followed by direct on-line cleaning HPLC purification. Optimization studies show that yields could be modulated by DNA template, enzyme and substrate concentration adjustments and longer reaction times. Large-scale synthesis rendered pure (in average 99%) products (1 < or = n < or = 7) in quantities of up to 100 nmol starting from 200 nmol cap analog. The capped RNA oligonucleotides were efficient substrates of Dengue virus (nucleoside-2'-O-)-methyltransferase, and human (guanine-N7)-methyltransferase. Methyltransfer reactions were monitored by a non-radioactive, quantitative HPLC assay. Additionally, the produced capped RNAs may serve in biochemical, inhibition and structural studies involving a variety of eukaryotic and viral methyltransferases and guanylyltransferases. | lld:pubmed |
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| pubmed-article:17259217 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259217 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259217 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17259217 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259217 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17259217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17259217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17259217 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17259217 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:17259217 | pubmed:author | pubmed-author:VasseurJ JJJ | lld:pubmed |
| pubmed-article:17259217 | pubmed:author | pubmed-author:CanardBB | lld:pubmed |
| pubmed-article:17259217 | pubmed:author | pubmed-author:DecrolyEE | lld:pubmed |
| pubmed-article:17259217 | pubmed:author | pubmed-author:SeliskoBB | lld:pubmed |
| pubmed-article:17259217 | pubmed:author | pubmed-author:AlvaresPP | lld:pubmed |
| pubmed-article:17259217 | pubmed:author | pubmed-author:PeyraneFF | lld:pubmed |
| pubmed-article:17259217 | pubmed:author | pubmed-author:BenarrochDD | lld:pubmed |
| pubmed-article:17259217 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17259217 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:17259217 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17259217 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17259217 | pubmed:pagination | e26 | lld:pubmed |
| pubmed-article:17259217 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17259217 | pubmed:meshHeading | pubmed-meshheading:17259217... | lld:pubmed |
| pubmed-article:17259217 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17259217 | pubmed:articleTitle | High-yield production of short GpppA- and 7MeGpppA-capped RNAs and HPLC-monitoring of methyltransfer reactions at the guanine-N7 and adenosine-2'O positions. | lld:pubmed |
| pubmed-article:17259217 | pubmed:affiliation | Centre National de la Recherche Scientifique and Universités d'Aix-Marseille I et II, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, AFMB-CNRS-ESIL, Case 925, 163 avenue de Luminy, 13288 Marseille Cedex 9, France. | lld:pubmed |
| pubmed-article:17259217 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17259217 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1494449 | entrezgene:pubmed | pubmed-article:17259217 | lld:entrezgene |
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