rdf:type |
|
lifeskim:mentions |
umls-concept:C0003451,
umls-concept:C0029341,
umls-concept:C0033684,
umls-concept:C0035150,
umls-concept:C0079925,
umls-concept:C0205195,
umls-concept:C0220781,
umls-concept:C0456387,
umls-concept:C0598629,
umls-concept:C0598829,
umls-concept:C1883254
|
pubmed:issue |
2
|
pubmed:dateCreated |
1990-2-8
|
pubmed:abstractText |
To enhance the penetration of oligonucleotide ('oligo') into cells, the oligo was combined with the hydrophobic undecyl residue. Using the 'DNA-synthesator', we synthesized oligo, complementary to the loop-forming site of the RNA, encoding polymerase 3 of the influenza virus (type A), and combined it with the undecyl residue added to the 5' terminal phosphate group. It was found that the modified oligo effectively suppresses the influenza A/PR8/34 (H1N1) virus reproduction and inhibits the synthesis of virus-specific proteins in MDCK cells. Under the same conditions, the non-modified antisense oligo and modified nonsense oligo did not affect the virus development.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
259
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
327-30
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1688418-Animals,
pubmed-meshheading:1688418-Antiviral Agents,
pubmed-meshheading:1688418-Cell Line,
pubmed-meshheading:1688418-Dogs,
pubmed-meshheading:1688418-Influenza A virus,
pubmed-meshheading:1688418-Kidney,
pubmed-meshheading:1688418-Molecular Weight,
pubmed-meshheading:1688418-Oligoribonucleotides,
pubmed-meshheading:1688418-RNA,
pubmed-meshheading:1688418-RNA, Antisense,
pubmed-meshheading:1688418-RNA, Messenger,
pubmed-meshheading:1688418-Viral Proteins,
pubmed-meshheading:1688418-Virus Replication
|
pubmed:year |
1990
|
pubmed:articleTitle |
A new class of antivirals: antisense oligonucleotides combined with a hydrophobic substituent effectively inhibit influenza virus reproduction and synthesis of virus-specific proteins in MDCK cells.
|
pubmed:affiliation |
Research Center of Molecular Diagnostics, USSR Ministry of Health, Moscow.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|