<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>10(2)</volume><submitter>Magbanua E</submitter><pubmed_abstract>Aptamers are oligonucleotides that bind targets with high specificity and affinity. They have become important tools for biosensing, target detection, drug delivery and therapy. We selected the quadruplex-forming 16-mer DNA aptamer AID-1 [d(GGGT) 4] with affinity for the interleukin-6 receptor (IL-6R) and identified single nucleotide variants that showed no significant loss of binding ability. The RNA counterpart of AID-1 [r(GGGU) 4] also bound IL-6R as quadruplex structure. AID-1 is identical to the well-known HIV inhibitor T30923, which inhibits both HIV infection and HIV-1 integrase. We also demonstrated that IL-6R specific RNA aptamers not only bind HIV-1 integrase and inhibit its 3' processing activity in vitro, but also are capable of preventing HIV de novo infection with the same ef</pubmed_abstract><journal>RNA biology</journal><pagination>216-27</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3594281</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>d(GGGT) 4 and r(GGGU) 4 are both HIV-1 inhibitors and interleukin-6 receptor aptamers.</pubmed_title><pmcid>PMC3594281</pmcid><pubmed_authors>Meyer C</pubmed_authors><pubmed_authors>Hahn U</pubmed_authors><pubmed_authors>Hauber J</pubmed_authors><pubmed_authors>Hansen B</pubmed_authors><pubmed_authors>Lorenzen I</pubmed_authors><pubmed_authors>Magbanua E</pubmed_authors><pubmed_authors>Rose-John S</pubmed_authors><pubmed_authors>Mayer G</pubmed_authors><pubmed_authors>Zivkovic T</pubmed_authors><pubmed_authors>Grotzinger J</pubmed_authors><pubmed_authors>Torda AE</pubmed_authors><pubmed_authors>Beschorner N</pubmed_authors></additional><is_claimable>false</is_claimable><name>d(GGGT) 4 and r(GGGU) 4 are both HIV-1 inhibitors and interleukin-6 receptor aptamers.</name><description>Aptamers are oligonucleotides that bind targets with high specificity and affinity. They have become important tools for biosensing, target detection, drug delivery and therapy. We selected the quadruplex-forming 16-mer DNA aptamer AID-1 [d(GGGT) 4] with affinity for the interleukin-6 receptor (IL-6R) and identified single nucleotide variants that showed no significant loss of binding ability. The RNA counterpart of AID-1 [r(GGGU) 4] also bound IL-6R as quadruplex structure. AID-1 is identical to the well-known HIV inhibitor T30923, which inhibits both HIV infection and HIV-1 integrase. We also demonstrated that IL-6R specific RNA aptamers not only bind HIV-1 integrase and inhibit its 3' processing activity in vitro, but also are capable of preventing HIV de novo infection with the same ef</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Feb</publication><modification>2026-04-30T23:32:51.969Z</modification><creation>2019-03-27T01:05:55Z</creation></dates><accession>S-EPMC3594281</accession><cross_references><pubmed>23235494</pubmed><doi>10.4161/rna.22951</doi></cross_references></HashMap>