(s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase
Identifieur interne : 000486 ( Istex/Corpus ); précédent : 000485; suivant : 000487(s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase
Auteurs : Szilvia Tökés ; Janos AradiSource :
- FEBS Letters [ 0014-5793 ] ; 1996.
English descriptors
- Teeft :
- Agents chemother, Alkaline phosphatase, Chain length, Chemical modification, Competitive inhibitors, Data points, Dixon plot, Free enzyme, Hplc analysis, Human immunodeficiency virus type, Inhibitor, Inhibitory, Inhibitory activity, Large number, Minute amount, Nucleic acids, Oligonucleotides, Potent inhibitors, Protein synthesis, Transcriptase, Unmodified base, Variable substrate.
Abstract
Abstract: Oligodeoxycytidylates were converted to s4dUMP-containing oligomers by treatment with liquid H2S. The inhibitory potency of the modified oligonucleotides on human immunodeficiency virus type 1 reverse transcriptase depended on the chain length and on the percentage of modification. The most potent reverse transcriptase inhibitor was (s4dU)35. The inhibitory pattern was competitive, when either poly(A)·(dT)16 or poly(C)·(dG)16 was used as template-primer (variable substrate), suggesting that the free enzyme interacts with (s4dU)35. The Ki values were 3.0 and 2.2 nM in the presence of poly(A)·(dT)16 and poly(C)·(dG)16, respectively.
Url:
DOI: 10.1016/0014-5793(96)01032-0
Links to Exploration step
ISTEX:58C8655DA75EEF980B9EF728BD3FF618BA65B321Le document en format XML
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Box 6, H-4012 Debrecen, Hungary</mods:affiliation></affiliation></author><author><name sortKey="Aradi, Janos" sort="Aradi, Janos" uniqKey="Aradi J" first="Janos" last="Aradi">Janos Aradi</name><affiliation><mods:affiliation>Department of Biochemistry, University Medical School of Debrecen, P.O. Box 6, H-4012 Debrecen, Hungary</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">FEBS Letters</title><title level="j" type="abbrev">FEBS</title><idno type="ISSN">0014-5793</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">396</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="43">43</biblScope><biblScope unit="page" to="46">46</biblScope></imprint><idno type="ISSN">0014-5793</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0014-5793</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Agents chemother</term><term>Alkaline phosphatase</term><term>Chain length</term><term>Chemical modification</term><term>Competitive inhibitors</term><term>Data points</term><term>Dixon plot</term><term>Free enzyme</term><term>Hplc analysis</term><term>Human immunodeficiency virus type</term><term>Inhibitor</term><term>Inhibitory</term><term>Inhibitory activity</term><term>Large number</term><term>Minute amount</term><term>Nucleic acids</term><term>Oligonucleotides</term><term>Potent inhibitors</term><term>Protein synthesis</term><term>Transcriptase</term><term>Unmodified base</term><term>Variable substrate</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Oligodeoxycytidylates were converted to s4dUMP-containing oligomers by treatment with liquid H2S. The inhibitory potency of the modified oligonucleotides on human immunodeficiency virus type 1 reverse transcriptase depended on the chain length and on the percentage of modification. The most potent reverse transcriptase inhibitor was (s4dU)35. The inhibitory pattern was competitive, when either poly(A)·(dT)16 or poly(C)·(dG)16 was used as template-primer (variable substrate), suggesting that the free enzyme interacts with (s4dU)35. The Ki values were 3.0 and 2.2 nM in the presence of poly(A)·(dT)16 and poly(C)·(dG)16, respectively.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>oligonucleotides</json:string><json:string>transcriptase</json:string><json:string>inhibitory activity</json:string><json:string>chain length</json:string><json:string>inhibitor</json:string><json:string>inhibitory</json:string><json:string>nucleic acids</json:string><json:string>chemical modification</json:string><json:string>potent inhibitors</json:string><json:string>agents chemother</json:string><json:string>competitive inhibitors</json:string><json:string>large number</json:string><json:string>alkaline phosphatase</json:string><json:string>variable substrate</json:string><json:string>data points</json:string><json:string>free enzyme</json:string><json:string>human immunodeficiency virus type</json:string><json:string>minute amount</json:string><json:string>unmodified base</json:string><json:string>protein synthesis</json:string><json:string>dixon plot</json:string><json:string>hplc analysis</json:string></teeft></keywords><author><json:item><name>Szilvia Tökés</name><affiliations><json:string>Department of Biochemistry, University Medical School of Debrecen, P.O. Box 6, H-4012 Debrecen, Hungary</json:string></affiliations></json:item><json:item><name>Janos Aradi</name><affiliations><json:string>Department of Biochemistry, University Medical School of Debrecen, P.O. Box 6, H-4012 Debrecen, Hungary</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Inhibition</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Reverse transcriptase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Human immunodeficiency virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Oligo 4-thio-2′-deoxyuridylate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Antitemplate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>RT, reverse transcriptase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HIV, human immunodeficiency virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>AIDS, acquired immunodeficiency syndrome</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>TCA, trichloroacetic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Na-PPi, Na-pyrophosphate</value></json:item></subject><arkIstex>ark:/67375/6H6-GLMLCDV6-Z</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Oligodeoxycytidylates were converted to s4dUMP-containing oligomers by treatment with liquid H2S. The inhibitory potency of the modified oligonucleotides on human immunodeficiency virus type 1 reverse transcriptase depended on the chain length and on the percentage of modification. The most potent reverse transcriptase inhibitor was (s4dU)35. The inhibitory pattern was competitive, when either poly(A)·(dT)16 or poly(C)·(dG)16 was used as template-primer (variable substrate), suggesting that the free enzyme interacts with (s4dU)35. The Ki values were 3.0 and 2.2 nM in the presence of poly(A)·(dT)16 and poly(C)·(dG)16, respectively.</abstract><qualityIndicators><score>5.502</score><pdfWordCount>2470</pdfWordCount><pdfCharCount>15635</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>4</pdfPageCount><pdfPageSize>576 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>86</abstractWordCount><abstractCharCount>648</abstractCharCount><keywordCount>10</keywordCount></qualityIndicators><title>(s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase</title><pmid><json:string>8906863</json:string></pmid><pii><json:string>0014-5793(96)01032-0</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>FEBS Letters</title><language><json:string>unknown</json:string></language><publicationDate>1996</publicationDate><issn><json:string>0014-5793</json:string></issn><pii><json:string>S0014-5793(00)X0097-X</json:string></pii><volume>396</volume><issue>1</issue><pages><first>43</first><last>46</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1996</json:string></date><geogName></geogName><orgName><json:string>Hungarian Academy of Sciences</json:string><json:string>University of Buffalo</json:string><json:string>Hungary Received</json:string><json:string>OTKA T</json:string></orgName><orgName_funder><json:string>OTKA T</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>P.O. Box</json:string><json:string>J. Aradi</json:string><json:string>J.E. MacDiarmid</json:string><json:string>S. TdkOs</json:string></persName><placeName><json:string>Germany</json:string><json:string>Hungary</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[7-9]</json:string><json:string>[12,15]</json:string><json:string>[23]</json:string><json:string>[11,13,15]</json:string><json:string>[6]</json:string><json:string>[22]</json:string><json:string>[17]</json:string><json:string>[25,26]</json:string><json:string>[1]</json:string><json:string>[21]</json:string><json:string>[11-13,15]</json:string><json:string>[18,19]</json:string><json:string>[26]</json:string><json:string>[7]</json:string><json:string>[25]</json:string><json:string>[2-5]</json:string><json:string>[12-15]</json:string><json:string>[24]</json:string><json:string>[27,28]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-GLMLCDV6-Z</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - cell biology</json:string><json:string>2 - biophysics</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Cell Biology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Genetics</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biochemistry</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Structural Biology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biophysics</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1996</publicationDate><copyrightDate>1996</copyrightDate><doi><json:string>10.1016/0014-5793(96)01032-0</json:string></doi><id>58C8655DA75EEF980B9EF728BD3FF618BA65B321</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-GLMLCDV6-Z/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-GLMLCDV6-Z/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-GLMLCDV6-Z/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">(s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1996</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Section title: Research letter</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">(s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase</title><author xml:id="author-0000"><persName><forename type="first">Szilvia</forename><surname>Tökés</surname></persName><affiliation>Department of Biochemistry, University Medical School of Debrecen, P.O. Box 6, H-4012 Debrecen, Hungary</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Janos</forename><surname>Aradi</surname></persName><note type="correspondence"><p>Corresponding author. Fax: (36) (52) 416-432.</p></note><affiliation>Department of Biochemistry, University Medical School of Debrecen, P.O. Box 6, H-4012 Debrecen, Hungary</affiliation></author><idno type="istex">58C8655DA75EEF980B9EF728BD3FF618BA65B321</idno><idno type="ark">ark:/67375/6H6-GLMLCDV6-Z</idno><idno type="DOI">10.1016/0014-5793(96)01032-0</idno><idno type="PII">0014-5793(96)01032-0</idno></analytic><monogr><title level="j">FEBS Letters</title><title level="j" type="abbrev">FEBS</title><idno type="pISSN">0014-5793</idno><idno type="PII">S0014-5793(00)X0097-X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996"></date><biblScope unit="volume">396</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="43">43</biblScope><biblScope unit="page" to="46">46</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1996</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: Oligodeoxycytidylates were converted to s4dUMP-containing oligomers by treatment with liquid H2S. The inhibitory potency of the modified oligonucleotides on human immunodeficiency virus type 1 reverse transcriptase depended on the chain length and on the percentage of modification. The most potent reverse transcriptase inhibitor was (s4dU)35. The inhibitory pattern was competitive, when either poly(A)·(dT)16 or poly(C)·(dG)16 was used as template-primer (variable substrate), suggesting that the free enzyme interacts with (s4dU)35. The Ki values were 3.0 and 2.2 nM in the presence of poly(A)·(dT)16 and poly(C)·(dG)16, respectively.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Inhibition</term></item><item><term>Reverse transcriptase</term></item><item><term>Human immunodeficiency virus</term></item><item><term>Oligo 4-thio-2′-deoxyuridylate</term></item><item><term>Antitemplate</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>RT, reverse transcriptase</term></item><item><term>HIV, human immunodeficiency virus</term></item><item><term>AIDS, acquired immunodeficiency syndrome</term></item><item><term>TCA, trichloroacetic acid</term></item><item><term>Na-PPi, Na-pyrophosphate</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1996">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-GLMLCDV6-Z/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>FEBS</jid><aid>96010320</aid><ce:pii>0014-5793(96)01032-0</ce:pii><ce:doi>10.1016/0014-5793(96)01032-0</ce:doi><ce:copyright type="unknown" year="1996"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Research letter</ce:textfn></ce:dochead><ce:title>(s<ce:sup>4</ce:sup>dU)<ce:inf>35</ce:inf>: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase</ce:title><ce:author-group><ce:author><ce:given-name>Szilvia</ce:given-name><ce:surname>Tökés</ce:surname></ce:author><ce:author><ce:given-name>Janos</ce:given-name><ce:surname>Aradi</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Department of Biochemistry, University Medical School of Debrecen, P.O. Box 6, H-4012 Debrecen, Hungary</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author. Fax: (36) (52) 416-432.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="6" month="8" year="1996"></ce:date-received><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Oligodeoxycytidylates were converted to s<ce:sup>4</ce:sup>dUMP-containing oligomers by treatment with liquid H<ce:inf>2</ce:inf>S. The inhibitory potency of the modified oligonucleotides on human immunodeficiency virus type 1 reverse transcriptase depended on the chain length and on the percentage of modification. The most potent reverse transcriptase inhibitor was (s<ce:sup>4</ce:sup>dU)<ce:inf>35</ce:inf>. The inhibitory pattern was competitive, when either poly(A)·(dT)<ce:inf>16</ce:inf> or poly(C)·(dG)<ce:inf>16</ce:inf> was used as template-primer (variable substrate), suggesting that the free enzyme interacts with (s<ce:sup>4</ce:sup>dU)<ce:inf>35</ce:inf>. The <ce:italic>K</ce:italic><ce:inf><ce:italic>i</ce:italic></ce:inf> values were 3.0 and 2.2 nM in the presence of poly(A)·(dT)<ce:inf>16</ce:inf> and poly(C)·(dG)<ce:inf>16</ce:inf>, respectively.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Inhibition</ce:text></ce:keyword><ce:keyword><ce:text>Reverse transcriptase</ce:text></ce:keyword><ce:keyword><ce:text>Human immunodeficiency virus</ce:text></ce:keyword><ce:keyword><ce:text>Oligo 4-thio-2′-deoxyuridylate</ce:text></ce:keyword><ce:keyword><ce:text>Antitemplate</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>RT, reverse transcriptase</ce:text></ce:keyword><ce:keyword><ce:text>HIV, human immunodeficiency virus</ce:text></ce:keyword><ce:keyword><ce:text>AIDS, acquired immunodeficiency syndrome</ce:text></ce:keyword><ce:keyword><ce:text>TCA, trichloroacetic acid</ce:text></ce:keyword><ce:keyword><ce:text>Na-PPi, Na-pyrophosphate</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>(s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>(s</title></titleInfo><name type="personal"><namePart type="given">Szilvia</namePart><namePart type="family">Tökés</namePart><affiliation>Department of Biochemistry, University Medical School of Debrecen, P.O. Box 6, H-4012 Debrecen, Hungary</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Janos</namePart><namePart type="family">Aradi</namePart><affiliation>Department of Biochemistry, University Medical School of Debrecen, P.O. Box 6, H-4012 Debrecen, Hungary</affiliation><description>Corresponding author. Fax: (36) (52) 416-432.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1996</dateIssued><copyrightDate encoding="w3cdtf">1996</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Oligodeoxycytidylates were converted to s4dUMP-containing oligomers by treatment with liquid H2S. The inhibitory potency of the modified oligonucleotides on human immunodeficiency virus type 1 reverse transcriptase depended on the chain length and on the percentage of modification. The most potent reverse transcriptase inhibitor was (s4dU)35. The inhibitory pattern was competitive, when either poly(A)·(dT)16 or poly(C)·(dG)16 was used as template-primer (variable substrate), suggesting that the free enzyme interacts with (s4dU)35. The Ki values were 3.0 and 2.2 nM in the presence of poly(A)·(dT)16 and poly(C)·(dG)16, respectively.</abstract><note type="content">Section title: Research letter</note><subject><genre>Keywords</genre><topic>Inhibition</topic><topic>Reverse transcriptase</topic><topic>Human immunodeficiency virus</topic><topic>Oligo 4-thio-2′-deoxyuridylate</topic><topic>Antitemplate</topic></subject><subject><genre>Abbreviations</genre><topic>RT, reverse transcriptase</topic><topic>HIV, human immunodeficiency virus</topic><topic>AIDS, acquired immunodeficiency syndrome</topic><topic>TCA, trichloroacetic acid</topic><topic>Na-PPi, Na-pyrophosphate</topic></subject><relatedItem type="host"><titleInfo><title>FEBS Letters</title></titleInfo><titleInfo type="abbreviated"><title>FEBS</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1996</dateIssued></originInfo><identifier type="ISSN">0014-5793</identifier><identifier type="PII">S0014-5793(00)X0097-X</identifier><part><date>1996</date><detail type="volume"><number>396</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>113</end></extent><extent unit="pages"><start>43</start><end>46</end></extent></part></relatedItem><identifier type="istex">58C8655DA75EEF980B9EF728BD3FF618BA65B321</identifier><identifier type="ark">ark:/67375/6H6-GLMLCDV6-Z</identifier><identifier type="DOI">10.1016/0014-5793(96)01032-0</identifier><identifier type="PII">0014-5793(96)01032-0</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-GLMLCDV6-Z/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= (s4dU)35: a novel, highly potent oligonucleotide inhibitor of the human immunodeficiency virus type 1 reverse transcriptase
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