{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T03:39:01Z","timestamp":1777433941142,"version":"3.51.4"},"reference-count":133,"publisher":"Portland Press Ltd.","issue":"10","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2017,5,15]]},"abstract":"<jats:p>Infections by the human immunodeficiency virus type 1 (HIV-1), the causative agent of the acquired immunodeficiency syndrome (AIDS), are still totaling an appalling 36.7 millions worldwide, with 1.1 million AIDS deaths\/year and a similar number of yearly new infections. All this, in spite of the discovery of HIV-1 as the AIDS etiological agent more than 30 years ago and the introduction of an effective combinatorial antiretroviral therapy (cART), able to control disease progression, more than 20 years ago. Although very effective, current cART is plagued by the emergence of drug-resistant viral variants and most of the efforts in the development of novel direct-acting antiviral agents (DAAs) against HIV-1 have been devoted toward the fighting of resistance. In this review, rather than providing a detailed listing of all the drugs and the corresponding resistance mutations, we aim, through relevant examples, at presenting to the general reader the conceptual shift in the approaches that are being taken to overcome the viral resistance hurdle. From the classic \u2018running faster\u2019 strategy, based on the development of novel DAAs active against the mutant viruses selected by the previous drugs and\/or presenting to the virus a high genetic barrier toward the development of resilience, to a \u2018jumping higher\u2019 approach, which looks at the cell, rather than the virus, as a source of valuable drug targets, in order to make the cellular environment non-permissive toward the replication of both wild-type and mutated viruses.<\/jats:p>","DOI":"10.1042\/bcj20160772","type":"journal-article","created":{"date-parts":[[2017,4,27]],"date-time":"2017-04-27T00:30:30Z","timestamp":1493253030000},"page":"1559-1577","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["How to win the HIV-1 drug resistance hurdle race: running faster or jumping higher?"],"prefix":"10.1042","volume":"474","author":[{"given":"Anna","family":"Garbelli","sequence":"first","affiliation":[{"name":"DNA Enzymology & Molecular Virology Unit, Institute of Molecular Genetics \u2014 CNR, via Abbiategrasso 207, Pavia 27100, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Valentina","family":"Riva","sequence":"additional","affiliation":[{"name":"DNA Enzymology & Molecular Virology Unit, Institute of Molecular Genetics \u2014 CNR, via Abbiategrasso 207, Pavia 27100, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emmanuele","family":"Crespan","sequence":"additional","affiliation":[{"name":"DNA Enzymology & Molecular Virology Unit, Institute of Molecular Genetics \u2014 CNR, via Abbiategrasso 207, Pavia 27100, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Giovanni","family":"Maga","sequence":"additional","affiliation":[{"name":"DNA Enzymology & Molecular Virology Unit, Institute of Molecular Genetics \u2014 CNR, via Abbiategrasso 207, Pavia 27100, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2017,4,26]]},"reference":[{"key":"2021112216374315400_BCJ-2016-0772CC1","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1016\/j.coviro.2016.03.004","article-title":"Current status and prospects of HIV treatment","volume":"18","author":"Cihlar","year":"2016","journal-title":"Curr. Opin. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC2","doi-asserted-by":"publisher","first-page":"4095","DOI":"10.3390\/v6104095","article-title":"Current perspectives on HIV-1 antiretroviral drug resistance","volume":"6","author":"Iyidogan","year":"2014","journal-title":"Viruses"},{"key":"2021112216374315400_BCJ-2016-0772CC3","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1038\/387188a0","article-title":"Decay characteristics of HIV-1-infected compartments during combination therapy","volume":"387","author":"Perelson","year":"1997","journal-title":"Nature"},{"key":"2021112216374315400_BCJ-2016-0772CC4","doi-asserted-by":"publisher","first-page":"e46","DOI":"10.1371\/journal.ppat.0030046","article-title":"ART suppresses plasma HIV-1 RNA to a stable set point predicted by pretherapy viremia","volume":"3","author":"Maldarelli","year":"2007","journal-title":"PLoS Pathog."},{"key":"2021112216374315400_BCJ-2016-0772CC5","doi-asserted-by":"publisher","first-page":"1312","DOI":"10.1093\/cid\/ciu585","article-title":"HIV-1 DNA decay dynamics in blood during more than a decade of suppressive antiretroviral therapy","volume":"59","author":"Besson","year":"2014","journal-title":"Clin. Infect. Dis."},{"key":"2021112216374315400_BCJ-2016-0772CC6","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1097\/COH.0000000000000120","article-title":"Review: influence of ART on HIV genetics","volume":"10","author":"Simonetti","year":"2015","journal-title":"Curr. Opin. HIV AIDS"},{"key":"2021112216374315400_BCJ-2016-0772CC7","doi-asserted-by":"publisher","first-page":"e1004010","DOI":"10.1371\/journal.ppat.1004010","article-title":"Lack of detectable HIV-1 molecular evolution during suppressive antiretroviral therapy","volume":"10","author":"Kearney","year":"2014","journal-title":"PLoS Pathog."},{"key":"2021112216374315400_BCJ-2016-0772CC8","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1126\/science.1254194","article-title":"Specific HIV integration sites are linked to clonal expansion and persistence of infected cells","volume":"345","author":"Maldarelli","year":"2014","journal-title":"Science"},{"key":"2021112216374315400_BCJ-2016-0772CC9","doi-asserted-by":"publisher","first-page":"e18889","DOI":"10.7554\/eLife.18889","article-title":"Establishment and stability of the latent HIV-1 DNA reservoir","volume":"5","author":"Brodin","year":"2016","journal-title":"eLife"},{"key":"2021112216374315400_BCJ-2016-0772CC10","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1038\/nature16933","article-title":"Persistent HIV-1 replication maintains the tissue reservoir during therapy","volume":"530","author":"Lorenzo-Redondo","year":"2016","journal-title":"Nature"},{"key":"2021112216374315400_BCJ-2016-0772CC11","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1097\/COH.0000000000000287","article-title":"Persistent HIV-1 replication during antiretroviral therapy","volume":"11","author":"Martinez-Picado","year":"2016","journal-title":"Curr. Opin. HIV AIDS"},{"key":"2021112216374315400_BCJ-2016-0772CC12","doi-asserted-by":"publisher","first-page":"e1004677","DOI":"10.1371\/journal.pcbi.1004677","article-title":"Residual viremia in treated HIV+ individuals","volume":"12","author":"Conway","year":"2016","journal-title":"PLoS Comput. Biol."},{"key":"2021112216374315400_BCJ-2016-0772CC13","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1016\/j.virusres.2007.12.021","article-title":"HIV-1 reverse transcriptase inhibitor resistance mutations and fitness: a view from the clinic and ex vivo","volume":"134","author":"Martinez-Picado","year":"2008","journal-title":"Virus Res."},{"key":"2021112216374315400_BCJ-2016-0772CC14","doi-asserted-by":"publisher","first-page":"305","DOI":"10.2174\/1389200043335478","article-title":"Structural determinants and molecular mechanisms for the resistance of HIV-1 RT to nucleoside analogues","volume":"5","author":"Deval","year":"2004","journal-title":"Curr. Drug Metab."},{"key":"2021112216374315400_BCJ-2016-0772CC15","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1089\/aid.2013.0153","article-title":"The high cost of fidelity","volume":"30","author":"Lloyd","year":"2014","journal-title":"AIDS Res. Hum. Retroviruses"},{"key":"2021112216374315400_BCJ-2016-0772CC16","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1002\/prot.21829","article-title":"The balance between the rates of incorporation and pyrophosphorolytic removal influences the HIV-1 reverse transcriptase bypass of an abasic site with deoxy-, dideoxy-, and ribonucleotides","volume":"71","author":"Sharma","year":"2008","journal-title":"Proteins"},{"key":"2021112216374315400_BCJ-2016-0772CC17","volume-title":"Antiretroviral Resistance in Clinical Practice","author":"De Luca","year":"2006"},{"key":"2021112216374315400_BCJ-2016-0772CC18","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1016\/j.virusres.2007.12.018","article-title":"Structural basis for drug resistance mechanisms for non-nucleoside inhibitors of HIV reverse transcriptase","volume":"134","author":"Ren","year":"2008","journal-title":"Virus Res."},{"key":"2021112216374315400_BCJ-2016-0772CC19","doi-asserted-by":"publisher","first-page":"9377","DOI":"10.1128\/JVI.00618-10","article-title":"Reduced fitness in cell culture of HIV-1 with nonnucleoside reverse transcriptase inhibitor-resistant mutations correlates with relative levels of reverse transcriptase content and RNase H activity in virions","volume":"84","author":"Wang","year":"2010","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC20","doi-asserted-by":"publisher","first-page":"1512","DOI":"10.1128\/JVI.77.2.1512-1523.2003","article-title":"Amino acid substitutions at position 190 of human immunodeficiency virus type 1 reverse transcriptase increase susceptibility to delavirdine and impair virus replication","volume":"77","author":"Huang","year":"2003","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC21","doi-asserted-by":"publisher","first-page":"4611","DOI":"10.1128\/AAC.48.12.4611-4617.2004","article-title":"Gln145met\/Leu changes in human immunodeficiency virus type 1 reverse transcriptase confer resistance to nucleoside and nonnucleoside analogs and impair virus replication","volume":"48","author":"Paolucci","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC22","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1021\/jm00122a029","article-title":"1-(2,3-Dideoxy-beta-d-glycero-pent-2-enofuranosyl)thymine. A highly potent and selective anti-HIV agent","volume":"32","author":"Mansuri","year":"1989","journal-title":"J. Med. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC23","doi-asserted-by":"publisher","first-page":"733","DOI":"10.1128\/AAC.36.4.733","article-title":"(\u2212)-2\u2032-Deoxy-3\u2032-thiacytidine is a potent, highly selective inhibitor of human immunodeficiency virus type 1 and type 2 replication in vitro","volume":"36","author":"Coates","year":"1992","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC24","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1128\/AAC.41.5.1082","article-title":"1592U89, a novel carbocyclic nucleoside analog with potent, selective anti-human immunodeficiency virus activity","volume":"41","author":"Daluge","year":"1997","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC25","doi-asserted-by":"publisher","first-page":"1292","DOI":"10.1128\/AAC.38.6.1292","article-title":"Anti-human immunodeficiency virus activities of the beta-L enantiomer of 2\u2032,3\u2032-dideoxycytidine and its 5-fluoro derivative in vitro","volume":"38","author":"Gosselin","year":"1994","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC26","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1128\/AAC.41.3.611","article-title":"Antiretroviral activities of acyclic nucleoside phosphonates [9-(2-phosphonylmethoxyethyl)adenine, 9-(2-phosphonylmethoxyethyl)guanine, (R)-9-(2-phosphonylmethoxypropyl)adenine, and MDL 74,968] in cell cultures and murine sarcoma virus-infected newborn NMRI mice","volume":"41","author":"Balzarini","year":"1997","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC27","doi-asserted-by":"publisher","first-page":"1773","DOI":"10.2217\/fmb.15.106","article-title":"Resistance to reverse transcriptase inhibitors used in the treatment and prevention of HIV-1 infection","volume":"10","author":"Sluis-Cremer","year":"2015","journal-title":"Future Microbiol."},{"key":"2021112216374315400_BCJ-2016-0772CC28","doi-asserted-by":"publisher","first-page":"24533","DOI":"10.1074\/jbc.M114.562694","article-title":"4\u2032-Ethynyl-2-fluoro-2\u2032-deoxyadenosine (EFdA) inhibits HIV-1 reverse transcriptase with multiple mechanisms","volume":"289","author":"Michailidis","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC29","first-page":"40","article-title":"The sugar ring conformation of 4\u2032-ethynyl-2-fluoro-2\u2032-deoxyadenosine and its recognition by the polymerase active site of HIV reverse transcriptase","volume":"57","author":"Kirby","year":"2011","journal-title":"Cell. Mol. Biol."},{"key":"2021112216374315400_BCJ-2016-0772CC30","doi-asserted-by":"publisher","first-page":"9274","DOI":"10.1073\/pnas.1605223113","article-title":"Structural basis of HIV inhibition by translocation-defective RT inhibitor 4\u2032-ethynyl-2-fluoro-2\u2032-deoxyadenosine (EFdA)","volume":"113","author":"Salie","year":"2016","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112216374315400_BCJ-2016-0772CC31","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1186\/1742-4690-10-65","article-title":"Hypersusceptibility mechanism of Tenofovir-resistant HIV to EFdA","volume":"10","author":"Michailidis","year":"2013","journal-title":"Retrovirology"},{"key":"2021112216374315400_BCJ-2016-0772CC32","doi-asserted-by":"publisher","first-page":"880","DOI":"10.3390\/v2040880","article-title":"HIV-1 RT inhibitors with a novel mechanism of action: NNRTIs that compete with the nucleotide substrate","volume":"2","author":"Maga","year":"2010","journal-title":"Viruses"},{"key":"2021112216374315400_BCJ-2016-0772CC33","doi-asserted-by":"publisher","first-page":"17336","DOI":"10.1074\/jbc.M112.433441","article-title":"Formation of a quaternary complex of HIV-1 reverse transcriptase with a nucleotide-competing inhibitor and its ATP enhancer","volume":"288","author":"Ehteshami","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC34","doi-asserted-by":"publisher","first-page":"1810","DOI":"10.1002\/anie.200604165","article-title":"Discovery of non-nucleoside inhibitors of HIV-1 reverse transcriptase competing with the nucleotide substrate","volume":"46","author":"Maga","year":"2007","journal-title":"Angew. Chem. Int. Ed."},{"key":"2021112216374315400_BCJ-2016-0772CC35","doi-asserted-by":"publisher","first-page":"1805","DOI":"10.1002\/anie.200905651","article-title":"Crystal structure of HIV-1 reverse transcriptase bound to a non-nucleoside inhibitor with a novel mechanism of action","volume":"49","author":"Freisz","year":"2010","journal-title":"Angew. Chem. Int. Ed."},{"key":"2021112216374315400_BCJ-2016-0772CC36","doi-asserted-by":"publisher","first-page":"847","DOI":"10.1590\/0074-02760150239","article-title":"Computational drug design strategies applied to the modelling of human immunodeficiency virus-1 reverse transcriptase inhibitors","volume":"110","author":"Santos","year":"2015","journal-title":"Mem. Inst. Oswaldo Cruz"},{"key":"2021112216374315400_BCJ-2016-0772CC37","doi-asserted-by":"publisher","first-page":"4680","DOI":"10.1128\/AAC.48.12.4680-4686.2004","article-title":"TMC125, a novel next-generation nonnucleoside reverse transcriptase inhibitor active against nonnucleoside reverse transcriptase inhibitor-resistant human immunodeficiency virus type 1","volume":"48","author":"Andries","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC38","doi-asserted-by":"publisher","first-page":"1901","DOI":"10.1021\/jm040840e","article-title":"In search of a novel anti-HIV drug: multidisciplinary coordination in the discovery of 4-[[4-[[4-[(1E)-2-cyanoethenyl]-2,6-dimethylphenyl]amino]-2-pyrimidinyl]amino]benzonitrile (R278474, rilpivirine)","volume":"48","author":"Janssen","year":"2005","journal-title":"J. Med. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC39","doi-asserted-by":"publisher","first-page":"38110","DOI":"10.1074\/jbc.M112.398180","article-title":"Biochemical mechanism of HIV-1 resistance to rilpivirine","volume":"287","author":"Singh","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC40","doi-asserted-by":"publisher","first-page":"250","DOI":"10.1093\/jac\/dks404","article-title":"Rilpivirine: a new non-nucleoside reverse transcriptase inhibitor","volume":"68","author":"Sharma","year":"2013","journal-title":"J. Antimicrob. Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC41","doi-asserted-by":"publisher","first-page":"7344","DOI":"10.1016\/j.bmcl.2011.10.027","article-title":"Design and synthesis of pyridone inhibitors of non-nucleoside reverse transcriptase","volume":"21","author":"Gomez","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"2021112216374315400_BCJ-2016-0772CC42","doi-asserted-by":"publisher","first-page":"917","DOI":"10.1016\/j.bmcl.2013.12.070","article-title":"Discovery of MK-1439, an orally bioavailable non-nucleoside reverse transcriptase inhibitor potent against a wide range of resistant mutant HIV viruses","volume":"24","author":"C\u00f4t\u00e9","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"2021112216374315400_BCJ-2016-0772CC43","doi-asserted-by":"publisher","first-page":"590","DOI":"10.1128\/AAC.04201-14","article-title":"In vitro resistance selection with doravirine (MK-1439), a novel nonnucleoside reverse transcriptase inhibitor with distinct mutation development pathways","volume":"59","author":"Feng","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC44","first-page":"95","article-title":"HIV protease inhibitors: a review of molecular selectivity and toxicity","volume":"7","author":"Lv","year":"2015","journal-title":"HIV AIDS"},{"key":"2021112216374315400_BCJ-2016-0772CC45","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1002\/rmv.624","article-title":"The history of antiretrovirals: key discoveries over the past 25 years","volume":"19","author":"De Clercq","year":"2009","journal-title":"Rev. Med. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC46","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1016\/j.antiviral.2006.05.007","article-title":"Aspects of successful drug discovery and development","volume":"71","author":"Pauwels","year":"2006","journal-title":"Antiviral Res."},{"key":"2021112216374315400_BCJ-2016-0772CC47","doi-asserted-by":"publisher","first-page":"547","DOI":"10.1016\/j.tim.2016.03.010","article-title":"Improving viral protease inhibitors to counter drug resistance","volume":"24","author":"Kurt Yilmaz","year":"2016","journal-title":"Trends Microbiol."},{"key":"2021112216374315400_BCJ-2016-0772CC48","doi-asserted-by":"publisher","first-page":"1333","DOI":"10.1016\/j.chembiol.2004.08.010","article-title":"Combating susceptibility to drug resistance: lessons from HIV-1 protease","volume":"11","author":"King","year":"2004","journal-title":"Chem. Biol."},{"key":"2021112216374315400_BCJ-2016-0772CC49","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1016\/S0969-2126(02)00720-7","article-title":"Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes","volume":"10","author":"Prabu-Jeyabalan","year":"2002","journal-title":"Structure"},{"key":"2021112216374315400_BCJ-2016-0772CC50","doi-asserted-by":"publisher","first-page":"1778","DOI":"10.1002\/anie.201102762","article-title":"Enhancing protein backbone binding \u2014 a fruitful concept for combating drug-resistant HIV","volume":"51","author":"Ghosh","year":"2012","journal-title":"Angew. Chem. Int. Ed."},{"key":"2021112216374315400_BCJ-2016-0772CC51","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1021\/ar7001232","article-title":"Design of HIV protease inhibitors targeting protein backbone: an effective strategy for combating drug resistance","volume":"41","author":"Ghosh","year":"2008","journal-title":"Acc. Chem. Res."},{"key":"2021112216374315400_BCJ-2016-0772CC52","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1016\/j.coviro.2013.03.012","article-title":"HIV-1 reverse transcriptase and antiviral drug resistance. Part 1","volume":"3","author":"Das","year":"2013","journal-title":"Curr. Opin. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC53","doi-asserted-by":"publisher","first-page":"1116","DOI":"10.1016\/j.chembiol.2013.07.014","article-title":"Substrate envelope-designed potent HIV-1 protease inhibitors to avoid drug resistance","volume":"20","author":"Nalam","year":"2013","journal-title":"Chem. Biol."},{"key":"2021112216374315400_BCJ-2016-0772CC54","doi-asserted-by":"crossref","first-page":"3218","DOI":"10.1128\/AAC.42.12.3218","article-title":"ABT-378, a highly potent inhibitor of the human immunodeficiency virus protease","volume":"42","author":"Sham","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC55","doi-asserted-by":"publisher","first-page":"642","DOI":"10.1097\/COH.0b013e3283136cee","article-title":"New approaches to HIV protease inhibitor drug design II: testing the substrate envelope hypothesis to avoid drug resistance and discover robust inhibitors","volume":"3","author":"Nalam","year":"2008","journal-title":"Curr. Opin. HIV AIDS"},{"key":"2021112216374315400_BCJ-2016-0772CC56","doi-asserted-by":"publisher","first-page":"e417","DOI":"10.1016\/S2352-3018(15)00176-9","article-title":"Protease inhibitor monotherapy for long-term management of HIV infection: a randomised, controlled, open-label, non-inferiority trial","volume":"2","author":"Paton","year":"2015","journal-title":"Lancet HIV"},{"key":"2021112216374315400_BCJ-2016-0772CC57","doi-asserted-by":"publisher","first-page":"2617","DOI":"10.1097\/QAD.0000000000001206","article-title":"Factors associated with virological rebound in HIV-infected patients receiving protease inhibitor monotherapy","volume":"30","author":"St\u00f6hr","year":"2016","journal-title":"AIDS"},{"key":"2021112216374315400_BCJ-2016-0772CC58","doi-asserted-by":"publisher","first-page":"547","DOI":"10.1586\/17474124.2015.1032938","article-title":"Ritonavir-boosted protease inhibitor based therapy: a new strategy in chronic hepatitis C therapy","volume":"9","author":"Brayer","year":"2015","journal-title":"Expert Rev. Gastroenterol. Hepatol."},{"key":"2021112216374315400_BCJ-2016-0772CC59","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1046\/j.1468-1293.2001.00063.x","article-title":"Principles and practice of HIV-protease inhibitor pharmacoenhancement","volume":"2","author":"Moyle","year":"2001","journal-title":"HIV Med."},{"key":"2021112216374315400_BCJ-2016-0772CC60","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1016\/j.dld.2010.09.007","article-title":"Forthcoming challenges in the management of direct-acting antiviral agents (DAAs) for hepatitis C","volume":"43","author":"Bruno","year":"2011","journal-title":"Dig. Liver Dis."},{"key":"2021112216374315400_BCJ-2016-0772CC61","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1093\/jac\/dkh029","article-title":"Pharmacological and therapeutic properties of ritonavir-boosted protease inhibitor therapy in HIV-infected patients","volume":"53","author":"Zeldin","year":"2004","journal-title":"J. Antimicrob. Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC62","doi-asserted-by":"publisher","first-page":"69","DOI":"10.5414\/CPP38069","article-title":"P-glycoprotein: a defense mechanism limiting oral bioavailability and CNS accumulation of drugs","volume":"38","author":"Fromm","year":"2000","journal-title":"Int. J. Clin. Pharmacol. Ther."},{"key":"2021112216374315400_BCJ-2016-0772CC63","doi-asserted-by":"publisher","first-page":"a006866","DOI":"10.1101\/cshperspect.a006866","article-title":"HIV: Cell binding and entry","volume":"2","author":"Wilen","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"issue":"Suppl 1","key":"2021112216374315400_BCJ-2016-0772CC64","doi-asserted-by":"publisher","first-page":"e6","DOI":"10.4081\/idr.2013.s1.e6","article-title":"Pathogenesis of HIV infection","volume":"5","author":"Naif","year":"2013","journal-title":"Infect. Dis. Rep."},{"key":"2021112216374315400_BCJ-2016-0772CC65","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1016\/j.coviro.2015.06.007","article-title":"CCR5\u039432 mutation and HIV infection: basis for curative HIV therapy","volume":"14","author":"Allers","year":"2015","journal-title":"Curr. Opin. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC66","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1016\/S0092-8674(00)80110-5","article-title":"Homozygous defect in HIV-1 coreceptor accounts for resistance of some multiply-exposed individuals to HIV-1 infection","volume":"86","author":"Liu","year":"1996","journal-title":"Cell"},{"key":"2021112216374315400_BCJ-2016-0772CC67","doi-asserted-by":"publisher","first-page":"722","DOI":"10.1038\/382722a0","article-title":"Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene","volume":"382","author":"Samson","year":"1996","journal-title":"Nature"},{"key":"2021112216374315400_BCJ-2016-0772CC68","doi-asserted-by":"publisher","first-page":"1240","DOI":"10.1038\/nm1196-1240","article-title":"The role of a mutant CCR5 allele in HIV-1 transmission and disease progression","volume":"2","author":"Huang","year":"1996","journal-title":"Nat. Med."},{"key":"2021112216374315400_BCJ-2016-0772CC69","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1038\/ng0597-100","article-title":"Global distribution of the CCR5 gene 32-basepair deletion","volume":"16","author":"Martinson","year":"1997","journal-title":"Nat. Genet."},{"key":"2021112216374315400_BCJ-2016-0772CC70","doi-asserted-by":"publisher","first-page":"e339","DOI":"10.1371\/journal.pbio.0030339","article-title":"The geographic spread of the CCR5 \u039432 HIV-resistance allele","volume":"3","author":"Novembre","year":"2005","journal-title":"PLoS Biol."},{"key":"2021112216374315400_BCJ-2016-0772CC71","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1007\/s11481-011-9268-5","article-title":"Early events of HIV-1 infection: can signaling be the next therapeutic target?","volume":"6","author":"Jones","year":"2011","journal-title":"J. Neuroimmune Pharmacol."},{"key":"2021112216374315400_BCJ-2016-0772CC72","doi-asserted-by":"publisher","first-page":"38","DOI":"10.12927\/whp.2010.21762","article-title":"HIV\/AIDS awareness and knowledge among secondary school students in China","volume":"11","author":"Zhao","year":"2010","journal-title":"World Health Popul."},{"key":"2021112216374315400_BCJ-2016-0772CC73","doi-asserted-by":"publisher","first-page":"264","DOI":"10.1038\/sj.gene.6364298","article-title":"Negative association between the chemokine receptor CCR5-\u039432 polymorphism and rheumatoid arthritis: a meta-analysis","volume":"7","author":"Prahalad","year":"2006","journal-title":"Genes Immun."},{"key":"2021112216374315400_BCJ-2016-0772CC74","doi-asserted-by":"publisher","first-page":"1443","DOI":"10.1097\/01.aids.0000183633.06580.8a","article-title":"Antiviral activity and safety of 873140, a novel CCR5 antagonist, during short-term monotherapy in HIV-infected adults","volume":"19","author":"Lalezari","year":"2005","journal-title":"AIDS"},{"key":"2021112216374315400_BCJ-2016-0772CC75","doi-asserted-by":"publisher","first-page":"858","DOI":"10.1128\/AAC.00821-07","article-title":"Hepatotoxicity observed in clinical trials of aplaviroc (GW873140)","volume":"52","author":"Nichols","year":"2008","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC76","doi-asserted-by":"publisher","first-page":"1293","DOI":"10.1097\/QAD.0b013e3280f00f9f","article-title":"Antiviral activity, pharmacokinetics and safety of vicriviroc, an oral CCR5 antagonist, during 14-day monotherapy in HIV-infected adults","volume":"21","author":"Sch\u00fcrmann","year":"2007","journal-title":"AIDS"},{"key":"2021112216374315400_BCJ-2016-0772CC77","doi-asserted-by":"publisher","first-page":"304","DOI":"10.1086\/518797","article-title":"Phase 2 study of the safety and efficacy of vicriviroc, a CCR5 inhibitor, in HIV-1\u2013Infected, treatment-experienced patients: AIDS clinical trials group 5211","volume":"196","author":"Gulick","year":"2007","journal-title":"J. Infect. Dis."},{"key":"2021112216374315400_BCJ-2016-0772CC78","doi-asserted-by":"publisher","first-page":"590","DOI":"10.1086\/650342","article-title":"Vicriviroc in combination therapy with an optimized regimen for treatment-experienced subjects: 48-week results of the VICTOR-E1 phase 2 trial","volume":"201","author":"Suleiman","year":"2010","journal-title":"J. Infect. Dis."},{"key":"2021112216374315400_BCJ-2016-0772CC79","doi-asserted-by":"publisher","first-page":"326","DOI":"10.1016\/j.jinf.2012.05.008","article-title":"Vicriviroc plus optimized background therapy for treatment-experienced subjects with CCR5 HIV-1 infection: final results of two randomized phase III trials","volume":"65","author":"Caseiro","year":"2012","journal-title":"J. Infect."},{"key":"2021112216374315400_BCJ-2016-0772CC80","doi-asserted-by":"publisher","first-page":"4584","DOI":"10.1128\/AAC.49.11.4584-4591.2005","article-title":"TAK-652 inhibits CCR5-mediated human immunodeficiency virus type 1 infection in vitro and has favorable pharmacokinetics in humans","volume":"49","author":"Baba","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC81","doi-asserted-by":"publisher","first-page":"118","DOI":"10.1097\/QAI.0b013e318213c2c0","article-title":"Safety, efficacy, and pharmacokinetics of TBR-652, a CCR5\/CCR2 antagonist, in HIV-1\u2013infected, treatment-experienced, CCR5 antagonist\u2013naive subjects","volume":"57","author":"Lalezari","year":"2011","journal-title":"J. Acquired Immune Defic. Syndr."},{"key":"2021112216374315400_BCJ-2016-0772CC82","doi-asserted-by":"publisher","first-page":"4721","DOI":"10.1128\/AAC.49.11.4721-4732.2005","article-title":"Maraviroc (UK-427,857), a potent, orally bioavailable, and selective small-Molecule inhibitor of chemokine receptor CCR5 with broad-spectrum anti-human immunodeficiency virus type 1 activity","volume":"49","author":"Dorr","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"2021112216374315400_BCJ-2016-0772CC83","doi-asserted-by":"publisher","first-page":"1442","DOI":"10.1056\/NEJMoa0803154","article-title":"Subgroup analyses of maraviroc in previously treated R5 HIV-1 infection","volume":"359","author":"F\u00e4tkenheuer","year":"2008","journal-title":"N. Engl J. Med."},{"key":"2021112216374315400_BCJ-2016-0772CC84","doi-asserted-by":"publisher","first-page":"4186","DOI":"10.3390\/v7082816","article-title":"CCR5 targeted cell therapy for HIV and prevention of viral escape","volume":"7","author":"H\u00fctter","year":"2015","journal-title":"Viruses"},{"key":"2021112216374315400_BCJ-2016-0772CC85","doi-asserted-by":"publisher","first-page":"2359","DOI":"10.1128\/JVI.02006-06","article-title":"Reduced maximal inhibition in phenotypic susceptibility assays indicates that viral strains resistant to the CCR5 antagonist maraviroc utilize inhibitor-bound receptor for entry","volume":"81","author":"Westby","year":"2007","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC86","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1186\/1742-4690-10-43","article-title":"A common mechanism of clinical HIV-1 resistance to the CCR5 antagonist maraviroc despite divergent resistance levels and lack of common gp120 resistance mutations","volume":"10","author":"Roche","year":"2013","journal-title":"Retrovirology"},{"key":"2021112216374315400_BCJ-2016-0772CC87","doi-asserted-by":"publisher","first-page":"10863","DOI":"10.1128\/JVI.01109-10","article-title":"A maraviroc-resistant HIV-1 with narrow cross-resistance to other CCR5 antagonists depends on both N-terminal and extracellular loop domains of drug-bound CCR5","volume":"84","author":"Tilton","year":"2010","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC88","doi-asserted-by":"publisher","first-page":"803","DOI":"10.1086\/650697","article-title":"Maraviroc versus efavirenz, both in combination with zidovudine-lamivudine, for the treatment of antiretroviral-naive subjects with CCR5-tropic HIV-1 infection","volume":"201","author":"Cooper","year":"2010","journal-title":"J. Infect. Dis."},{"key":"2021112216374315400_BCJ-2016-0772CC89","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1097\/QAI.0b013e3181ff63ee","article-title":"Mapping and characterization of vicriviroc resistance mutations from HIV-1 isolated from treatment-experienced subjects enrolled in a phase II study (VICTOR-E1)","volume":"56","author":"McNicholas","year":"2011","journal-title":"J. Acquired Immune Defic. Syndr."},{"key":"2021112216374315400_BCJ-2016-0772CC90","doi-asserted-by":"publisher","first-page":"420","DOI":"10.1097\/QAI.0b013e3181f25574","article-title":"Evolution of CCR5 antagonist resistance in an HIV-1 subtype C clinical isolate","volume":"55","author":"Henrich","year":"2010","journal-title":"J. Acquired Immune Defic. Syndr."},{"key":"2021112216374315400_BCJ-2016-0772CC91","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1016\/j.virol.2007.12.009","article-title":"Mapping resistance to the CCR5 co-receptor antagonist vicriviroc using heterologous chimeric HIV-1 envelope genes reveals key determinants in the C2-V5 domain of gp120","volume":"373","author":"Ogert","year":"2008","journal-title":"Virology"},{"key":"2021112216374315400_BCJ-2016-0772CC92","doi-asserted-by":"publisher","first-page":"8210","DOI":"10.1128\/JVI.00444-08","article-title":"In vivo emergence of vicriviroc resistance in a human immunodeficiency virus type 1 subtype C-infected subject","volume":"82","author":"Tsibris","year":"2008","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC93","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1016\/j.virol.2010.01.037","article-title":"Clinical resistance to vicriviroc through adaptive V3 loop mutations in HIV-1 subtype D gp120 that alter interactions with the N-terminus and ECL2 of CCR5","volume":"400","author":"Ogert","year":"2010","journal-title":"Virology"},{"key":"2021112216374315400_BCJ-2016-0772CC94","doi-asserted-by":"publisher","first-page":"6505","DOI":"10.1128\/JVI.00374-10","article-title":"HIV-1 resistance to CCR5 antagonists associated with highly efficient use of CCR5 and altered tropism on primary CD4+ T cells","volume":"84","author":"Pfaff","year":"2010","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC95","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s12977-015-0177-1","article-title":"A single-residue change in the HIV-1 V3 loop associated with maraviroc resistance impairs CCR5 binding affinity while increasing replicative capacity","volume":"12","author":"Garcia-Perez","year":"2015","journal-title":"Retrovirology"},{"key":"2021112216374315400_BCJ-2016-0772CC96","doi-asserted-by":"publisher","first-page":"11807","DOI":"10.1128\/JVI.78.21.11807-11815.2004","article-title":"Coevolution of RANTES sensitivity and mode of CCR5 receptor use by human immunodeficiency virus type 1 of the R5 phenotype","volume":"78","author":"Karlsson","year":"2004","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC97","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1186\/s12977-016-0309-2","article-title":"Frequency and Env determinants of HIV-1 subtype C strains from antiretroviral therapy-naive subjects that display incomplete inhibition by maraviroc","volume":"13","author":"Borm","year":"2016","journal-title":"Retrovirology"},{"key":"2021112216374315400_BCJ-2016-0772CC98","doi-asserted-by":"publisher","first-page":"5318","DOI":"10.1073\/pnas.0811713106","article-title":"Resistance to CCR5 inhibitors caused by sequence changes in the fusion peptide of HIV-1 gp41","volume":"106","author":"Anastassopoulou","year":"2009","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112216374315400_BCJ-2016-0772CC99","doi-asserted-by":"publisher","first-page":"1470","DOI":"10.1086\/652189","article-title":"Characterization of emergent HIV resistance in treatment-naive subjects enrolled in a vicriviroc phase 2 trial","volume":"201","author":"McNicholas","year":"2010","journal-title":"J. Infect. Dis."},{"key":"2021112216374315400_BCJ-2016-0772CC100","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1007\/7355_2014_45","article-title":"Targeting Cellular Cofactors in HIV Therapy","volume":"15","author":"D\u00fcrr","year":"2014","journal-title":"Top. Med. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC101","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1038\/nchembio.370","article-title":"Rational design of small-molecule inhibitors of the LEDGF\/p75-integrase interaction and HIV replication","volume":"6","author":"Christ","year":"2010","journal-title":"Nat. Chem. Biol."},{"key":"2021112216374315400_BCJ-2016-0772CC102","doi-asserted-by":"publisher","first-page":"1911","DOI":"10.1002\/pro.2997","article-title":"Allosteric HIV-1 integrase inhibitors promote aberrant protein multimerization by directly mediating inter-subunit interactions: structural and thermodynamic modeling studies","volume":"25","author":"Deng","year":"2016","journal-title":"Protein Sci."},{"key":"2021112216374315400_BCJ-2016-0772CC103","doi-asserted-by":"publisher","first-page":"e1004171","DOI":"10.1371\/journal.ppat.1004171","article-title":"A new class of multimerization selective inhibitors of HIV-1 integrase","volume":"10","author":"Sharma","year":"2014","journal-title":"PLoS Pathog."},{"key":"2021112216374315400_BCJ-2016-0772CC104","doi-asserted-by":"publisher","first-page":"1167","DOI":"10.2174\/1568026615666150901115106","article-title":"Targeting virus-host interactions of HIV replication","volume":"16","author":"Weydert","year":"2016","journal-title":"Curr. Top. Med. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC105","doi-asserted-by":"publisher","first-page":"2598","DOI":"10.2741\/1994","article-title":"Mechanisms controlling CDK9 activity","volume":"11","author":"Marshall","year":"2006","journal-title":"Front. Biosci."},{"key":"2021112216374315400_BCJ-2016-0772CC106","doi-asserted-by":"publisher","first-page":"812","DOI":"10.1016\/j.jmb.2012.12.005","article-title":"Effect of mimetic CDK9 inhibitors on HIV-1-activated transcription","volume":"425","author":"Van Duyne","year":"2013","journal-title":"J. Mol. Biol."},{"key":"2021112216374315400_BCJ-2016-0772CC107","doi-asserted-by":"publisher","first-page":"2072","DOI":"10.1002\/cbic.200900303","article-title":"Identification of flavopiridol analogues that selectively inhibit positive transcription elongation factor (P-TEFb) and block HIV-1 replication","volume":"10","author":"Ali","year":"2009","journal-title":"ChemBioChem"},{"key":"2021112216374315400_BCJ-2016-0772CC108","doi-asserted-by":"publisher","first-page":"342","DOI":"10.2174\/092986711794839188","article-title":"Novel, selective CDK9 inhibitors for the treatment of HIV infection","volume":"18","author":"Nemeth","year":"2011","journal-title":"Curr. Med. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC109","doi-asserted-by":"publisher","first-page":"1187","DOI":"10.1038\/nbt.1496","article-title":"Small-molecule inhibition of HIV-1 Vif","volume":"26","author":"Nathans","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"2021112216374315400_BCJ-2016-0772CC110","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1155\/2010\/649315","article-title":"Towards inhibition of Vif-APOBEC3G interaction: which protein to target?","volume":"2010","author":"Cadima-Couto","year":"2010","journal-title":"Adv. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC111","doi-asserted-by":"publisher","first-page":"381","DOI":"10.1016\/j.cell.2004.09.029","article-title":"Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function","volume":"119","author":"Yedavalli","year":"2004","journal-title":"Cell"},{"key":"2021112216374315400_BCJ-2016-0772CC112","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1006\/viro.1999.9659","article-title":"Hepatitis C virus core protein interacts with a human DEAD box protein DDX3","volume":"257","author":"Owsianka","year":"1999","journal-title":"Virology"},{"key":"2021112216374315400_BCJ-2016-0772CC113","doi-asserted-by":"publisher","first-page":"15751","DOI":"10.1074\/jbc.274.22.15751","article-title":"Hepatitis C virus core protein binds to a DEAD box RNA helicase","volume":"274","author":"Mamiya","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC114","doi-asserted-by":"crossref","first-page":"2841","DOI":"10.1128\/JVI.73.4.2841-2853.1999","article-title":"Hepatitis C virus core protein interacts with cellular putative RNA helicase","volume":"73","author":"You","year":"1999","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC115","doi-asserted-by":"publisher","first-page":"13922","DOI":"10.1128\/JVI.01517-07","article-title":"DDX3 DEAD-box RNA helicase is required for hepatitis C virus RNA replication","volume":"81","author":"Ariumi","year":"2007","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC116","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1016\/j.virol.2013.11.008","article-title":"Cellular DDX3 regulates Japanese encephalitis virus replication by interacting with viral un-translated regions","volume":"449","author":"Li","year":"2014","journal-title":"Virology"},{"key":"2021112216374315400_BCJ-2016-0772CC117","doi-asserted-by":"publisher","first-page":"450","DOI":"10.1016\/j.antiviral.2009.12.011","article-title":"Strategies for development of Dengue virus inhibitors","volume":"85","author":"Noble","year":"2010","journal-title":"Antivir. Res."},{"key":"2021112216374315400_BCJ-2016-0772CC118","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.virol.2012.09.041","article-title":"P-body components LSM1, GW182, DDX3, DDX6 and XRN1 are recruited to WNV replication sites and positively regulate viral replication","volume":"436","author":"Chahar","year":"2013","journal-title":"Virology"},{"key":"2021112216374315400_BCJ-2016-0772CC119","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/S1672-0229(03)01002-7","article-title":"Advances in the study of SR protein family","volume":"1","author":"Ma","year":"2003","journal-title":"Genomics Proteomics Bioinformatics"},{"key":"2021112216374315400_BCJ-2016-0772CC120","doi-asserted-by":"publisher","first-page":"843","DOI":"10.1016\/j.jmb.2008.09.048","article-title":"Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3","volume":"385","author":"Kalverda","year":"2009","journal-title":"J. Mol. Biol."},{"issue":"Pt 7","key":"2021112216374315400_BCJ-2016-0772CC121","doi-asserted-by":"publisher","first-page":"1647","DOI":"10.1099\/vir.0.052670-0","article-title":"Vaccinia virus protein K7 is a virulence factor that alters the acute immune response to infection","volume":"94","author":"Benfield","year":"2013","journal-title":"J. Gen. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC122","doi-asserted-by":"publisher","first-page":"11977","DOI":"10.1128\/JVI.00432-12","article-title":"Identification of RNA-protein interaction networks involved in the Norovirus life cycle","volume":"86","author":"Vashist","year":"2012","journal-title":"J. Virol."},{"key":"2021112216374315400_BCJ-2016-0772CC123","doi-asserted-by":"publisher","first-page":"3015","DOI":"10.2174\/092986711796391688","article-title":"Targeting the human DEAD-box polypeptide 3 (DDX3) RNA helicase as a novel strategy to inhibit viral replication","volume":"18","author":"Garbelli","year":"2011","journal-title":"Curr. Med. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC124","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1042\/BST0390679","article-title":"Viruses and the human DEAD-box helicase DDX3: inhibition or exploitation?","volume":"39","author":"Schr\u00f6der","year":"2011","journal-title":"Biochem. Soc. Trans."},{"key":"2021112216374315400_BCJ-2016-0772CC125","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1016\/j.virol.2004.09.039","article-title":"A DEAD box protein facilitates HIV-1 replication as a cellular co-factor of Rev","volume":"330","author":"Fang","year":"2004","journal-title":"Virology"},{"key":"2021112216374315400_BCJ-2016-0772CC126","doi-asserted-by":"publisher","first-page":"5043","DOI":"10.1021\/jm800332m","article-title":"Ring expanded nucleoside analogues inhibit RNA helicase and intracellular human immunodeficiency virus type 1 replication","volume":"51","author":"Yedavalli","year":"2008","journal-title":"J. Med. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC127","doi-asserted-by":"publisher","first-page":"150","DOI":"10.1016\/j.jmb.2007.06.050","article-title":"Crystal structure of conserved domains 1 and 2 of the human DEAD-box helicase DDX3X in complex with the mononucleotide AMP","volume":"372","author":"H\u00f6gbom","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2021112216374315400_BCJ-2016-0772CC128","doi-asserted-by":"publisher","first-page":"6635","DOI":"10.1021\/jm8008844","article-title":"Pharmacophore modeling and molecular docking led to the discovery of inhibitors of human immunodeficiency virus-1 replication targeting the human cellular aspartic acid\u2013glutamic acid\u2013alanine\u2013aspartic acid box polypeptide 3","volume":"51","author":"Maga","year":"2008","journal-title":"J. Med. Chem."},{"key":"2021112216374315400_BCJ-2016-0772CC129","doi-asserted-by":"publisher","first-page":"1371","DOI":"10.1002\/cmdc.201100166","article-title":"Toward the discovery of novel anti-HIV drugs. Second-generation inhibitors of the cellular ATPase DDX3 with improved anti-HIV activity: synthesis, structure-activity relationship analysis, cytotoxicity studies, and target validation","volume":"6","author":"Maga","year":"2011","journal-title":"ChemMedChem"},{"key":"2021112216374315400_BCJ-2016-0772CC130","doi-asserted-by":"publisher","first-page":"2094","DOI":"10.1016\/j.bmcl.2011.12.135","article-title":"Discovery of the first small molecule inhibitor of human DDX3 specifically designed to target the RNA binding site: towards the next generation HIV-1 inhibitors","volume":"22","author":"Radi","year":"2012","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"2021112216374315400_BCJ-2016-0772CC131","doi-asserted-by":"publisher","first-page":"2443","DOI":"10.1021\/acs.jcim.5b00419","article-title":"Homology model-based virtual screening for the identification of human helicase DDX3 inhibitors","volume":"55","author":"Fazi","year":"2015","journal-title":"J. Chem. Inf. Model."},{"key":"2021112216374315400_BCJ-2016-0772CC132","doi-asserted-by":"publisher","first-page":"5388","DOI":"10.1073\/pnas.1522987113","article-title":"Human DDX3 protein is a valuable target to develop broad spectrum antiviral agents","volume":"113","author":"Brai","year":"2016","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021112216374315400_BCJ-2016-0772CC133","doi-asserted-by":"publisher","first-page":"14","DOI":"10.1016\/j.coviro.2016.02.001","article-title":"Which therapeutic strategy will achieve a cure for HIV-1?","volume":"18","author":"Cillo","year":"2016","journal-title":"Curr. Opin. Virol."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/474\/10\/1559\/688314\/bcj-2016-0772c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/474\/10\/1559\/688314\/bcj-2016-0772c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T23:23:15Z","timestamp":1637623395000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/474\/10\/1559\/49406\/How-to-win-the-HIV-1-drug-resistance-hurdle-race"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,4,26]]},"references-count":133,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2017,5,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bcj20160772","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,4,26]]}}}