{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T00:00:39Z","timestamp":1779321639734,"version":"3.51.4"},"reference-count":126,"publisher":"Elsevier","isbn-type":[{"value":"9780323900164","type":"print"}],"license":[{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100007921","name":"University of Pittsburgh","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007921","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI150481"],"award-info":[{"award-number":["AI150481"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021]]},"DOI":"10.1016\/bs.enz.2021.07.007","type":"book-chapter","created":{"date-parts":[[2021,11,30]],"date-time":"2021-11-30T14:42:31Z","timestamp":1638283351000},"page":"227-247","source":"Crossref","is-referenced-by-count":12,"title":["Retroviral RNase H: Structure, mechanism, and inhibition"],"prefix":"10.1016","member":"78","reference":[{"key":"10.1016\/bs.enz.2021.07.007_bb0010","series-title":"Retroviruses","author":"Coffin","year":"1997"},{"key":"10.1016\/bs.enz.2021.07.007_bb0015","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1091\/mbc.E20-09-0612","article-title":"50th anniversary of the discovery of reverse transcriptase","volume":"32","author":"Coffin","year":"2021","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/bs.enz.2021.07.007_bb0020","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1038\/newbio234240a0","article-title":"Association of viral reverse transcriptase with an enzyme degrading the RNA moiety of RNA-DNA hybrids","volume":"234","author":"Molling","year":"1971","journal-title":"Nat. New Biol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0025","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/0042-6822(74)90302-X","article-title":"Characterization of reverse transcriptase and RNase H from friend-murine leukemia virus","volume":"62","author":"Moelling","year":"1974","journal-title":"Virology"},{"key":"10.1016\/bs.enz.2021.07.007_bb0030","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1002\/j.1460-2075.1988.tb02805.x","article-title":"Identification and characterization of HIV-specific RNase H by monoclonal antibody","volume":"7","author":"Hansen","year":"1987","journal-title":"EMBO J."},{"key":"10.1016\/bs.enz.2021.07.007_bb0035","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.virusres.2016.12.019","article-title":"Viral reverse transcriptases","volume":"234","author":"Men\u00e9ndez-Arias","year":"2017","journal-title":"Virus Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0040","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1146\/annurev.pa.36.040196.002553","article-title":"Structural mechanisms of HIV drug resistance","volume":"36","author":"Erickson","year":"1996","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0045","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0166-3542(98)00025-4","article-title":"The role of non-nucleoside reverse transcriptase inhibitors (NNRTIs) in the therapy of HIV-1 infection1 presented at the eleventh international conference on antiviral research, San Diego, CA, 5\u201310 April 1998.1","volume":"38","author":"De Clercq","year":"1998","journal-title":"Antivir. Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0050","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1038\/nrd1660","article-title":"Integrase inhibitors to treat HIV\/AIDS","volume":"4","author":"Pommier","year":"2005","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/bs.enz.2021.07.007_bb0055","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1124\/mi.9.2.5","article-title":"Anti-HIV-1 therapeutics: from FDA-approved drugs to hypothetical future targets","volume":"9","author":"Adamson","year":"2009","journal-title":"Mol. Interv."},{"key":"10.1016\/bs.enz.2021.07.007_bb0060","doi-asserted-by":"crossref","first-page":"a007161","DOI":"10.1101\/cshperspect.a007161","article-title":"HIV-1 antiretroviral drug therapy","volume":"2","author":"Arts","year":"2012","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/bs.enz.2021.07.007_bb0065","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1097\/COH.0000000000000478","article-title":"New HIV drugs: 2018 and beyond","volume":"13","author":"Gulick","year":"2018","journal-title":"Curr. Opin. HIV AIDS"},{"key":"10.1016\/bs.enz.2021.07.007_bb0070","doi-asserted-by":"crossref","first-page":"10895","DOI":"10.1073\/pnas.88.23.10895","article-title":"Crystals of a ternary complex of human immunodeficiency virus type 1 reverse transcriptase with a monoclonal antibody Fab fragment and double-stranded DNA diffract x-rays to 3.5-a resolution","volume":"88","author":"Jacobo-Molina","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0075","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1126\/science.1377403","article-title":"Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor","volume":"256","author":"Kohlstaedt","year":"1992","journal-title":"Science"},{"key":"10.1016\/bs.enz.2021.07.007_bb0080","doi-asserted-by":"crossref","first-page":"6320","DOI":"10.1073\/pnas.90.13.6320","article-title":"Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA","volume":"90","author":"Jacobo-Molina","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0085","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1086\/416128","article-title":"Origins and evolutionary relationships of retroviruses","volume":"64","author":"Doolittle","year":"1989","journal-title":"Q. Rev. Biol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0090","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1128\/JVI.77.1.366-374.2003","article-title":"The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage","volume":"77","author":"Pettit","year":"2003","journal-title":"J. Virol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0095","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1186\/1742-4690-2-66","article-title":"Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates","volume":"2","author":"Pettit","year":"2005","journal-title":"Retrovirology"},{"key":"10.1016\/bs.enz.2021.07.007_bb0100","doi-asserted-by":"crossref","first-page":"1187","DOI":"10.1101\/gr.185101","article-title":"Phylogenetic analysis of ribonuclease H domains suggests a late, chimeric origin of LTR retrotransposable elements and retroviruses","volume":"11","author":"Malik","year":"2001","journal-title":"Genome Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0105","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1159\/000084971","article-title":"Ribonuclease H evolution in retrotransposable elements","volume":"110","author":"Malik","year":"2005","journal-title":"Cytogenet. Genome Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0110","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1111\/nyas.12668","article-title":"The reverse transcriptase-RNase H: from viruses to antiviral defense","volume":"1341","author":"Moelling","year":"2015","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/bs.enz.2021.07.007_bb0115","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.3389\/fmicb.2017.01745","article-title":"RNase H as gene modifier, driver of evolution and antiviral defense","volume":"8","author":"Moelling","year":"2017","journal-title":"Front. Microbiol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0120","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/S0969-2126(01)00142-3","article-title":"Recombining the structures of HIV integrase, RuvC and RNase H","volume":"3","author":"Yang","year":"1995","journal-title":"Structure"},{"key":"10.1016\/bs.enz.2021.07.007_bb0125","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1038\/embor.2008.256","article-title":"Retroviral integrase superfamily: the structural perspective","volume":"10","author":"Nowotny","year":"2009","journal-title":"EMBO Rep."},{"key":"10.1016\/bs.enz.2021.07.007_bb0130","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/0092-8674(79)90357-X","article-title":"A detailed model of reverse transcription and tests of crucial aspects","volume":"18","author":"Gilboa","year":"1979","journal-title":"Cell"},{"key":"10.1016\/bs.enz.2021.07.007_bb0135","doi-asserted-by":"crossref","first-page":"7423","DOI":"10.1016\/S0021-9258(20)89464-2","article-title":"Polymerization and RNase H activities of the reverse transcriptases from avian myeloblastosis, human immunodeficiency, and Moloney murine leukemia viruses are functionally uncoupled","volume":"266","author":"DeStefano","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0140","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.virusres.2007.12.007","article-title":"RNase H activity: structure, specificity, and function in reverse transcription","volume":"134","author":"Schultz","year":"2008","journal-title":"Virus Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0145","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1111\/j.1742-4658.2009.06909.x","article-title":"Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription","volume":"276","author":"Champoux","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/bs.enz.2021.07.007_bb0150","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/S1054-3589(07)56005-9","article-title":"Inhibitors of HIV-1 reverse transcriptase","volume":"56","author":"Ilina","year":"2008","journal-title":"Adv. Pharmacol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0155","doi-asserted-by":"crossref","first-page":"900","DOI":"10.3390\/v2040900","article-title":"HIV-1 ribonuclease H: structure, catalytic mechanism and inhibitors","volume":"2","author":"Beilhartz","year":"2010","journal-title":"Viruses"},{"key":"10.1016\/bs.enz.2021.07.007_bb0160","first-page":"521","article-title":"Inhibitors of HIV-1 reverse transcriptase-associated ribonuclease H activity","volume":"1","author":"Ilina","year":"2012","journal-title":"Biology (Basel)"},{"key":"10.1016\/bs.enz.2021.07.007_bb0165","doi-asserted-by":"crossref","first-page":"2127","DOI":"10.4155\/fmc.13.178","article-title":"Active site and allosteric inhibitors of the ribonuclease H activity of HIV reverse transcriptase","volume":"5","author":"Corona","year":"2013","journal-title":"Future Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0170","doi-asserted-by":"crossref","first-page":"1956","DOI":"10.2174\/0929867321666140120121158","article-title":"Recent progress in the research of small molecule HIV-1 RNase H inhibitors","volume":"21","author":"Cao","year":"2014","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0175","doi-asserted-by":"crossref","first-page":"129","DOI":"10.3851\/IMP2690","article-title":"Past and future. Current drugs targeting HIV-1 integrase and reverse transcriptase-associated ribonuclease H activity: single and dual active site inhibitors","volume":"23","author":"Esposito","year":"2014","journal-title":"Antivir. Chem. Chemother."},{"key":"10.1016\/bs.enz.2021.07.007_bb0180","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1021\/acs.accounts.9b00450","article-title":"Cutting into the substrate dominance: pharmacophore and structure-based approaches toward inhibiting human immunodeficiency virus reverse transcriptase-associated ribonuclease H","volume":"53","author":"Wang","year":"2020","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0185","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1111\/j.1742-4658.2009.06908.x","article-title":"Ribonuclease H: the enzymes in eukaryotes","volume":"276","author":"Cerritelli","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/bs.enz.2021.07.007_bb0190","doi-asserted-by":"crossref","first-page":"1482","DOI":"10.1111\/j.1742-4658.2009.06907.x","article-title":"Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes","volume":"276","author":"Tadokoro","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/bs.enz.2021.07.007_bb0195","doi-asserted-by":"crossref","first-page":"7648","DOI":"10.1073\/pnas.83.20.7648","article-title":"Computer analysis of retroviral pol genes: assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes","volume":"83","author":"Johnson","year":"1986","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0200","doi-asserted-by":"crossref","first-page":"4160","DOI":"10.1093\/nar\/gkt1414","article-title":"The RNase H-like superfamily: new members, comparative structural analysis and evolutionary classification","volume":"42","author":"Majorek","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0205","doi-asserted-by":"crossref","first-page":"7625","DOI":"10.1128\/JVI.00353-10","article-title":"Structural basis for the inhibition of RNase H activity of HIV-1 reverse transcriptase by RNase H active site-directed inhibitors","volume":"84","author":"Su","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0210","doi-asserted-by":"crossref","first-page":"8233","DOI":"10.1073\/pnas.150220297","article-title":"Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding","volume":"97","author":"Chen","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0215","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.str.2004.02.032","article-title":"The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus","volume":"12","author":"Das","year":"2004","journal-title":"Structure"},{"key":"10.1016\/bs.enz.2021.07.007_bb0220","doi-asserted-by":"crossref","first-page":"5051","DOI":"10.1021\/acs.jmedchem.6b00465","article-title":"Design, synthesis, and biological evaluations of hydroxypyridonecarboxylic acids as inhibitors of HIV reverse transcriptase associated RNase H","volume":"59","author":"Kankanala","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0225","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.jmb.2010.02.019","article-title":"Visualizing the molecular interactions of a nucleotide analog, GS-9148, with HIV-1 reverse transcriptase-DNA complex","volume":"397","author":"Lansdon","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0230","doi-asserted-by":"crossref","first-page":"8125","DOI":"10.1093\/nar\/gku487","article-title":"Structures of HIV-1 RT-RNA\/DNA ternary complexes with dATP and nevirapine reveal conformational flexibility of RNA\/DNA: insights into requirements for RNase H cleavage","volume":"42","author":"Das","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0235","doi-asserted-by":"crossref","first-page":"2740","DOI":"10.1073\/pnas.92.7.2740","article-title":"Substitution of a highly basic helix\/loop sequence into the RNase H domain of human immunodeficiency virus reverse transcriptase restores its Mn(2+)-dependent RNase H activity","volume":"92","author":"Keck","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0240","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/nsmb.2785","article-title":"Ty3 reverse transcriptase complexed with an RNA-DNA hybrid shows structural and functional asymmetry","volume":"21","author":"Nowak","year":"2014","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0245","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1126\/science.2169648","article-title":"Structure of ribonuclease H phased at 2 a resolution by MAD analysis of the selenomethionyl protein","volume":"249","author":"Yang","year":"1990","journal-title":"Science"},{"key":"10.1016\/bs.enz.2021.07.007_bb0250","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1038\/347306a0","article-title":"Three-dimensional structure of ribonuclease H from E. coli","volume":"347","author":"Katayanagi","year":"1990","journal-title":"Nature"},{"key":"10.1016\/bs.enz.2021.07.007_bb0255","doi-asserted-by":"crossref","first-page":"4615","DOI":"10.1016\/S0021-9258(19)39607-3","article-title":"Identification of the amino acid residues involved in an active site of Escherichia coli ribonuclease H by site-directed mutagenesis","volume":"265","author":"Kanaya","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0260","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/S0021-9258(18)54118-1","article-title":"Role of histidine 124 in the catalytic function of ribonuclease HI from Escherichia coli","volume":"268","author":"Oda","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0265","doi-asserted-by":"crossref","first-page":"32729","DOI":"10.1074\/jbc.271.51.32729","article-title":"Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48","volume":"271","author":"Kanaya","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0270","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/S1389-1723(99)80168-6","article-title":"Molecular diversities of RNases H","volume":"88","author":"Ohtani","year":"1999","journal-title":"J. Biosci. Bioeng."},{"key":"10.1016\/bs.enz.2021.07.007_bb0275","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1016\/j.cell.2005.04.024","article-title":"Crystal structures of RNase H bound to an RNA\/DNA hybrid: substrate specificity and metal-dependent catalysis","volume":"121","author":"Nowotny","year":"2005","journal-title":"Cell"},{"key":"10.1016\/bs.enz.2021.07.007_bb0280","doi-asserted-by":"crossref","first-page":"1924","DOI":"10.1038\/sj.emboj.7601076","article-title":"Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release","volume":"25","author":"Nowotny","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/bs.enz.2021.07.007_bb0285","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1126\/science.1707186","article-title":"Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase","volume":"252","author":"Davies","year":"1991","journal-title":"Science"},{"key":"10.1016\/bs.enz.2021.07.007_bb0290","doi-asserted-by":"crossref","first-page":"3793","DOI":"10.1093\/nar\/22.18.3793","article-title":"Quantitative analysis of RNA cleavage during RNA-directed DNA synthesis by human immunodeficiency and avian myeloblastosis virus reverse transcriptases","volume":"22","author":"DeStefano","year":"1994","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0295","doi-asserted-by":"crossref","first-page":"32515","DOI":"10.1074\/jbc.M103958200","article-title":"Physical mapping of HIV reverse transcriptase to the 5\u2032 end of RNA primers","volume":"276","author":"DeStefano","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0300","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.1074\/jbc.M510504200","article-title":"Sequence, distance, and accessibility are determinants of 5\u2032-end-directed cleavages by retroviral RNases H","volume":"281","author":"Schultz","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0305","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/S0021-9258(18)52449-2","article-title":"Reverse transcriptase.RNase H from the human immunodeficiency virus. Relationship of the DNA polymerase and RNA hydrolysis activities","volume":"266","author":"Furfine","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0310","doi-asserted-by":"crossref","first-page":"10763","DOI":"10.1073\/pnas.89.22.10763","article-title":"Human immunodeficiency virus type 1 reverse transcriptase: spatial and temporal relationship between the polymerase and RNase H activities","volume":"89","author":"Gopalakrishnan","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0315","doi-asserted-by":"crossref","first-page":"40433","DOI":"10.1074\/jbc.M111.289850","article-title":"Mechanism of HIV reverse transcriptase inhibition by zinc: formation of a highly stable enzyme-(primer-template) complex with profoundly diminished catalytic activity","volume":"286","author":"Fenstermacher","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0320","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1093\/protein\/12.11.975","article-title":"Metal binding and activation of the ribonuclease H domain from moloney murine leukemia virus","volume":"12","author":"Goedken","year":"1999","journal-title":"Protein Eng."},{"key":"10.1016\/bs.enz.2021.07.007_bb0325","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1007\/s007750050009","article-title":"Metal-ion stoichiometry of the HIV-1 RT ribonuclease H domain: evidence for two mutually exclusive sites leads to new mechanistic insights on metal-mediated hydrolysis in nucleic acid biochemistry","volume":"5","author":"Cowan","year":"2000","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0330","doi-asserted-by":"crossref","first-page":"6498","DOI":"10.1073\/pnas.90.14.6498","article-title":"A general two-metal-ion mechanism for catalytic RNA","volume":"90","author":"Steitz","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0335","doi-asserted-by":"crossref","first-page":"40850","DOI":"10.1074\/jbc.R112.389056","article-title":"Human immunodeficiency virus reverse transcriptase: 25 years of research, drug discovery, and promise","volume":"287","author":"Le Grice","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0340","doi-asserted-by":"crossref","first-page":"3137","DOI":"10.1021\/ja411408x","article-title":"Calcium inhibition of ribonuclease H1 two-metal ion catalysis","volume":"136","author":"Rosta","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/bs.enz.2021.07.007_bb0345","doi-asserted-by":"crossref","first-page":"6852","DOI":"10.1093\/nar\/gkg881","article-title":"Two-metal ion mechanism of RNA cleavage by HIV RNase H and mechanism-based design of selective HIV RNase H inhibitors","volume":"31","author":"Klumpp","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0350","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.molcel.2006.03.013","article-title":"Making and breaking nucleic acids: two-Mg2+\u2212ion catalysis and substrate specificity","volume":"22","author":"Yang","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1016\/bs.enz.2021.07.007_bb0355","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1021\/bi0204894","article-title":"Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium","volume":"42","author":"Pari","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2021.07.007_bb0360","doi-asserted-by":"crossref","first-page":"639","DOI":"10.4236\/ajac.2011.26073","article-title":"Targeting divalent metal ions at the active site of the HIV-1 RNase H domain: NMR studies on the interactions of divalent metal ions with RNase H and its inhibitors","volume":"2","author":"Yan","year":"2011","journal-title":"Am. J. Anal. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0365","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1063\/1.1744152","article-title":"Reaction rates by nuclear magnetic resonance","volume":"28","author":"Mcconnell","year":"1958","journal-title":"J. Chem. Phys."},{"key":"10.1016\/bs.enz.2021.07.007_bb0370","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pnmrs.2013.02.001","article-title":"Using chemical shift perturbation to characterise ligand binding","volume":"73","author":"Williamson","year":"2013","journal-title":"Prog. Nucl. Magn. Reson. Spectrosc."},{"key":"10.1016\/bs.enz.2021.07.007_bb0375","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1007\/s10858-012-9678-6","article-title":"Accuracy and precision of protein-ligand interaction kinetics determined from chemical shift titrations","volume":"54","author":"Markin","year":"2012","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/bs.enz.2021.07.007_bb0380","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1007\/s10858-012-9630-9","article-title":"Increased precision for analysis of protein-ligand dissociation constants determined from chemical shift titrations","volume":"53","author":"Markin","year":"2012","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/bs.enz.2021.07.007_bb0385","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1007\/s10858-012-9636-3","article-title":"NMR line shapes and multi-state binding equilibria","volume":"53","author":"Kovrigin","year":"2012","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/bs.enz.2021.07.007_bb0390","doi-asserted-by":"crossref","first-page":"143","DOI":"10.2174\/9781608059621115010007","article-title":"Protein-inhibitor interaction studies using NMR","volume":"1","author":"Ishima","year":"2015","journal-title":"Appl. NMR Spectrosc."},{"key":"10.1016\/bs.enz.2021.07.007_bb0395","doi-asserted-by":"crossref","first-page":"12420","DOI":"10.1021\/acs.jpcb.6b08323","article-title":"Entire-dataset analysis of NMR fast-exchange titration spectra: a Mg2+ titration analysis for HIV-1 ribonuclease H domain","volume":"120","author":"Karki","year":"2016","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/bs.enz.2021.07.007_bb0400","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1093\/protein\/7.9.1103","article-title":"Construction of an enzymatically active ribonuclease H domain of human immunodeficiency virus type 1 reverse transcriptase","volume":"7","author":"Stahl","year":"1994","journal-title":"Protein Eng."},{"key":"10.1016\/bs.enz.2021.07.007_bb0405","doi-asserted-by":"crossref","first-page":"2777","DOI":"10.1074\/jbc.C200621200","article-title":"Inhibition of HIV-1 ribonuclease H by a novel diketo acid, 4-[5-(benzoylamino)thien-2-yl]-2,4-dioxobutanoic acid","volume":"278","author":"Shaw-Reid","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0410","doi-asserted-by":"crossref","first-page":"5781","DOI":"10.1021\/jm900597q","article-title":"RNase H active site inhibitors of human immunodeficiency virus type 1 reverse transcriptase: design, biochemical activity, and structural information","volume":"52","author":"Kirschberg","year":"2009","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0415","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1016\/j.str.2009.09.016","article-title":"Structure of HIV-1 reverse transcriptase with the inhibitor beta-thujaplicinol bound at the RNase H active site","volume":"17","author":"Himmel","year":"2009","journal-title":"Structure"},{"key":"10.1016\/bs.enz.2021.07.007_bb0420","doi-asserted-by":"crossref","first-page":"4462","DOI":"10.1021\/jm2000757","article-title":"Synthesis, activity, and structural analysis of novel alpha-hydroxytropolone inhibitors of human immunodeficiency virus reverse transcriptase-associated ribonuclease H","volume":"54","author":"Chung","year":"2011","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0425","doi-asserted-by":"crossref","first-page":"2905","DOI":"10.1128\/AAC.01594-10","article-title":"Structural and binding analysis of pyrimidinol carboxylic acid and N-hydroxy quinazolinedione HIV-1 RNase H inhibitors","volume":"55","author":"Lansdon","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/bs.enz.2021.07.007_bb0430","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.ab.2003.06.001","article-title":"A fluorescence-based high-throughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity","volume":"322","author":"Parniak","year":"2003","journal-title":"Anal. Biochem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0435","doi-asserted-by":"crossref","first-page":"6101","DOI":"10.1128\/AAC.03605-14","article-title":"Identification of highly conserved residues involved in inhibition of HIV-1 RNase H function by diketo acid derivatives","volume":"58","author":"Corona","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/bs.enz.2021.07.007_bb0440","doi-asserted-by":"crossref","first-page":"1915","DOI":"10.1021\/jm501799k","article-title":"Structure-activity relationship of pyrrolyl diketo acid derivatives as dual inhibitors of HIV-1 integrase and reverse transcriptase ribonuclease H domain","volume":"58","author":"Cuzzucoli Crucitti","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0445","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"10.1016\/bs.enz.2021.07.007_bb0450","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1016\/j.ejmech.2018.07.039","article-title":"6-Arylthio-3-hydroxypyrimidine-2,4-diones potently inhibited HIV reverse transcriptase-associated RNase H with antiviral activity","volume":"156","author":"Wang","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0455","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1016\/j.ejmech.2019.01.081","article-title":"Pharmacophore-based design of novel 3-hydroxypyrimidine-2,4-dione subtypes as inhibitors of HIV reverse transcriptase-associated RNase H: tolerance of a nonflexible linker","volume":"166","author":"Tang","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0460","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.ejmech.2017.09.054","article-title":"Design, synthesis and biological evaluations of N-Hydroxy thienopyrimidine-2,4-diones as inhibitors of HIV reverse transcriptase-associated RNase H","volume":"141","author":"Kankanala","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0465","doi-asserted-by":"crossref","first-page":"5045","DOI":"10.1021\/acs.jmedchem.7b00440","article-title":"Double-winged 3-hydroxypyrimidine-2,4-diones: potent and selective inhibition against HIV-1 RNase H with significant antiviral activity","volume":"60","author":"Vernekar","year":"2017","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0470","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.02203-17","article-title":"Developing and evaluating inhibitors against the RNase H active site of HIV-1 reverse transcriptase","volume":"92","author":"Boyer","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0475","doi-asserted-by":"crossref","first-page":"798","DOI":"10.1021\/acsmedchemlett.9b00617","article-title":"Pyrrolyl pyrazoles as non-diketo acid inhibitors of the HIV-1 ribonuclease H function of reverse transcriptase","volume":"11","author":"Messore","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2021.07.007_bb0480","doi-asserted-by":"crossref","first-page":"3179","DOI":"10.1021\/bi9624696","article-title":"Inhibition of the ribonuclease H and DNA polymerase activities of HIV-1 reverse transcriptase by N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone","volume":"36","author":"Borkow","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2021.07.007_bb0485","doi-asserted-by":"crossref","first-page":"1370","DOI":"10.1074\/jbc.M110254200","article-title":"Mutational analysis of Tyr-501 of HIV-1 reverse transcriptase. Effects on ribonuclease H activity and inhibition of this activity by N-acylhydrazones","volume":"277","author":"Arion","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0490","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1124\/mol.62.2.398","article-title":"Destabilization of the HIV-1 reverse transcriptase dimer upon interaction with N-acyl hydrazone inhibitors","volume":"62","author":"Sluis-Cremer","year":"2002","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0495","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1111\/cbdd.12010","article-title":"Structural basis of the allosteric inhibitor interaction on the HIV-1 reverse transcriptase RNase H domain","volume":"80","author":"Christen","year":"2012","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/bs.enz.2021.07.007_bb0500","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1021\/cb600303y","article-title":"HIV-1 reverse transcriptase structure with RNase H inhibitor dihydroxy benzoyl naphthyl hydrazone bound at a novel site","volume":"1","author":"Himmel","year":"2006","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0505","doi-asserted-by":"crossref","first-page":"440","DOI":"10.3389\/fmicb.2017.00440","article-title":"Chelation motifs affecting metal-dependent viral enzymes: N'-acylhydrazone ligands as dual target inhibitors of HIV-1 integrase and reverse transcriptase ribonuclease H domain","volume":"8","author":"Carcelli","year":"2017","journal-title":"Front. Microbiol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0510","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1016\/j.bmcl.2007.11.127","article-title":"Triazole derivatives as non-nucleoside inhibitors of HIV-1 reverse transcriptase\u2014structure-activity relationships and crystallographic analysis","volume":"18","author":"Kirschberg","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2021.07.007_bb0515","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.3390\/molecules25051183","article-title":"1,2,4-triazolo[1,5-a]pyrimidines as a novel class of inhibitors of the HIV-1 reverse transcriptase-associated ribonuclease H activity","volume":"25","author":"Desantis","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/bs.enz.2021.07.007_bb0520","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.3390\/molecules25061338","article-title":"2-(Arylamino)-6-(trifluoromethyl)nicotinic acid derivatives: new HIV-1 RT dual inhibitors active on viral replication","volume":"25","author":"Corona","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/bs.enz.2021.07.007_bb0525","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1080\/14756366.2021.1887170","article-title":"Flavonoids and acid-hydrolysis derivatives of neo-clerodane diterpenes from Teucrium flavum subsp. glaucum as inhibitors of the HIV-1 reverse transcriptase-associated RNase H function","volume":"36","author":"Fois","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0530","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/j.bbrc.2006.11.018","article-title":"Substrate-dependent inhibition or stimulation of HIV RNase H activity by non-nucleoside reverse transcriptase inhibitors (NNRTIs)","volume":"352","author":"Hang","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/bs.enz.2021.07.007_bb0535","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1124\/mol.107.038596","article-title":"Efavirenz accelerates HIV-1 reverse transcriptase ribonuclease H cleavage, leading to diminished zidovudine excision","volume":"73","author":"Radzio","year":"2008","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0540","doi-asserted-by":"crossref","first-page":"5238","DOI":"10.1128\/JVI.01545-09","article-title":"A novel molecular mechanism of dual resistance to nucleoside and nonnucleoside reverse transcriptase inhibitors","volume":"84","author":"Nikolenko","year":"2010","journal-title":"J. Virol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0545","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.bpj.2010.11.004","article-title":"Allosteric suppression of HIV-1 reverse transcriptase structural dynamics upon inhibitor binding","volume":"100","author":"Seckler","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/bs.enz.2021.07.007_bb0550","doi-asserted-by":"crossref","first-page":"8986","DOI":"10.1016\/S0021-9258(19)38799-X","article-title":"Dimerization of human immunodeficiency virus type 1 reverse transcriptase. A target for chemotherapeutic intervention","volume":"265","author":"Restle","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0555","doi-asserted-by":"crossref","first-page":"13080","DOI":"10.1016\/S0021-9258(17)36800-X","article-title":"Inhibition of human-immunodeficiency-virus Type-1 reverse-transcriptase dimerization using synthetic peptides derived from the connection domain","volume":"269","author":"Divita","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0560","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S0022-2836(02)01433-X","article-title":"Role of residues in the tryptophan repeat motif for HIV-1 reverse transcriptase dimerization","volume":"326","author":"Tachedjian","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0565","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.1021\/bi0484264","article-title":"Insight into the mechanism of a peptide inhibitor of HIV reverse transcriptase dimerization","volume":"44","author":"Depollier","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2021.07.007_bb0570","doi-asserted-by":"crossref","first-page":"4834","DOI":"10.1021\/jm0604575","article-title":"Structure-activity relationships of [2\u2032,5\u2032-bis-O-(tert-butyldimethylsilyl)-beta-D-ribofuranosyl]- 3\u2032-spiro-5\u2032 '-(4\u2032 '-amino-1\u2032 ',2\u2032 '-oxathiole-2\u2032 ',2\u2032 '-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization","volume":"49","author":"Sluis-Cremer","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0575","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.antiviral.2006.05.021","article-title":"Dimerization inhibitors of HIV-1 reverse transcriptase, protease and integrase: a single mode of inhibition for the three HIV enzymes?","volume":"71","author":"Camarasa","year":"2006","journal-title":"Antivir. Res."},{"key":"10.1016\/bs.enz.2021.07.007_bb0580","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1002\/cbic.200700669","article-title":"Small molecule inhibitors targeting HIV-1 reverse transcriptase dimerization","volume":"9","author":"Grohmann","year":"2008","journal-title":"Chembiochem"},{"key":"10.1016\/bs.enz.2021.07.007_bb0585","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1074\/jbc.M802199200","article-title":"A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility","volume":"284","author":"Agopian","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2021.07.007_bb0590","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1021\/acsmedchemlett.9b00623","article-title":"Peptides mimicking the beta7\/beta8 loop of HIV-1 reverse transcriptase p51 as \"hotspot-targeted\" dimerization inhibitors","volume":"11","author":"Sanchez-Murcia","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2021.07.007_bb0595","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0014-5793(92)80172-D","article-title":"RNase H activity of HIV reverse transcriptase is confined exclusively to the dimeric forms","volume":"300","author":"Restle","year":"1992","journal-title":"FEBS Lett."},{"key":"10.1016\/bs.enz.2021.07.007_bb0600","doi-asserted-by":"crossref","first-page":"2779","DOI":"10.1021\/bi051915z","article-title":"Effects of efavirenz binding on the subunit equilibria of HIV-1 reverse transcriptase","volume":"45","author":"Venezia","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2021.07.007_bb0605","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1002\/jmr.300070212","article-title":"Buried surface analysis of HIV-1 reverse transcriptase p66\/p51 heterodimer and its interaction with dsDNA template\/primer","volume":"7","author":"Ding","year":"1994","journal-title":"J. Mol. Recognit."},{"key":"10.1016\/bs.enz.2021.07.007_bb0610","doi-asserted-by":"crossref","first-page":"7242","DOI":"10.1073\/pnas.91.15.7242","article-title":"Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer","volume":"91","author":"Wang","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0615","doi-asserted-by":"crossref","first-page":"13012","DOI":"10.1021\/bi00211a009","article-title":"Structure\/function studies of HIV-1(1) reverse transcriptase: dimerization-defective mutant L289K","volume":"32","author":"Goel","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2021.07.007_bb0620","doi-asserted-by":"crossref","first-page":"8553","DOI":"10.1021\/bi952773j","article-title":"Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization","volume":"35","author":"Ghosh","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2021.07.007_bb0625","doi-asserted-by":"crossref","first-page":"6334","DOI":"10.1073\/pnas.97.12.6334","article-title":"Analysis of mutations and suppressors affecting interactions between the subunits of the HIV type 1 reverse transcriptase","volume":"97","author":"Tachedjian","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2021.07.007_bb0630","doi-asserted-by":"crossref","first-page":"10247","DOI":"10.1128\/JVI.79.16.10247-10257.2005","article-title":"Mutations that abrogate human immunodeficiency virus type 1 reverse transcriptase dimerization affect maturation of the reverse transcriptase heterodimer","volume":"79","author":"Wapling","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/bs.enz.2021.07.007_bb0635","doi-asserted-by":"crossref","first-page":"1879","DOI":"10.2174\/138161206776873590","article-title":"Dimerization of human immunodeficiency virus type 1 reverse transcriptase as an antiviral target","volume":"12","author":"Srivastava","year":"2006","journal-title":"Curr. Pharm. Des."}],"container-title":["The Enzymes","Viral Replication Enzymes and their Inhibitors Part B"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604721000172?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604721000172?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,7,24]],"date-time":"2025-07-24T11:05:14Z","timestamp":1753355114000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604721000172"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021]]},"ISBN":["9780323900164"],"references-count":126,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2021.07.007","relation":{},"ISSN":["1874-6047"],"issn-type":[{"value":"1874-6047","type":"print"}],"subject":[],"published":{"date-parts":[[2021]]}}}