{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T21:31:35Z","timestamp":1790544695863,"version":"4.1.0"},"reference-count":62,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2021,9,1]],"date-time":"2021-09-01T00:00:00Z","timestamp":1630454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,9,1]],"date-time":"2021-09-01T00:00:00Z","timestamp":1630454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T00:00:00Z","timestamp":1627516800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100009139","name":"DZIF","doi-asserted-by":"publisher","award":["TTU 05.902"],"award-info":[{"award-number":["TTU 05.902"]}],"id":[{"id":"10.13039\/100009139","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001655","name":"DAAD","doi-asserted-by":"publisher","award":["PPP 57155496"],"award-info":[{"award-number":["PPP 57155496"]}],"id":[{"id":"10.13039\/501100001655","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"DFG","doi-asserted-by":"publisher","award":["WE 4388\/6-1"],"award-info":[{"award-number":["WE 4388\/6-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003042","name":"EKFS","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003042","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2021,9]]},"DOI":"10.1016\/j.jbc.2021.101031","type":"journal-article","created":{"date-parts":[[2021,7,30]],"date-time":"2021-07-30T23:11:38Z","timestamp":1627686698000},"page":"101031","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Epistatic interactions promote persistence of NS3-Q80K in\u00a0HCV infection by compensating for protein folding instability"],"prefix":"10.1016","volume":"297","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0775-0907","authenticated-orcid":false,"given":"Georg","family":"Dultz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1752-5060","authenticated-orcid":false,"given":"Sanjay K.","family":"Srikakulam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Konetschnik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tetsuro","family":"Shimakami","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8806-6850","authenticated-orcid":false,"given":"Nadezhda T.","family":"Doncheva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julia","family":"Dietz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christoph","family":"Sarrazin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8873-7167","authenticated-orcid":false,"given":"Ricardo M.","family":"Biondi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Zeuzem","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0403-2160","authenticated-orcid":false,"given":"Robert","family":"Tamp\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga V.","family":"Kalinina","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1823-4863","authenticated-orcid":false,"given":"Christoph","family":"Welsch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2021.101031_bib1","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1093\/infdis\/jiu613","article-title":"Global origin and transmission of hepatitis C virus nonstructural protein 3 Q80K polymorphism","volume":"211","author":"McCloskey","year":"2015","journal-title":"J.\u00a0Infect. Dis."},{"key":"10.1016\/j.jbc.2021.101031_bib2","series-title":"Handbook of Antimicrobial Resistance","author":"G\u00f6tte","year":"2017"},{"key":"10.1016\/j.jbc.2021.101031_bib3","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/j.jhep.2018.10.031","article-title":"HCV genotype 1-6 NS3 residue 80 substitutions impact protease inhibitor activity and promote viral escape","volume":"70","author":"Pham","year":"2019","journal-title":"J.\u00a0Hepatol."},{"key":"10.1016\/j.jbc.2021.101031_bib4","doi-asserted-by":"crossref","first-page":"2430","DOI":"10.1002\/hep.29693","article-title":"Impact of hepatitis C virus polymorphisms on direct-acting antiviral treatment efficacy: Regulatory analyses and perspectives","volume":"67","author":"Harrington","year":"2018","journal-title":"Hepatology"},{"key":"10.1016\/j.jbc.2021.101031_bib5","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.antiviral.2015.01.003","article-title":"Prevalence of the hepatitis C virus NS3 polymorphism Q80K in genotype 1 patients in the European region","volume":"116","author":"Sarrazin","year":"2015","journal-title":"Antiviral Res."},{"key":"10.1016\/j.jbc.2021.101031_bib6","doi-asserted-by":"crossref","first-page":"7548","DOI":"10.1128\/AAC.01444-15","article-title":"In\u00a0vitro activity of simeprevir against hepatitis C virus genotype 1 clinical isolates and its correlation with NS3 sequence and site-directed mutants","volume":"59","author":"Verbinnen","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jbc.2021.101031_bib7","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1016\/j.jhep.2014.11.032","article-title":"Virology analyses of HCV isolates from genotype 1-infected patients treated with simeprevir plus peginterferon\/ribavirin in phase IIb\/III studies","volume":"62","author":"Lenz","year":"2015","journal-title":"J.\u00a0Hepatol."},{"key":"10.1016\/j.jbc.2021.101031_bib8","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1053\/j.gastro.2017.11.007","article-title":"Patterns of resistance-associated substitutions in patients with chronic HCV infection following treatment with direct-acting antivirals","volume":"154","author":"Dietz","year":"2018","journal-title":"Gastroenterology"},{"key":"10.1016\/j.jbc.2021.101031_bib9","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1042\/BST20170063","article-title":"Biomolecular coevolution and its applications: Going from structure prediction toward signaling, epistasis, and function","volume":"45","author":"Zerihun","year":"2017","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jbc.2021.101031_bib10","doi-asserted-by":"crossref","DOI":"10.2202\/1544-6115.1517","article-title":"Epistatic interactions","volume":"9","author":"VanderWeele","year":"2010","journal-title":"Stat. Appl. Genet. Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101031_bib11","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/bs.mie.2020.07.012","article-title":"Statistical analysis of mutational epistasis to reveal intramolecular interaction networks in proteins","volume":"643","author":"Miton","year":"2020","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jbc.2021.101031_bib12","first-page":"1","article-title":"The hepatitis C virus NS3 protein: A model RNA helicase and potential drug target","volume":"9","author":"Frick","year":"2007","journal-title":"Curr. Issues Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101031_bib13","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1038\/nrmicro3046","article-title":"The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection","volume":"11","author":"Bartenschlager","year":"2013","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2021.101031_bib14","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1016\/j.cell.2005.08.012","article-title":"Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3","volume":"122","author":"Seth","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101031_bib15","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1038\/nature04193","article-title":"Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus","volume":"437","author":"Meylan","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101031_bib16","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.molcel.2005.08.014","article-title":"VISA is an adapter protein required for virus-triggered IFN-beta signaling","volume":"19","author":"Xu","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2021.101031_bib17","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1038\/ni1243","article-title":"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction","volume":"6","author":"Kawai","year":"2005","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.jbc.2021.101031_bib18","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1016\/j.jhep.2014.11.009","article-title":"Hepatitis C virus variants resistant to macrocyclic NS3-4A inhibitors subvert IFN-\u03b2 induction by efficient MAVS cleavage","volume":"62","author":"Welsch","year":"2015","journal-title":"J.\u00a0Hepatol."},{"key":"10.1016\/j.jbc.2021.101031_bib19","doi-asserted-by":"crossref","first-page":"7624","DOI":"10.1128\/JVI.00724-08","article-title":"NS3 helicase domains involved in infectious intracellular hepatitis C virus particle assembly","volume":"82","author":"Ma","year":"2008","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.jbc.2021.101031_bib20","doi-asserted-by":"crossref","first-page":"29929","DOI":"10.1074\/jbc.M804065200","article-title":"Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase","volume":"283","author":"Beran","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101031_bib21","doi-asserted-by":"crossref","first-page":"5362","DOI":"10.1128\/JVI.03188-14","article-title":"Protease inhibitors block multiple functions of the NS3\/4A protease-helicase during the hepatitis C virus life cycle","volume":"89","author":"McGivern","year":"2015","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.jbc.2021.101031_bib22","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.antiviral.2008.08.004","article-title":"Molecular targets for flavivirus drug discovery","volume":"81","author":"Sampath","year":"2009","journal-title":"Antiviral Res."},{"key":"10.1016\/j.jbc.2021.101031_bib23","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1053\/j.gastro.2010.10.056","article-title":"Protease inhibitor-resistant hepatitis C virus mutants with reduced fitness from impaired production of infectious virus","volume":"140","author":"Shimakami","year":"2011","journal-title":"Gastroenterology"},{"key":"10.1016\/j.jbc.2021.101031_bib24","doi-asserted-by":"crossref","first-page":"D363","DOI":"10.1093\/nar\/gkl970","article-title":"euHCVdb: The European hepatitis C virus database","volume":"35","author":"Combet","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2021.101031_bib25","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1038\/nprot.2007.321","article-title":"The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability","volume":"2","author":"Niesen","year":"2007","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.jbc.2021.101031_bib26","series-title":"Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists","author":"Copeland","year":"2013"},{"key":"10.1016\/j.jbc.2021.101031_bib27","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.1002\/pro.5560071011","article-title":"Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease","volume":"7","author":"Taremi","year":"1998","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2021.101031_bib28","doi-asserted-by":"crossref","first-page":"11450","DOI":"10.1021\/acs.jpcb.8b07379","article-title":"Stability effects of protein mutations: The role of long-range contacts","volume":"122","author":"Bigman","year":"2018","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.jbc.2021.101031_bib29","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1128\/MMBR.05023-11","article-title":"Viral quasispecies evolution","volume":"76","author":"Domingo","year":"2012","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.jbc.2021.101031_bib30","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.3000544","article-title":"Rapid emergence of protease inhibitor resistance in hepatitis C virus","volume":"2","author":"Rong","year":"2010","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.jbc.2021.101031_bib31","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/j.jtbi.2010.08.036","article-title":"Understanding hepatitis C viral dynamics with direct-acting antiviral agents due to the interplay between intracellular replication and cellular infection dynamics","volume":"267","author":"Guedj","year":"2010","journal-title":"J.\u00a0Theor. Biol."},{"key":"10.1016\/j.jbc.2021.101031_bib32","doi-asserted-by":"crossref","first-page":"13862","DOI":"10.1074\/jbc.RA120.013898","article-title":"Extended interaction networks with HCV protease NS3-4A substrates explain the lack of adaptive capability against protease inhibitors","volume":"295","author":"Dultz","year":"2020","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101031_bib33","doi-asserted-by":"crossref","first-page":"8205","DOI":"10.1074\/jbc.M510246200","article-title":"Mutations conferring resistance to SCH6, a novel hepatitis C virus NS3\/4A protease inhibitor. Reduced RNA replication fitness and partial rescue by second-site mutations","volume":"281","author":"Yi","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101031_bib34","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1053\/j.gastro.2011.11.035","article-title":"Peptidomimetic escape mechanisms arise via genetic diversity in the ligand-binding site of the hepatitis C virus NS3\/4A serine protease","volume":"142","author":"Welsch","year":"2012","journal-title":"Gastroenterology"},{"key":"10.1016\/j.jbc.2021.101031_bib35","doi-asserted-by":"crossref","first-page":"2354","DOI":"10.1016\/j.jmb.2019.04.034","article-title":"Near-neighbor interactions in the NS3-4A protease of HCV impact replicative fitness of drug-resistant viral variants","volume":"431","author":"Doncheva","year":"2019","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101031_bib36","doi-asserted-by":"crossref","first-page":"16152","DOI":"10.1073\/pnas.0705366104","article-title":"Protein stability imposes limits on organism complexity and speed of molecular evolution","volume":"104","author":"Zeldovich","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101031_bib37","doi-asserted-by":"crossref","first-page":"691","DOI":"10.3390\/v11080691","article-title":"Effects of the Q80K polymorphism on the physicochemical properties of hepatitis C virus subtype 1a NS3 protease","volume":"11","author":"Peres-da-Silva","year":"2019","journal-title":"Viruses"},{"key":"10.1016\/j.jbc.2021.101031_bib38","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1021\/acschembio.7b01078","article-title":"Modulation of the allosteric communication between the polo-box domain and the catalytic domain in Plk1 by small compounds","volume":"13","author":"Raab","year":"2018","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.jbc.2021.101031_bib39","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.sbi.2019.11.005","article-title":"Proteins: Molecules defined by their trade-offs","volume":"60","author":"Bigman","year":"2020","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jbc.2021.101031_bib40","doi-asserted-by":"crossref","first-page":"e02601","DOI":"10.1128\/AAC.02601-17","article-title":"Unexpected replication boost by simeprevir for simeprevir-resistant variants in genotype 1a hepatitis C virus","volume":"62","author":"Murai","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jbc.2021.101031_bib41","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.vaccine.2004.05.009","article-title":"A\u00a0liposomal peptide vaccine inducing CD8+ T cells in HLA-A2.1 transgenic mice, which recognise human cells encoding hepatitis C virus (HCV) proteins","volume":"23","author":"Engler","year":"2004","journal-title":"Vaccine"},{"key":"10.1016\/j.jbc.2021.101031_bib42","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1136\/gut.2005.072231","article-title":"Relation between viral fitness and immune escape within the hepatitis C virus protease","volume":"55","author":"S\u00f6derholm","year":"2006","journal-title":"Gut"},{"key":"10.1016\/j.jbc.2021.101031_bib43","doi-asserted-by":"crossref","DOI":"10.1128\/mSphereDirect.00554-17","article-title":"Stability of the influenza virus hemagglutinin protein correlates with evolutionary dynamics","volume":"3","author":"Klein","year":"2018","journal-title":"mSphere"},{"key":"10.1016\/j.jbc.2021.101031_bib44","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1080\/14760584.2017.1306441","article-title":"Influence of protein fold stability on immunogenicity and its implications for vaccine design","volume":"16","author":"Scheiblhofer","year":"2017","journal-title":"Expert Rev. Vaccines"},{"key":"10.1016\/j.jbc.2021.101031_bib45","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003042","article-title":"Rapid antigen processing and presentation of a protective and immunodominant HLA-B\u221727-restricted hepatitis C virus-specific CD8+ T-cell epitope","volume":"8","author":"Schmidt","year":"2012","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2021.101031_bib46","doi-asserted-by":"crossref","first-page":"12098","DOI":"10.1128\/JVI.01860-14","article-title":"Increased replicative fitness can lead to decreased drug sensitivity of hepatitis C virus","volume":"88","author":"Sheldon","year":"2014","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.jbc.2021.101031_bib47","doi-asserted-by":"crossref","first-page":"W382","DOI":"10.1093\/nar\/gki387","article-title":"The FoldX web server: An online force field","volume":"33","author":"Schymkowitz","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2021.101031_bib48","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1016\/S0969-2126(00)80025-8","article-title":"Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase","volume":"7","author":"Yao","year":"1999","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2021.101031_bib49","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1002\/jcc.20291","article-title":"GROMACS: Fast, flexible, and free","volume":"26","author":"van der Spoel","year":"2005","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.jbc.2021.101031_bib50","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1002\/prot.21123","article-title":"Comparison of multiple AMBER force fields and development of improved protein backbone parameters","volume":"65","author":"Hornak","year":"2006","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2021.101031_bib51","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0121114","article-title":"Comparing molecular dynamics force fields in the essential subspace","volume":"10","author":"Mart\u00edn-Garc\u00eda","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2021.101031_bib52","doi-asserted-by":"crossref","first-page":"9020","DOI":"10.1021\/jp8001614","article-title":"Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations","volume":"112","author":"Joung","year":"2008","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.jbc.2021.101031_bib53","article-title":"Canonical sampling through velocity rescaling","volume":"126","author":"Bussi","year":"2007","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.jbc.2021.101031_bib54","doi-asserted-by":"crossref","first-page":"7182","DOI":"10.1063\/1.328693","article-title":"Polymorphic transitions in single crystals: A new molecular dynamics method","volume":"52","author":"Parrinello","year":"1981","journal-title":"J.\u00a0Appl. Phys."},{"key":"10.1016\/j.jbc.2021.101031_bib55","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1080\/08927028808080941","article-title":"A\u00a0leap-frog algorithm for stochastic dynamics","volume":"1","author":"Van Gunsteren","year":"1988","journal-title":"Mol. Simul."},{"key":"10.1016\/j.jbc.2021.101031_bib56","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: An N\u00b7log(N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.jbc.2021.101031_bib57","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1021\/ct700200b","article-title":"P-LINCS:\u2009 A parallel linear constraint solver for molecular simulation","volume":"4","author":"Hess","year":"2008","journal-title":"J.\u00a0Chem. Theory Comput."},{"key":"10.1016\/j.jbc.2021.101031_bib58","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.tibs.2011.01.002","article-title":"Analyzing and visualizing residue networks of protein structures","volume":"36","author":"Doncheva","year":"2011","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jbc.2021.101031_bib59","doi-asserted-by":"crossref","first-page":"2310","DOI":"10.1073\/pnas.0510727103","article-title":"Production of infectious genotype 1a hepatitis C virus (Hutchinson strain) in cultured human hepatoma cells","volume":"103","author":"Yi","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101031_bib60","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1002\/jmv.20302","article-title":"Genetic heterogeneity of the NS3 protease gene in hepatitis C virus genotype 1 from untreated infected patients","volume":"75","author":"Vallet","year":"2005","journal-title":"J.\u00a0Med. Virol."},{"key":"10.1016\/j.jbc.2021.101031_bib61","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1093\/molbev\/msp259","article-title":"SeaView version\u00a04:\u00a0A\u00a0multiplatform graphical user interface for sequence alignment and phylogenetic tree building","volume":"27","author":"Gouy","year":"2010","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.jbc.2021.101031_bib62","doi-asserted-by":"crossref","first-page":"20986","DOI":"10.1073\/pnas.1006370107","article-title":"Drug resistance against HCV NS3\/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding","volume":"107","author":"Romano","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925821008334?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925821008334?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T16:34:47Z","timestamp":1762187687000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925821008334"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,9]]},"references-count":62,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2021,9]]}},"alternative-id":["S0021925821008334"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101031","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2021,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Epistatic interactions promote persistence of NS3-Q80K in\u00a0HCV infection by compensating for protein folding instability","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101031","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"101031"}}