Zobrazit více v PubMed
Gates B. [Video File]. Ted Talk2015 The Next Outbreak? We’re Not Ready. [(accessed on 29 December 2020)]; Available online: https://www.ted.com/talks/bill_gates_the_next_outbreak_we_re_not_ready?language=dz.
Commission WMH . Report of Clustering Pneumonia of Unknown Etiology in Wuhan City. Commission WMH; Wuhan, China: 2020.
Zhu N., Zhang D., Wang W., Li X., Yang B., Song J., Zhao X., Huang B., Shi W., Lu R., et al. A Novel Coronavirus from Patients with Pneumonia in China, 2019. N. Engl. J. Med. 2020;382:727–733. doi: 10.1056/NEJMoa2001017.
PubMed
DOI
PMC
Lai C.-C., Wang C.-Y., Wang Y.-H., Hsueh S.-C., Ko W.-C., Hsueh P.-R. Global epidemiology of coronavirus disease 2019 (COVID-19): Disease incidence, daily cumulative index, mortality, and their association with country healthcare resources and economic status. Int. J. Antimicrob. Agents. 2020;55:105946. doi: 10.1016/j.ijantimicag.2020.105946.
PubMed
DOI
PMC
Coronaviridae Study Group of the International Committee on Taxonomy of V The species Severe acute respiratory syndrome-related coronavirus: Classifying 2019-nCoV and naming it SARS-CoV-2. Nat. Microbiol. 2020;5:536–544. doi: 10.1038/s41564-020-0695-z.
PubMed
DOI
PMC
Wu J., Feng C.L., Xian X.Y., Qiang J., Zhang J., Mao Q.X., Kong S.F., Chen Y.C., Pan J.P. Novel coronavirus pneumonia (COVID-19) CT distribution and sign features. Zhonghua Jie He He Hu Xi Za Zhi. 2020;43:E030.
PubMed
Zhou P., Yang X.-L., Wang X.-G., Hu B., Zhang L., Zhang W., Si H.-R., Zhu Y., Li B., Huang C.-L., et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020;579:270–273. doi: 10.1038/s41586-020-2012-7.
PubMed
DOI
PMC
Cardenas-Conejo Y., Linan-Rico A., Garcia-Rodriguez D.A., Centeno-Leija S., Serrano-Posada H. An exclusive 42 amino acid signature in pp1ab protein provides insights into the evolutive history of the 2019 novel human-pathogenic coronavirus (SARS-CoV-2) J. Med. Virol. 2020;92:688–692. doi: 10.1002/jmv.25758.
PubMed
DOI
PMC
Chan C.-M., Tsoi H., Chan W.-M., Zhai S., Wong C.-O., Yao X., Chan W.Y., Tsui S.K.W., Chan H.Y.E. The ion channel activity of the SARS-coronavirus 3a protein is linked to its pro-apoptotic function. Int. J. Biochem. Cell Biol. 2009;41:2232–2239. doi: 10.1016/j.biocel.2009.04.019.
PubMed
DOI
PMC
Kim D., Lee J.Y., Yang J.S., Kim J.W., Kim V.N., Chang H. The Architecture of SARS-CoV-2 Transcriptome. Cell. 2020;181:914–921.e10. doi: 10.1016/j.cell.2020.04.011.
PubMed
DOI
PMC
Pathak K.B., Nagy P.D. Defective Interfering RNAs: Foes of Viruses and Friends of Virologists. Viruses. 2009;1:895–919. doi: 10.3390/v1030895.
PubMed
DOI
PMC
Robertson M.P., Igel H., Baertsch R., Haussler D., Ares M., Scott W.G. The Structure of a Rigorously Conserved RNA Element within the SARS Virus Genome. PLoS Biol. 2004;3:e5. doi: 10.1371/journal.pbio.0030005.
PubMed
DOI
PMC
Baranov P.V., Henderson C.M., Anderson C.B., Gesteland R.F., Atkins J.F., Howard M.T. Programmed ribosomal frameshifting in decoding the SARS-CoV genome. Virology. 2005;332:498–510. doi: 10.1016/j.virol.2004.11.038.
PubMed
DOI
PMC
Ketteler R. On programmed ribosomal frameshifting: The alternative proteomes. Front. Genet. 2012;3:242. doi: 10.3389/fgene.2012.00242.
PubMed
DOI
PMC
Jacks T., Power M.D., Masiarz F.R., Luciw P.A., Barr P.J., Varmus H.E. Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nat. Cell Biol. 1988;331:280–283. doi: 10.1038/331280a0.
PubMed
DOI
Jagger B.W., Wise H.M., Kash J.C., Walters K.-A., Wills N.M., Xiao Y.-L., Dunfee R.L., Schwartzman L.M., Ozinsky A., Bell G.L., et al. An Overlapping Protein-Coding Region in Influenza A Virus Segment 3 Modulates the Host Response. Science. 2012;337:199–204. doi: 10.1126/science.1222213.
PubMed
DOI
PMC
Herold J., Siddell S.G. An ‘elaborated’ pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA. Nucleic Acids Res. 1993;21:5838–5842. doi: 10.1093/nar/21.25.5838.
PubMed
DOI
PMC
Brierley I., Rolley N.J., Jenner A.J., Inglis S.C. Mutational analysis of the RNA pseudoknot component of a coronavirus ribosomal frameshifting signal. J. Mol. Biol. 1991;220:889–902. doi: 10.1016/0022-2836(91)90361-9.
PubMed
DOI
PMC
Brierley I., Jenner A.J., Inglis S.C. Mutational analysis of the “slippery-sequence” component of a coronavirus ribosomal frameshifting signal. J. Mol. Biol. 1992;227:463–479. doi: 10.1016/0022-2836(92)90901-U.
PubMed
DOI
PMC
Liphardt J., Napthine S., Kontos H., Brierley I. Evidence for an RNA pseudoknot loop-helix interaction essential for efficient −1 ribosomal frameshifting. J. Mol. Biol. 1999;288:321–335. doi: 10.1006/jmbi.1999.2689.
PubMed
DOI
PMC
Jonassen C.M., OJonassen T., Grinde B. A common RNA motif in the 3′ end of the genomes of astroviruses, avian infectious bronchitis virus and an equine rhinovirus. J. Gen. Virol. 1998;79:715–718. doi: 10.1099/0022-1317-79-4-715.
PubMed
DOI
Maran T. Mimicry and Meaning: Structure and Semiosis of Biological Mimicry. Springer International Publishing; Berlin/Heidelberg, Germany: 2017.
Ariza-Mateos A., Gómez J. Viral tRNA Mimicry from a Biocommunicative Perspective. Front. Microbiol. 2017;8:2395. doi: 10.3389/fmicb.2017.02395.
PubMed
DOI
PMC
Peng Q., Peng R., Yuan B., Zhao J., Wang M., Wang X. Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2. Cell Rep. 2020;31:107774. doi: 10.1016/j.celrep.2020.107774.
PubMed
DOI
PMC
Plant E.P., Pérez-Alvarado G.C., Jacobs J.L., Mukhopadhyay B., Hennig M., Dinman J.D. A Three-Stemmed mRNA Pseudoknot in the SARS Coronavirus Frameshift Signal. PLoS Biol. 2005;3:e172. doi: 10.1371/journal.pbio.0030172.
PubMed
DOI
PMC
Brierley I., Digard P., Inglis S.C. Characterization of an efficient coronavirus ribosomal frameshifting signal: Requirement for an RNA pseudoknot. Cell. 1989;57:537–547. doi: 10.1016/0092-8674(89)90124-4.
PubMed
DOI
PMC
Kilstrup M. Naturalizing semiotics: The triadic sign of Charles Sanders Peirce as a systems property. Prog. Biophys. Mol. Biol. 2015;119:563–575. doi: 10.1016/j.pbiomolbio.2015.08.013.
PubMed
DOI
Dana A., Tuller T. Determinants of Translation Elongation Speed and Ribosomal Profiling Biases in Mouse Embryonic Stem Cells. PLoS Comput. Biol. 2012;8:e1002755. doi: 10.1371/journal.pcbi.1002755.
PubMed
DOI
PMC
Bai Y., Yao L., Wei T., Tian F., Jin D.Y., Chen L., Wang M. Presumed Asymptomatic Carrier Transmission of COVID-19. JAMA. 2020;323:1406–1407. doi: 10.1001/jama.2020.2565.
PubMed
DOI
PMC
Berman H.M., Westbrook J., Feng Z., Gilliland G., Bhat T.N., Weissig H., Shindyalov I.N., Bourne P.E. The Protein Data Bank. Nucleic Acids Res. 2000;28:235–242. doi: 10.1093/nar/28.1.235.
PubMed
DOI
PMC
Corum J., Zimmer C. Bad News Wrapped in Protein: Inside the Coronavirus Genome. The New York Times. Apr 3, 2020.
Schubert K., Karousis E.D., Jomaa A., Scaiola A., Echeverria B., Gurzeler L.A. SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation. Nat. Struct. Mol. Biol. 2020;27:959–966. doi: 10.1038/s41594-020-0511-8.
PubMed
DOI
Benedetti F., Snyder G.A., Giovanetti M., Angeletti S., Gallo R.C., Ciccozzi M. Emerging of a SARS-CoV-2 viral strain with a deletion in nsp1. J. Transl. Med. 2020;18:329. doi: 10.1186/s12967-020-02507-5.
PubMed
DOI
PMC
Angeletti S., Benvenuto D., Bianchi M., Giovanetti M., Pascarella S., Ciccozzi M. COVID-2019: The role of the nsp2 and nsp3 in its pathogenesis. J. Med. Virol. 2020;92:584–588. doi: 10.1002/jmv.25719.
PubMed
DOI
PMC
Santerre M., Arjona S.P., Allen C.N., Shcherbik N., Sawaya B.E. Why do SARS-CoV-2 NSPs rush to the ER? J. Neurol. 2020;1:1–10. doi: 10.1007/s00415-020-10197-8.
PubMed
DOI
PMC
Khan M.T., Zeb M.T., Ahsan H., Ahmed A., Ali A., Akhtar K. SARS-CoV-2 nucleocapsid and Nsp3 binding: An in silico study. Arch. Microbiol. 2020;4:1–8. doi: 10.1007/s00203-020-01998-6.
PubMed
DOI
PMC
Beachboard D.C., Anderson-Daniels J.M., Denison M.R. Mutations across Murine Hepatitis Virus nsp4 Alter Virus Fitness and Membrane Modifications. J. Virol. 2014;89:2080–2089. doi: 10.1128/JVI.02776-14.
PubMed
DOI
PMC
Hagemeijer M.C., Ulasli M., Vonk A.M., Reggiori F., Rottier P.J.M., De Haan C.A.M. Mobility and Interactions of Coronavirus Nonstructural Protein 4. J. Virol. 2011;85:4572–4577. doi: 10.1128/JVI.00042-11.
PubMed
DOI
PMC
Stobart C.C., Sexton N.R., Munjal H., Lu X., Molland K.L., Tomar S., Mesecar A.D., Denison M.R. Chimeric Exchange of Coronavirus nsp5 Proteases (3CLpro) Identifies Common and Divergent Regulatory Determinants of Protease Activity. J. Virol. 2013;87:12611–12618. doi: 10.1128/JVI.02050-13.
PubMed
DOI
PMC
Yang H., Xie W., Xue X., Yang K., Ma J., Liang W. Design of wide-spectrum inhibitors targeting coronavirus main proteases. PLoS Biol. 2005;3:e324.
PubMed
PMC
Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R. Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs. Science. 2003;300:1763–1767. doi: 10.1126/science.1085658.
PubMed
DOI
Muramatsu T., Takemoto C., Kim Y.T., Wang H., Nishii W., Terada T. SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity. Proc. Natl. Acad. Sci. USA. 2016;113:12997–13002. doi: 10.1073/pnas.1601327113.
PubMed
DOI
PMC
Oostra M., Hagemeijer M.C., Van Gent M., Bekker C.P.J., Lintelo E.G.T., Rottier P.J.M., De Haan C.A.M. Topology and Membrane Anchoring of the Coronavirus Replication Complex: Not All Hydrophobic Domains of nsp3 and nsp6 Are Membrane Spanning. J. Virol. 2008;82:12392–12405. doi: 10.1128/JVI.01219-08.
PubMed
DOI
PMC
Falke S. Ph.D. Thesis. Staats- und Universitätsbibliothek; Hamburg, Germany: 2014. Coronaviral Polyprotein Nsp7-10: Proteolytic Processing and Dynamic Interactions within the Transcriptase/Replicase Complex.
Krichel B., Falke S., Hilgenfeld R., Redecke L., Uetrecht C. Processing of the SARS-CoV pp1a/ab nsp7-10 region. Biochem. J. 2020;477:1009–1019. doi: 10.1042/BCJ20200029.
PubMed
DOI
PMC
Subissi L., Posthuma C.C., Collet A., Zevenhoven-Dobbe J.C., Gorbalenya A.E., Decroly E., Snijder E.J., Canard B., Imbert I. One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities. Proc. Natl. Acad. Sci. USA. 2014;111:E3900–E3909. doi: 10.1073/pnas.1323705111.
PubMed
DOI
PMC
Littler D.R., Gully B.S. Crystal structure on the SARS-CoV-2 non-structural protein 9, Nsp9. iScience. 2020;7:101258. doi: 10.1016/j.isci.2020.101258.
PubMed
DOI
PMC
Egloff M.-P., Ferron F., Campanacci V., Longhi S., Rancurel C., Dutartre H., Snijder E.J., Gorbalenya A.E., Cambillau C., Canard B. The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world. Proc. Natl. Acad. Sci. USA. 2004;101:3792–3796. doi: 10.1073/pnas.0307877101.
PubMed
DOI
PMC
Sutton G., Fry E., Carter L., Sainsbury S., Walter T., Nettleship J. The nsp9 replicase protein of SARS-coronavirus, structure and functional insights. Structure. 2004;12:341–353. doi: 10.1016/j.str.2004.01.016.
PubMed
DOI
PMC
Miknis Z.J., Donaldson E.F., Umland T.C., Rimmer R.A., Baric R.S., Schultz L.W. Severe Acute Respiratory Syndrome Coronavirus nsp9 Dimerization Is Essential for Efficient Viral Growth. J. Virol. 2009;83:3007–3018. doi: 10.1128/JVI.01505-08.
PubMed
DOI
PMC
Chandel V., Sharma P.P., Raj S., Choudhari R., Rathi B., Kesari K.K. Structure-based drug repurposing for targeting Nsp9 replicase and spike proteins of severe acute respiratory syndrome coronavirus 2. J. Biomol. Struct. Dyn. 2020;2020:1–14. doi: 10.1080/07391102.2020.1811773.
PubMed
DOI
PMC
Bouvet M., Debarnot C., Imbert I., Selisko B., Snijder E.J., Canard B. In vitro reconstitution of SARS-coronavirus mRNA cap methylation. PLoS Pathog. 2010;6:e1000863. doi: 10.1371/annotation/a0dde376-2eb1-4ce3-8887-d29f5ba6f162.
PubMed
DOI
PMC
Lugari A., Betzi S., Decroly E., Bonnaud E., Hermant A., Guillemot J.-C., Debarnot C., Borg J.-P., Bouvet M., Canard B., et al. Molecular Mapping of the RNA Cap 2′-O-Methyltransferase Activation Interface between Severe Acute Respiratory Syndrome Coronavirus nsp10 and nsp16. J. Biol. Chem. 2010;285:33230–33241. doi: 10.1074/jbc.M110.120014.
PubMed
DOI
PMC
Bouvet M., Imbert I., Subissi L., Gluais L., Canard B., Decroly E. RNA 3′-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex. Proc. Natl. Acad. Sci. USA. 2012;109:9372–9377. doi: 10.1073/pnas.1201130109.
PubMed
DOI
PMC
Sheikh J.A., Singh J., Singh H., Jamal S., Khubaib M., Kohli S. Emerging genetic diversity among clinical isolates of SARS-CoV-2: Lessons for today. Infect Genet Evol. 2020;84:104330. doi: 10.1016/j.meegid.2020.104330.
PubMed
DOI
PMC
Agostini M.L., Andres E.L., Sims A.C., Graham R.L., Sheahan T.P., Lu X., Smith E.C., Case J.B., Feng J.Y., Jordan R., et al. Coronavirus Susceptibility to the Antiviral Remdesivir (GS-5734) Is Mediated by the Viral Polymerase and the Proofreading Exoribonuclease. mBio. 2018;9:e00221-18. doi: 10.1128/mBio.00221-18.
PubMed
DOI
PMC
Gordon C.J., Tchesnokov E.P., Woolner E., Perry J.K., Feng J.Y., Porter D.P., Götte M. Remdesivir is a direct-acting antiviral that inhibits RNA-dependent RNA polymerase from severe acute respiratory syndrome coronavirus 2 with high potency. J. Biol. Chem. 2020;295:6785–6797. doi: 10.1074/jbc.RA120.013679.
PubMed
DOI
PMC
Mirza M.U., Froeyen M. Structural elucidation of SARS-CoV-2 vital proteins: Computational methods reveal potential drug candidates against main protease, Nsp12 polymerase and Nsp13 helicase. J. Pharm. Anal. 2020;10:320–328. doi: 10.1016/j.jpha.2020.04.008.
PubMed
DOI
PMC
Neogi U., Hill K.J., Ambikan A.T., Heng X., Quinn T.P., Byrareddy S.N. Feasibility of Known RNA Polymerase Inhibitors as Anti-SARS-CoV-2 Drugs. Pathogens. 2020;9:320. doi: 10.3390/pathogens9050320.
PubMed
DOI
PMC
Shannon A., Le N.T., Selisko B., Eydoux C., Alvarez K., Guillemot J.C. Remdesivir and SARS-CoV-2: Structural requirements at both nsp12 RdRp and nsp14 Exonuclease active-sites. Antivir. Res. 2020;178:104793. doi: 10.1016/j.antiviral.2020.104793.
PubMed
DOI
PMC
Frieman M., Basu D., Matthews K., Taylor J., Jones G., Pickles R. Yeast based small molecule screen for inhibitors of SARS-CoV. PLoS ONE. 2011;6:e28479. doi: 10.1371/journal.pone.0028479.
PubMed
DOI
PMC
Gordon D.E., Jang G.M., Bouhaddou M., Xu J., Obernier K., White K.M. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature. 2020;583:459–468. doi: 10.1038/s41586-020-2286-9.
PubMed
DOI
PMC
Sinha S.K., Shakya A., Prasad S.K., Singh S., Gurav N.S., Prasad R.S. An in-silico evaluation of different Saikosaponins for their potency against SARS-CoV-2 using NSP15 and fusion spike glycoprotein as targets. J. Biomol. Struct. Dyn. 2020:1–12. doi: 10.1080/07391102.2020.1762741.
PubMed
DOI
PMC
Wang Y., Sun Y., Wu A., Xu S., Pan R., Zeng C. Coronavirus nsp10/nsp16 Methyltransferase Can Be Targeted by nsp10-Derived Peptide In Vitro and In Vivo To Reduce Replication and Pathogenesis. J. Virol. 2015;89:8416–8427. doi: 10.1128/JVI.00948-15.
PubMed
DOI
PMC
Issa E., Merhi G., Panossian B., Salloum T., Tokajian S. SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis. mSystems. 2020;5:e00266–e00320. doi: 10.1128/mSystems.00266-20.
PubMed
DOI
PMC
Frieman M., Yount B., Heise M., Kopecky-Bromberg S.A., Palese P., Baric R. Severe Acute Respiratory Syndrome Coronavirus ORF6 Antagonizes STAT1 Function by Sequestering Nuclear Import Factors on the Rough Endoplasmic Reticulum/Golgi Membrane. J. Virol. 2007;81:9812–9824. doi: 10.1128/JVI.01012-07.
PubMed
DOI
PMC
Taylor J.K., Coleman C.M., Postel S., Sisk J.M., Bernbaum J.G., Venkataraman T., Sundberg E.J., Frieman M.B. Severe Acute Respiratory Syndrome Coronavirus ORF7a Inhibits Bone Marrow Stromal Antigen 2 Virion Tethering through a Novel Mechanism of Glycosylation Interference. J. Virol. 2015;89:11820–11833. doi: 10.1128/JVI.02274-15.
PubMed
DOI
PMC
Holland L.A., Kaelin E.A., Maqsood R., Estifanos B., Wu L.I., Varsani A. An 81 nucleotide deletion in SARS-CoV-2 ORF7a identified from sentinel surveillance in Arizona (Jan-Mar 2020) J. Virol. 2020;94:e00711–e00720. doi: 10.1128/JVI.00711-20.
PubMed
DOI
PMC
Pekosz A., Schaecher S.R., Diamond M.S., Fremont D.H., Sims A.C., Baric R.S. Structure, expression, and intracellular localization of the SARS-CoV accessory proteins 7a and 7b. Adv. Exp. Med. Biol. 2006;581:115–120.
PubMed
PMC
Oostra M., De Haan C.A.M., Rottier P.J.M. The 29-Nucleotide Deletion Present in Human but Not in Animal Severe Acute Respiratory Syndrome Coronaviruses Disrupts the Functional Expression of Open Reading Frame 8. J. Virol. 2007;81:13876–13888. doi: 10.1128/JVI.01631-07.
PubMed
DOI
PMC
Cagliani R., Forni D., Clerici M., Sironi M. Computational Inference of Selection Underlying the Evolution of the Novel Coronavirus, Severe Acute Respiratory Syndrome Coronavirus 2. J. Virol. 2020;94 doi: 10.1128/JVI.00411-20.
PubMed
DOI
PMC
Chan J., Kok K.-H., Zhu Z., Chu H., To K.K.-W., Yuan S., Yuen K.-Y. Genomic characterization of the 2019 novel human-pathogenic coronavirus isolated from a patient with atypical pneumonia after visiting Wuhan. Emerg. Microbes Infect. 2020;9:221–236. doi: 10.1080/22221751.2020.1719902.
PubMed
DOI
PMC
De Groot R.J. Virus Taxonomy. In: Press E.A., editor. Ninth Report of the International Committee on Taxonomy of Viruses. Elsevier; Washington, DC, USA: 2012. pp. 806–828.
Konrad R., Eberle U., Dangel A., Treis B., Berger A., Bengs K. Rapid establishment of laboratory diagnostics for the novel coronavirus SARS-CoV-2 in Bavaria, Germany, February 2020. Euro Surveill. 2020;25:2000173. doi: 10.2807/1560-7917.ES.2020.25.9.2000173.
PubMed
DOI
PMC
Li F. Structure, Function, and Evolution of Coronavirus Spike Proteins. Annu. Rev. Virol. 2016;3:237–261. doi: 10.1146/annurev-virology-110615-042301.
PubMed
DOI
PMC
Vankadari N., Wilce J.A. Emerging WuHan (COVID-19) coronavirus: Glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26. Emerg. Microbes Infect. 2020;9:601–604. doi: 10.1080/22221751.2020.1739565.
PubMed
DOI
PMC
Wan Y., Shang J., Graham R., Baric R.S., Li F. Receptor Recognition by the Novel Coronavirus from Wuhan: An Analysis Based on Decade-Long Structural Studies of SARS Coronavirus. J. Virol. 2020;94 doi: 10.1128/JVI.00127-20.
PubMed
DOI
PMC
Coutard B., Valle C., De Lamballerie X., Canard B., Seidah N., Decroly E. The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade. Antivir. Res. 2020;176:104742. doi: 10.1016/j.antiviral.2020.104742.
PubMed
DOI
PMC
Korber B., Fischer W.M., Gnanakaran S., Yoon H., Theiler J., Abfalterer W. Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus. Cell. 2020;182:812–827.e19. doi: 10.1016/j.cell.2020.06.043.
PubMed
DOI
PMC
Rambaut A., Loman N., Pybus O., Barclay W., Barrett J., Carabelli A. Preliminary genomic characterisation of an emergent SARS-CoV-2 lineage in the UK defined by a novel set of spike mutations. [(accessed on 15 December 2020)];Genom. Epidemiol. 2020 Available online: https://virological.org/t/preliminary-genomic-characterisation-of-an-emergent-sars-cov-2-lineage-in-the-uk-defined-by-a-novel-set-of-spike-mutations/563.
Kandeel M., Ibrahim A.A., Fayez M., Al-Nazawi M. From SARS and MERS CoVs to SARS-CoV-2: Moving toward more biased codon usage in viral structural and nonstructural genes. J. Med. Virol. 2020;92:660–666. doi: 10.1002/jmv.25754.
PubMed
DOI
PMC
Ruch T.R., Machamer C.E. The Coronavirus E Protein: Assembly and Beyond. Viruses. 2012;4:363–382. doi: 10.3390/v4030363.
PubMed
DOI
PMC
Goh G.K.-M., Dunker A.K., Foster J.A., Uversky V. HIV Vaccine Mystery and Viral Shell Disorder. Biomolecules. 2019;9:178. doi: 10.3390/biom9050178.
PubMed
DOI
PMC
Gralinski L.E., Menachery V.D. Return of the Coronavirus: 2019-nCoV. Viruses. 2020;12:135. doi: 10.3390/v12020135.
PubMed
DOI
PMC
Menachery V.D., Graham R.L., Baric R. Jumping species—A mechanism for coronavirus persistence and survival. Curr. Opin. Virol. 2017;23:1–7. doi: 10.1016/j.coviro.2017.01.002.
PubMed
DOI
PMC
McBride R., Van Zyl M., Fielding B.C. The Coronavirus Nucleocapsid Is a Multifunctional Protein. Viruses. 2014;6:2991–3018. doi: 10.3390/v6082991.
PubMed
DOI
PMC
Chechetkin V.R., Lobzin V.V. Ribonucleocapsid assembly/packaging signals in the genomes of the coronaviruses SARS-CoV and SARS-CoV-2: Detection, comparison and implications for therapeutic targeting. J. Biomol. Struct. Dyn. 2020:1–15. doi: 10.1080/07391102.2020.1815581.
PubMed
DOI
PMC
Srinivasan S., Cui H., Gao Z., Liu M., Lu S., Mkandawire W. Structural Genomics of SARS-CoV-2 Indicates Evolutionary Conserved Functional Regions of Viral Proteins. Viruses. 2020;12:360. doi: 10.3390/v12040360.
PubMed
DOI
PMC
Saikatendu K.S., Joseph J.S., Subramanian V., Clayton T., Griffith M., Moy K., Velasquez J., Neuman B.W., Buchmeier M.J., Stevens R.C., et al. Structural Basis of Severe Acute Respiratory Syndrome Coronavirus ADP-Ribose-1″-Phosphate Dephosphorylation by a Conserved Domain of nsP3. Structure. 2005;13:1665–1675. doi: 10.1016/j.str.2005.07.022.
PubMed
DOI
PMC