Szekely J, Mongkolprasert J, Jeayodae N, Senorit C, Chaimuti P, Swangphon P, et al. Development, analytical, and clinical evaluation of rapid immunochromatographic antigen test for SARS-CoV-2 variants detection. Diagnostics (Basel). 2022;12:381.
Suthar TR, Gaikwad ST, Suthar AD. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and coronavirus disease-2019 (COVID-19): a review. Int J Curr Microbiol Appl Sci. 2020;9:3201–8.
Ma W, Yang J, Fu H, Su C, Yu C, Wang Q, et al. Genomic perspectives on the emerging SARS-CoV-2 omicron variant. Genomics Proteomics Bioinform. 2019. https://doi.org/10.1016/j.gpb.2022.01.001.
Aleem A, Samad ABA, Slenker AK. Emerging variants of SARS-CoV-2 and novel therapeutics against coronavirus (COVID-19). In: StatPearls. Treasure Island, StatPearls Publishing ; 2022.
Mohapatra RK, Kandi V, Verma S, Dhama K. Challenges of the Omicron (B.1.1.529) variant and its lineages: a global perspective. ChemBioChem. 2022;23:e202200059.
Tompa DR, Immanuel A, Srikanth S, Kadhirvel S. Trends and strategies to combat viral infections: a review on FDA approved antiviral drugs. Int J Biol Macromol. 2021;172:524–41.
El-Shabasy RM, Nayel MA, Taher MM, Abdelmonem R, Shoueir KR, Kenawy ER. Three waves changes, new variant strains, and vaccination effect against COVID-19 pandemic. Int J Biol Macromol. 2022;204:161–8.
Hassan SS, Lundstrom K, Barh D, Silva RJS, Andrade BS, Azevedo V, et al. Implications derived from S-protein variants of SARS-CoV-2 from six continents. Int J Biol Macromol. 2021;191:934–55.
Hassan SS, Lundstrom K, Serrano-Aroca Á, Adadi P, Aljabali A, Redwan E, et al. Emergence of unique SARS-CoV-2 ORF10 variants and their impact on protein structure and function. Int J Biol Macromol. 2022;194:128–43.
Souza PFN, Mesquita FP, Amaral JL, Landim PGC, Lima KRP, Costa MB, et al. The spike glycoprotein of SARS-CoV-2: a review of how mutations of spike glycoproteins have driven the emergence of variants with high transmissibility and immune escape. Int J Biol Macromol. 2022;208:105–25.
Cai Q, Mu J, Lei Y, Ge J, Aryee AA, Zhang X, et al. Simultaneous detection of the spike and nucleocapsid proteins from SARS-CoV-2 based on ultrasensitive single molecule assays. Anal Bioanal Chem. 2021;413:4645–54.
Zheng J. SARS-CoV-2: an emerging coronavirus that causes a global threat. Int J Biol Sci. 2020;16:1678–85.
Awadasseid A, Wu Y, Tanaka Y, Zhang W. Current advances in the development of SARS-CoV-2 vaccines. Int J Biol Sci. 2021;17:8–19.
Krammer F. SARS-CoV-2 vaccines in development. Nature. 2020;586:516–27.
Li C, Zhan W, Yang Z, Tu C, Hu G, Zhang X, et al. Broad neutralization of SARS-CoV-2 variants by an inhalable bispecific single-domain antibody. Cell. 2022;185:1389-401.e18.
Altmann DM, Boyton RJ. COVID-19 vaccination: the road ahead. Science. 2022;375:1127–32.
Zinzula L, Basquin J, Bohn S, Beck F, Klumpe S, Pfeifer G, et al. High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2. Biochem Biophys Res Commun. 2021;538:54–62.
Ahammad I, Lira SS. Designing a novel mRNA vaccine against SARS-CoV-2: an immunoinformatics approach. Int J Biol Macromol. 2020;162:820–37.
Dong Y, Dai T, Wei Y, Zhang L, Zheng M, Zhou F. A systematic review of SARS-CoV-2 vaccine candidates. Sig Transduct Target Ther. 2020;5:237.
Supekar NT, Shajahan A, Gleinich AS, Rouhani DS, Heiss C, Chapla DG, et al. Variable posttranslational modifications of severe acute respiratory syndrome coronavirus 2 nucleocapsid protein. Glycobiology. 2021;31:1080–92.
Chang CK, Hou MH, Chang CF, Hsiao CD, Huang TH. The SARS coronavirus nucleocapsid protein–forms and functions. Antiviral Res. 2014;103:39–50.
Burbelo PD, Riedo FX, Morishima C, Rawlings S, Smith D, Das S, et al. Detection of nucleocapsid antibody to SARS-CoV-2 is more sensitive than antibody to spike protein in COVID-19 patients. medRxiv 2020; https://doi.org/10.1101/2020.04.20.20071423.
Yasui F, Kai C, Kitabatake M, Inoue S, Yoneda M, Yokochi S, et al. Prior immunization with severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) nucleocapsid protein causes severe pneumonia in mice infected with SARS-CoV. J Immunol. 2008;181:6337–48.
Ihling C, Tänzler D, Hagemann S, Kehlen A, Hüttelmaier S, Arlt C, et al. Mass spectrometric identification of SARS-CoV-2 proteins from gargle solution samples of COVID-19 patients. J Proteome Res. 2020;19:4389–92.
Gouveia D, Miotello G, Gallais F, Gaillard JC, Debroas S, Bellanger L, et al. Proteotyping SARS-CoV-2 virus from nasopharyngeal swabs: a proof-of-concept focused on a 3 min mass spectrometry window. J Proteome Res. 2020;19:4407–16.
Baggen J, Vanstreels E, Jansen S, Daelemans D. Cellular host factors for SARS-CoV-2 infection. Nat Microbiol. 2021;6:1219–32.
Yao H, Song Y, Chen Y, Wu N, Xu J, Sun C, et al. Molecular architecture of the SARS-CoV-2 virus. Cell. 2020;183:730-8.e13.
Peng Y, Du N, Lei Y, Dorje S, Qi J, Luo T, et al. Structures of the SARS-CoV-2 nucleocapsid and their perspectives for drug design. EMBO J. 2020;39: e105938.
Michel CJ, Mayer C, Poch O, Thompson JD. Characterization of accessory genes in coronavirus genomes. Virol J. 2020;17:131.
Matsuo T. Viewing SARS-CoV-2 nucleocapsid protein in terms of molecular flexibility. Biology. 2021;10:454.
Bianchi M, Borsetti A, Ciccozzi M, Pascarella S. SARS-Cov-2 ORF3a: mutability and function. Int J Biol Macromol. 2021;170:820–6.
Hassan SS, Attrish D, Ghosh S, Choudhury PP, Uversky VN, Uhal BD, et al. Notable sequence homology of the ORF10 protein introspects the architecture of SARS-COV-2. Int J Biol Macromol. 2020;181:801–9.
Yan L, Ge J, Zheng L, Zhang Y, Gao Y, Wang T, et al. Cryo-EM structure of an extended SARS-CoV-2 replication and transcription complex reveals an intermediate state in cap synthesis. Cell. 2021;184:184-93.e10.
Jin Z, Du X, Xu Y, Deng Y, Liu M, Zhao Y, et al. Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors. Nature. 2020;582:289–93.
Gao X, Qin B, Chen P, Zhu K, Hou P, Wojdyla JA, et al. Crystal structure of SARS-CoV-2 papain-like protease. Acta Pharm Sin B. 2021;11:237–45.
Gao Y, Yan L, Huang Y, Liu F, Zhao Y, Cao L, et al. Structure of the RNA-dependent RNA polymerase from COVID-19 virus. Science. 2020;368:779–82.
Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell. 2020;181:281-92.e6.
Kang S, Yang M, Hong Z, Zhang L, Huang Z, Chen X, et al. Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites. Acta Pharm Sin B. 2020;10:1228–38.
V’Kovski P, Kratzel A, Steiner S, Stalder H, Thiel V. Coronavirus biology and replication: implications for SARS-CoV-2. Nat Rev Microbiol. 2021;19:155–70.
Bouback TA, Samad A, Nur SM, Abdullah-Al-Mamun M, Alam R, Hossen MS, et al. Spike protein recognizer receptor ACE2 targeted identification of potential natural antiviral drug candidates against SARS-CoV-2. Int J Biol Macromol. 2021;191:1114–25.
Souza PFN, Lopes FES, Amaral JL, Freitas CDT, Oliveira JTA. A molecular docking study revealed that synthetic peptides induced conformational changes in the structure of SARS-CoV-2 spike glycoprotein, disrupting the interaction with human ACE2 receptor. Int J Biol Macromol. 2020;164:66–76.
Letko M, Marzi A, Munster V. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses. Nat Microbiol. 2020;5:562–9.
Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020;181:271-80.e8.
Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature. 2020;581:215–20.
Shang J, Ye G, Shi K, Wan Y, Luo C, Aihara H, et al. Structural basis of receptor recognition by SARS-CoV-2. Nature. 2020;581:221–4.
留言 (0)