Results 21 to 30 of about 38,894 (153)
Targeting SARS-CoV-2 Nsp12/Nsp8 interaction interface with approved and investigational drugs: anin silicostructure-based approach [PDF]
, 2020 In this study, the Nsp12-Nsp8 complex of SARS-CoV-2 was targeted with structure-based and computer-aided drug design approach because of its vital role in viral replication.Turgut-Balık, Dilek, Ata, Oğuz, Turgut Balık, Didem, Uğurel, Erennur, İnci, Tuğba Gül, Mutlu, Özal, Turgut Balık, Dilek, Koçer, Sinem, Uğurel, Osman Mutluhan, Sarıyer, Emrah +9 morecore +3 more sourcesDevelopment of novel monoclonal antibodies against nsp12 of SARS-CoV-2
Virology Journal, 2022 AbstractA novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has caused a global pandemic of coronavirus disease 19. Coronaviruses, including SARS-CoV-2, use RNA-dependent RNA polymerase (RdRP) for viral replication and transcription.Mitsuhiro Machitani, Junko Takei, Mika K. Kaneko, Saori Ueki, Hirofumi Ohashi, Koichi Watashi, Yukinari Kato, Kenkichi Masutomi +7 moreopenaire +3 more sourcesRNA binding sites in NSP12 protein.
, 2023 The structure of SARS-CoV-2 replication-transcription complex indicated in the PDB ID:501 6XEZ (Whole-model, A) and the SARS-CoV-2 NSP12 (Small-model, B). (C) RMSD comparison of Whole-model and Small-model. (PPTX)Shiho Torii (12770667), Yong Dam Jeong (14846302), Kei Sato (493447), Rigel Suzuki (12770673), Kwang Su Kim (1960972), Jumpei Ito (761675), Hiroyuki Asakura (1617940), Teppei Shimamura (133856), Takasuke Fukuhara (673475), Yasuhisa Fujita (10344689), Shoya Iwanami (3945266), Kazuhisa Yoshimura (322429), Kenji Sadamasu (7438220), Jun Koseki (738263), Yoshiharu Matsuura (357989), Shingo Iwami (266092), Mami Nagashima (14846305) +16 morecore +2 more sourcesThe P323L substitution in the SARS-CoV-2 polymerase (NSP12) confers a selective advantage during infection
Genome Biology, 2023 Abstract Background The mutational landscape of SARS-CoV-2 varies at the dominant viral genome sequence and minor genomic variant population. During the COVID-19 pandemic, an early substitution in the genome was the D614G change in the spike protein, associated with an increase in transmissibility. Genomes with D614G are Goldswain, H., Dong, X., Penrice-Randal, R., Alruwaili, M., Shawli, G.T., Prince, T., Williamson, M.K., Raghwani, J., Randle, N., Jones, B., Donovan-Banfield, I., Salguero, F.J., Tree, J.A., Hall, Y., Hartley, C., Erdmann, M., Bazire, J., Jearanaiwitayakul, T., Semple, M.G., Openshaw, P.J.M., Baillie, J.K., Baillie, J.K., Semple, M.G., Openshaw, P.J.M., Carson, G., Alex, B., Andrikopoulos, P., Bach, B., Barclay, W.S., Bogaert, D., Chand, M., Chechi, K., Cooke, G.S., da Silva Filipe, A., de Silva, T., Docherty, A.B., dos Santos Correia, G., Dumas, M.-E., Dunning, J., Fletcher, T., Green, C.A., Greenhalf, W., Griffin, J.L., Gupta, R.K., Harrison, E.M., Hiscox, J.A., Ho, A.Y.W., Horby, P.W., Ijaz, S., Khoo, S., Klenerman, P., Law, A., Lewis, M.R., Liggi, S., Lim, W.S., Maslen, L., Mentzer, A.J., Merson, L., Meynert, A.M., Moore, S.C., Noursadeghi, M., Olanipekun, M., Osagie, A., Palmarini, M., Palmieri, C., Paxton, W.A., Pollakis, G., Price, N., Rambaut, A., Robertson, D.L., Russell, C.D., Sancho-Shimizu, V., Sands, C.J., Scott, J.T., Sigfrid, L., Solomon, T., Sriskandan, S., Stuart, D., Summers, C., Swann, O.V., Takats, Z., Takis, P., Tedder, R.S., Thompson, A.A.R., Thomson, E.C., Thwaites, R.S., Turtle, L.C.W., Zambon, M., Hardwick, H., Donohue, C., Griffiths, F., Oosthuyzen, W., Donegan, C., Spencer, R.G., Norman, L., Pius, R., Drake, T.M., Fairfield, C.J., Knight, S.R., Mclean, K.A., Murphy, D., Shaw, C.A., Dalton, J., Girvan, M., Saviciute, E., Roberts, S., Harrison, J., Marsh, L., Connor, M., Halpin, S., Jackson, C., Gamble, C., Plotkin, D., Lee, J., Leeming, G., Law, A., Wham, M., Clohisey, S., Hendry, R., Scott-Brown, J., Shaw, V., McDonald, S.E., Keating, S., Ahmed, K.A., Armstrong, J.A., Ashworth, M., Asiimwe, I.G., Bakshi, S., Barlow, S.L., Booth, L., Brennan, B., Bullock, K., Catterall, B.W.A., Clark, J.J., Clarke, E.A., Cole, S., Cooper, L., Cox, H., Davis, C., Dincarslan, O., Dunn, C., Dyer, P., Elliott, A., Evans, A., Finch, L., Fisher, L.W.S., Foster, T., Garcia-Dorival, I., Gunning, P., Jensen, R.L., Jones, C.B., Jones, T.R., Khandaker, S., King, K., Kiy, R.T., Koukorava, C., Lake, A., Lant, S., Latawiec, D., Lavelle-Langham, L., Lefteri, D., Lett, L., Livoti, L.A., Mancini, M., McDonald, S., McEvoy, L., McLauchlan, J., Metelmann, S., Miah, N.S., Middleton, J., Mitchell, J., Moore, S.C., Murphy, E.G., Pilgrim, J., Reynolds, W., Ridley, P.M., Sales, D., Shaw, V.E., Shears, R.K., Small, B., Subramaniam, K.S., Szemiel, A., Taggart, A., Tanianis-Hughes, J., Thomas, J., Trochu, E., van Tonder, L., Wilcock, E., Zhang, J.E., Flaherty, L., Maziere, N., Cass, E., Carracedo, A.D., Carlucci, N., Holmes, A., Massey, H., Murphy, L., McCafferty, S., Clark, R., Fawkes, A., Bernatoniene, J., Collini, P., Dark, P., Dushianthan, A., Gkrania-Klotsas, E., Hawcutt, D.B., Lillie, P., Meda, M., Moses, S., Pattison, N., Sharma, A., Vancheeswaran, R., Welters, I., Papineni, P., Wootton, D.G., Darby, A.C., Hiscox, J.A. +216 more +13 more sourcesNSP12-RNA binding structure and comparison of thermodynamic stability.
, 2023 (A) Overall view of NSP12 protein and location of the RDV. (B) RMSD comparison of RNA-binding proteins. (C) Comparison of the molecular vibrations of WT and each mutant.Shiho Torii (12770667), Yong Dam Jeong (14846302), Kei Sato (493447), Rigel Suzuki (12770673), Kwang Su Kim (1960972), Jumpei Ito (761675), Hiroyuki Asakura (1617940), Teppei Shimamura (133856), Takasuke Fukuhara (673475), Yasuhisa Fujita (10344689), Shoya Iwanami (3945266), Kazuhisa Yoshimura (322429), Kenji Sadamasu (7438220), Jun Koseki (738263), Yoshiharu Matsuura (357989), Shingo Iwami (266092), Mami Nagashima (14846305) +16 morecore +1 more sourceStructural Homology-Based Drug Repurposing Approach for Targeting NSP12 SARS-CoV-2
Molecules, 2022 The severe acute respiratory syndrome coronavirus 2, also known as SARS-CoV-2, is the causative agent of the COVID-19 global pandemic. SARS-CoV-2 has a highly conserved non-structural protein 12 (NSP-12) involved in RNA-dependent RNA polymerase (RdRp) activity.Abdulelah Aljuaid, Abdus Salam, Mazen Almehmadi, Soukayna Baammi, Fahad M. Alshabrmi, Mamdouh Allahyani, Khadijah M. Al-Zaydi, Abdullah M. Izmirly, Sarah Almaghrabi, Bandar K. Baothman, Muhammad Shahab +10 moreopenaire +3 more sourcesConservation of NSP12 E802 and NSP6 I168 in coronaviruses.
, 2021 Excel file with the frequency of NSP12 E802 (A) and frequency of NSP6 I168 (B). (XLSX)Andres Merits (191446), Gauthier Lieber (10196207), Meredith E. Stewart (11450472), Oscar A. MacLean (10297450), Alain Kohl (252931), Sam J. Wilson (9344990), Brian J. Willett (11450469), Rute Maria Pinto (10196222), Arthur Wickenhagen (9344984), Daniel Mair (5849150), Agnieszka M. Szemiel (10196243), Wilhelm Furnon (10196183), Nicolas M. Suarez (11450466), Matthew L. Turnbull (10196156), Massimo Palmarini (81656), Ana da Silva Filipe (5849153), Arvind H. Patel (10196255), Emma C. Thomson (10196249), Richard J. Orton (7832015), Sainan Wang (713604) +19 morecore +1 more source
