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For: Essalmani R, Jain J, Susan-Resiga D, Andréo U, Evagelidis A, Derbali RM, Huynh DN, Dallaire F, Laporte M, Delpal A, Sutto-Ortiz P, Coutard B, Mapa C, Wilcoxen K, Decroly E, Nq Pham T, Cohen ÉA, Seidah NG. Distinctive Roles of Furin and TMPRSS2 in SARS-CoV-2 Infectivity. J Virol 2022;:e0012822. [PMID: 35343766 DOI: 10.1128/jvi.00128-22] [Cited by in Crossref: 9] [Cited by in F6Publishing: 12] [Article Influence: 9.0] [Reference Citation Analysis]
Number Citing Articles
1 Chan S. Fusion assays for screening of fusion inhibitors targeting SARS-CoV-2 entry and syncytia formation. Front Pharmacol 2022;13. [DOI: 10.3389/fphar.2022.1007527] [Reference Citation Analysis]
2 Wagoner J, Herring S, Hsiang TY, Ianevski A, Biering SB, Xu S, Hoffmann M, Pöhlmann S, Gale M Jr, Aittokallio T, Schiffer JT, White JM, Polyak SJ. Combinations of Host- and Virus-Targeting Antiviral Drugs Confer Synergistic Suppression of SARS-CoV-2. Microbiol Spectr 2022;:e0333122. [PMID: 36190406 DOI: 10.1128/spectrum.03331-22] [Reference Citation Analysis]
3 Tu B, Gao Y, An X, Wang H, Huang Y. Localized delivery of nanomedicine and antibodies for combating COVID-19. Acta Pharm Sin B 2022. [PMID: 36168329 DOI: 10.1016/j.apsb.2022.09.011] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
4 Harte JV, Wakerlin SL, Lindsay AJ, Mccarthy JV, Coleman-vaughan C. Metalloprotease-Dependent S2′-Activation Promotes Cell–Cell Fusion and Syncytiation of SARS-CoV-2. Viruses 2022;14:2094. [DOI: 10.3390/v14102094] [Reference Citation Analysis]
5 Gellenoncourt S, Saunders N, Robinot R, Auguste L, Rajah MM, Kervevan J, Jeger-Madiot R, Staropoli I, Planchais C, Mouquet H, Buchrieser J, Schwartz O, Chakrabarti LA. The Spike-Stabilizing D614G Mutation Interacts with S1/S2 Cleavage Site Mutations To Promote the Infectious Potential of SARS-CoV-2 Variants. J Virol 2022;:e0130122. [PMID: 36121299 DOI: 10.1128/jvi.01301-22] [Reference Citation Analysis]
6 Ohradanova-repic A, Skrabana R, Gebetsberger L, Tajti G, Baráth P, Ondrovičová G, Praženicová R, Jantova N, Hrasnova P, Stockinger H, Leksa V. Blockade of TMPRSS2-mediated priming of SARS-CoV-2 by lactoferricin. Front Immunol 2022;13:958581. [DOI: 10.3389/fimmu.2022.958581] [Reference Citation Analysis]
7 Sebastián-martín A, Sánchez BG, Mora-rodríguez JM, Bort A, Díaz-laviada I. Role of Dipeptidyl Peptidase-4 (DPP4) on COVID-19 Physiopathology. Biomedicines 2022;10:2026. [DOI: 10.3390/biomedicines10082026] [Reference Citation Analysis]
8 Stevaert A, Van Berwaer R, Mestdagh C, Vandeput J, Vanstreels E, Raeymaekers V, Laporte M, Naesens L. Impact of SARS-CoV-2 Spike Mutations on Its Activation by TMPRSS2 and the Alternative TMPRSS13 Protease. mBio 2022;:e0137622. [PMID: 35913162 DOI: 10.1128/mbio.01376-22] [Reference Citation Analysis]
9 Seidah NG, Garçon D. Expanding Biology of PCSK9: Roles in Atherosclerosis and Beyond. Curr Atheroscler Rep 2022. [PMID: 35904732 DOI: 10.1007/s11883-022-01057-z] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 3.0] [Reference Citation Analysis]
10 Qiao S, Zhang S, Ge J, Wang X. The spike glycoprotein of highly pathogenic human coronaviruses: structural insights for understanding infection, evolution and inhibition. FEBS Open Bio 2022. [PMID: 35689514 DOI: 10.1002/2211-5463.13454] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
11 Cendron L, Rothenberger S, Cassari L, Dettin M, Pasquato A. Proprotein convertases regulate trafficking and maturation of key proteins within the secretory pathway. Advances in Protein Chemistry and Structural Biology 2022. [DOI: 10.1016/bs.apcsb.2022.10.001] [Reference Citation Analysis]