Reply to: Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
https://www.nature.com/articles/s41589-023-01425-z.pdf
Reference12 articles.
1. Harrison, N. L., Abbott, G. W., McClenaghan, C., Nichols, C. G. & Cabrera Garcia, D. Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection. Nat. Chem. Biol., https://doi.org/10.1038/s41589-023-01423-1 (2023).
2. Ma, D. et al. Golgi export of the Kir2.1 channel is driven by a trafficking signal located within its tertiary structure. Cell 145, 1102–1115 (2011).
3. Cohen, J. F., Lin, L. D. & Machamer, C. E. Identification of a Golgi complex-targeting signal in the cytoplasmic tail of the severe acute respiratory syndrome coronavirus envelope protein. J. Virol. 85, 5794–5803 (2011).
4. Jimenez-Guardeño, J. M. et al. The PDZ-binding motif of severe acute respiratory syndrome coronavirus envelope protein is a determinant of viral pathogenesis. PLoS Pathog. 10, e1004320 (2014).
5. Oh, C.-K. et al. Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection. Nat. Chem. Biol. 19, 275–283 (2023).
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