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Therapeutic Targeting of Innate Immune Receptors Against SARS-CoV-2 Infection

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A specific phosphorylation-dependent conformational switch of SARS-CoV-2 nucleoprotein inhibits RNA bindingPreprint

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Risk factors for SARS-CoV-2 seroprevalence following the first pandemic wave in UK healthcare workers in a large NHS Foundation TrustPreprint

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Modifications to the SR-Rich Region of the SARS-CoV-2 Nucleocapsid Regulate Self-Association and Attenuate RNA InteractionsPreprint

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Valuable Contributions and Lessons Learned from Proteomics and Metabolomics Studies of COVID-19

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4D-DIA Proteomics Uncovers New Insights into Host Salivary Response Following SARS-CoV-2 Omicron Infection

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The Disorderly Nature of Caliciviruses

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Antigenic properties of the SARS-CoV-2 nucleoprotein are altered by the RNA admixture

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SpkH (Sll0005) from Synechocystis sp. PCC 6803 is an active Mn2+-dependent Ser kinase

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Dynamic interactions of dimeric hub proteins underlie their diverse functions and structures: A comparative analysis of 14-3-3 and LC8

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Advancing Viral Defense: Unravelling the Potential of Host-Directed Antivirals Against SARS-CoV-2

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High-resolution structure reveals enhanced 14-3-3 binding by a mutant SARS-CoV-2 nucleoprotein variant with improved replicative fitness

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Direct interaction between human DDX1 and SARS-CoV-2 nucleocapsid protein is regulated by phosphorylation

Wang, L., Baxley, R. M., Largaespada, D. A., Aihara, H., & Bielinsky, A. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111408 · Cited by 1 · see citing works

Liquid-liquid phase separation and amyloid aggregation in the 14-3-3 protein family

Rapalytė, S., Karalkevičiu̅tė, V., Baronaitė, I., Veiveris, D., Smirnovas, V., Žiaunys, M., & Šulskis, D. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152660 · Cited by 1 · see citing works

Risk factors for SARS-CoV-2 seroprevalence following the first pandemic wave in UK healthcare workers in a large NHS Foundation Trust

Colton, H., Hodgson, D., Hornsby, H. R., Brown, R. L., Mckenzie, J., Bradley, K. L., James, C. T., Lindsey, B. B., Birch, S., Marsh, L., et al. (2022) · Wellcome Open Research · doi:10.12688/wellcomeopenres.17143.2 · Cited by 1 · see citing works

Mapping SARS-CoV-2 Nucleocapsid Function with NanobodiesPreprint

Weinstein, J. B., Bates, T. A., Anastas, A., Alfahdli, A., Trank-Greene, M., McBride, S. K., Garcia, M., Parson, M. A., Jenkins, M. L., Burke, J. E., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.26.701894 · Cited by 1 · see citing works

Comparative Analysis of Small Moleclues and Natural Plants Compounds as Therapeutic Inhibitors Targeting RdRp and Nucleocapsid Proteins of SARS CoV 2: An in Silico ApproachPreprint

Poleboyina, P. K. (2021) · Research Square · doi:10.21203/rs.3.rs-655036/v1

Peer Review #3 of "Antigenic properties of the SARS-CoV-2 nucleoprotein are altered by the RNA admixture (v0.1)"

(2022) · PeerJ · doi:10.7287/peerj.12751v0.1/reviews/3

Peer Review #3 of "Antigenic properties of the SARS-CoV-2 nucleoprotein are altered by the RNA admixture (v0.2)"

(2022) · PeerJ · doi:10.7287/peerj.12751v0.2/reviews/3

Peer Review #2 of "Antigenic properties of the SARS-CoV-2 nucleoprotein are altered by the RNA admixture (v0.1)"

(2022) · PeerJ · doi:10.7287/peerj.12751v0.1/reviews/2

Peer Review #1 of "Antigenic properties of the SARS-CoV-2 nucleoprotein are altered by the RNA admixture (v0.2)"

(2022) · PeerJ · doi:10.7287/peerj.12751v0.2/reviews/1

Peer Review #2 of "Antigenic properties of the SARS-CoV-2 nucleoprotein are altered by the RNA admixture (v0.2)"

(2022) · PeerJ · doi:10.7287/peerj.12751v0.2/reviews/2

Peer Review #1 of "Antigenic properties of the SARS-CoV-2 nucleoprotein are altered by the RNA admixture (v0.1)"

(2022) · PeerJ · doi:10.7287/peerj.12751v0.1/reviews/1

Intragenomic rearrangements in SARS-CoV-2, other betacoronaviruses, and alphacoronavirusesPreprint

Patarca, R., & Haseltine, W. A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.07.483258

Nucleocapsid Phosphoprotein (N-Protein)

Zhang, J. (2023) · Springer series in biophysics · doi:10.1007/978-3-031-36773-1_22

Proteome profiling of intestinal cultures treated with Bacteroides fragilis vesicles revealed new mechanisms of anti-inflammatory responsePreprint

Shagaleeva, O. Y., Pobeguts, O. V., Kashatnikova, D. A., Kardonsky, D. A., Vorob'eva, E. M., Silantiev, A. S., Efimov, B. A., Matyushkina, D. S., Vanyushkina, A., & Zakharzhevskaya, N. B. (2024) · Research Square · doi:10.21203/rs.3.rs-3970402/v1

An open-sourced 3D printable microscope with a large CNC stagePreprint

Dégut, C., & Plevin, M. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.31.630915

πDMD Simulation as a Strategy for Refinement of AlphaFold2 Modeled Fuzzy Protein Complexes Structures

Muradyan, N., Sargsyan, A. A., Arakelov, V., Paronyan, A., Arakelov, G., & Nazaryan, K. (2025) · Molecular Biology · doi:10.1134/s0026893324700870

SARS-CoV-2 nucleocapsid protein delays cell cycle in S-phase

Liu, J., Liu, M., Yu, X., Wang, P., Guan, X., Huo, W., Zhang, J., Cui, M., Li, X., Zhou, X., et al. (2025) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2025.151671

PermaPhosPeptide Technology: Recombinant Production of Permanently Phosphorylated Oligopeptides for 14–3–3 Protein Interactomic Studies

Perfilova, K. V., Cooley, R. B., & Sluchanko, N. N. (2025) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.5c00531

Identification of merozoite secreted repertoire and immuno-pharmacological inhibition of a novel host-parasite interaction to block malarial infectionPreprint

Singh, N., Munjal, A., Kumari, G., Kaushik, S., Kahlon, A. K., Gupta, S., Chaurasiya, A., Anam, Z.-E., Maurya, M. K., Srivastava, P., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.15.537002

Intramolecular loops control SARS-CoV-2 nucleocapsid protein self-association and nucleic acid binding dependent on phosphorylationPreprint

Nguyen, A., Datta, S. A., Trent, C., Wu, D., Saleem, Z., Szczęsna, E., Yau, W., Owoborode, F., Li, Y., Adly, A. N., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.10.698783

Packaging of the Coronavirus Ribonucleoprotein—A Symphony of Enthalpy and Entropy

Huang, T., Chang, C.-F., & Chang, C. (2026) · Journal of the Chinese Chemical Society · doi:10.1002/jccs.70210

Extracellular Vesicle Protein Cargo Reveals Potential Long-Term Biological Impact of Long COVID

Oda, K., Belmonte, A. D., Boulifard, D. A., Jakubski, S., White, L. E., Beckett, C. G., Letizia, A., Porter, C., Villasante, E. F., Johnson, Y. S., et al. (2026) · Cells · doi:10.3390/cells15211969

Viral proteins that facilitate RNA replication

Černỳ, P. (2023) · Digital Repository (National Repository of Grey Literature)

Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins

Eisenreichová, A., & Bouřa, E. (2022) · Journal of Structural Biology · doi:10.1016/j.jsb.2022.107879 · Cited by 9 · see citing works

Human 14-3-3 Proteins Site-selectively Bind the Mutational Hotspot Region of SARS-CoV-2 Nucleoprotein Modulating its Phosphoregulation

Tugaeva, K. V., Sysoev, A. A., Kapitonova, A. A., Smith, J. L. R., Zhu, P., Cooley, R. B., Antson, A. A., & Sluchanko, N. N. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167891 · Cited by 27 · see citing works

Mutations in the phosphorylation sites of SARS-CoV-2 encoded nucleocapsid protein and structure model of sequestration by protein 14-3-3

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A novel phosphorylation site in SARS-CoV-2 nucleocapsid regulates its RNA-binding capacity and phase separation in host cells

Wu, J., Zhong, Y., Liu, X., Lu, X., Zeng, W., Wu, C., Xing, F., Cao, L., Zheng, F., Hou, P., et al. (2022) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjac003 · Cited by 12 · see citing works