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MICHIGAN STATE UNIVERSITY
College of Natural Science
Cryo-EM

Publications

  1. Yu, P. et al. (2026) “Structural analysis of a Gram-positive type VII ABC transporter induced by cell wall-targeting antibiotics,” Structure, 34(1), pp. 145-156.e4. Available at: https://doi.org/10.1016/j.str.2025.10.004. 
  2. Subramanian, S., Dover, J.A. and Parent, K.N. (2025) “The Shigella siphophage Sf11 tail structure and host attachment mechanism,” Journal of Virology, 99(12). Available at: https://doi.org/10.1128/jvi.01367-25. 
  3. Gatreddi, S. et al. (2025) “Structures of two LarA‐like nickel‐pincer nucleotide cofactor‐utilizing enzymes with a single catalytic histidine residue,” Protein Science, 34(12). Available at: https://doi.org/10.1002/pro.70362. 
  4. Oliveira, J. dos S. et al. (2025) “Intracellular iron positively modulates the replicative cycle of mimiviruses, increasing virus production,” Journal of Virology, 99(10). Available at: https://doi.org/10.1128/jvi.01025-25. 
  5. Rastandeh, A. et al. (2025) “Measuring the selective packaging of RNA molecules by viral coat proteins in cells,” Proceedings of the National Academy of Sciences, 122(33). Available at: https://doi.org/10.1073/pnas.2505190122. 
  6. Granados-Villanueva, D., Rossow, A. and Kim, K.H. (2025) “Get4/5-mediated remodeling of Get3’s substrate-binding chamber: Insights into tail-anchored protein targeting by the GET pathway,” Journal of Biological Chemistry, 301(10), p. 110667. Available at: https://doi.org/10.1016/j.jbc.2025.110667. 
  7. Arachchige, E.J. et al. (2025) “Structural and Functional Characterization of Pseudomonas aeruginosa Virulence Factor AaaA, an Autotransporter with Arginine-Specific Aminopeptidase Activity,” Journal of Molecular Biology, 437(19), p. 169358. Available at: https://doi.org/10.1016/j.jmb.2025.169358. 
  8. MuhammedNazaar, S. et al. (2025) “The lipid bilayer strengthens the cooperative network of membrane proteins,” Science Advances, 11(27). Available at: https://doi.org/10.1126/sciadv.adv9568. 
  9. Subramanian, S. et al. (2024) “Moo19 and B2: Structures of Schitoviridae podophages with T = 9 geometry and tailspikes with esterase activity,” Science Advances, 10(51). Available at: https://doi.org/10.1126/sciadv.adt0022. 
  10. Cortines, J.R. et al. (2024) “Transition metals and oxidation reactions trigger stargate opening during the initial stages of the replicative cycle of the giant Tupanvirus,” mBio, 15(10). Available at: https://doi.org/10.1128/mbio.02192-24. 
  11. Boyd, C.M. et al. (2024) “A Vibrio cholerae viral satellite maximizes its spread and inhibits phage by remodeling hijacked phage coat proteins into small capsids,” eLife, 12. Available at: https://doi.org/10.7554/eLife.87611.3. 
  12. Subramanian, S. et al. (2024) “Cryo-EM structure of a Shigella podophage reveals a hybrid tail and novel decoration proteins,” Structure, 32(1), pp. 24-34.e4. Available at: https://doi.org/10.1016/j.str.2023.10.007. 
  13. Orlando, M.A. et al. (2024) “Substrate engagement by the intramembrane metalloprotease SpoIVFB,” Nature Communications, 15(1), p. 8276. Available at: https://doi.org/10.1038/s41467-024-52634-6. 
  14. George, N.L. and Orlando, B.J. (2023) “Architecture of a complete Bce-type antimicrobial peptide resistance module,” Nature Communications, 14(1), p. 3896. Available at: https://doi.org/10.1038/s41467-023-39678-w. 
  15. Subramanian, S. et al. (2022) “Host Range Expansion of Shigella Phage Sf6 Evolves through Point Mutations in the Tailspike,” Journal of Virology, 96(16). Available at: https://doi.org/10.1128/jvi.00929-22. 
  16. Orlando, B.J. et al. (2022) “Development, structure, and mechanism of synthetic antibodies that target claudin and Clostridium perfringens enterotoxin complexes,” Journal of Biological Chemistry, 298(9), p. 102357. Available at: https://doi.org/10.1016/j.jbc.2022.102357. 
  17. George, N.L., Schilmiller, A.L. and Orlando, B.J. (2022) “Conformational snapshots of the bacitracin sensing and resistance transporter BceAB,” Proceedings of the National Academy of Sciences, 119(14). Available at: https://doi.org/10.1073/pnas.2123268119. 
  18. Gaffney, K.A. et al. (2022) “Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein,” Proceedings of the National Academy of Sciences, 119(1). Available at: https://doi.org/10.1073/pnas.2109169119. 
  19. Doore, S.M. et al. (2021) “Large Metabolic Rewiring from Small Genomic Changes between Strains of Shigella flexneri,” Journal of Bacteriology, 203(11). Available at: https://doi.org/10.1128/JB.00056-21. 
  20. Strubbe-Rivera, J.O. et al. (2021) “Modeling the Effects of Calcium Overload on Mitochondrial Ultrastructural Remodeling,” Applied Sciences, 11(5), p. 2071. Available at: https://doi.org/10.3390/app11052071. 
  21. Strubbe-Rivera, J.O. et al. (2021) “The mitochondrial permeability transition phenomenon elucidated by cryo-EM reveals the genuine impact of calcium overload on mitochondrial structure and function,” Scientific Reports, 11(1), p. 1037. Available at: https://doi.org/10.1038/s41598-020-80398-8. 
  22. Dong, S. et al. (2020) “Promotion of CTL epitope presentation by a nanoparticle with environment-responsive stability and phagolysosomal escape capacity,” Journal of Controlled Release, 328, pp. 653–664. Available at: https://doi.org/10.1016/j.jconrel.2020.09.033. 
  23. Doore, S., Subramanian, S. and Parent, K. (2020) “Structural Analysis of the Shigella Virus Sf14 Capsid,” Microscopy and Microanalysis, 26(S2), pp. 1306–1306. Available at: https://doi.org/10.1017/S143192762001764X. 
  24. Schrad, J.R. et al. (2020) “Structural and Proteomic Characterization of the Initiation of Giant Virus Infection,” Cell, 181(5), pp. 1046-1061.e6. Available at: https://doi.org/10.1016/j.cell.2020.04.032. 
  25. Subramanian, S. and Parent, K. (2020) “Structure of the Shigella flexneri podophage HRP29,” Microscopy and Microanalysis, 26(S2), pp. 2744–2744. Available at: https://doi.org/10.1017/S1431927620022643. 
  26. Newcomer, R.L. et al. (2019) “The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy,” eLife, 8. Available at: https://doi.org/10.7554/eLife.45345. 
  27. Strubbe, J.O. et al. (2019) “Mitochondrial ultrastructure, function, and calcium buffering by massive calcium loading observed using advanced cryo‐electron microscopy, high‐resolution respirometry and spectrofluorimetry,” The FASEB Journal, 33(S1). Available at: https://doi.org/10.1096/fasebj.2019.33.1_supplement.543.14. 
  28. Strubbe, J.O. et al. (2019) “Cardiac Mitochondria Ultrastructural and Functional Changes Caused by Massive Calcium Loading Observed using Cryo-EM and High-Resolution Respirometry,” Biophysical Journal, 116(3), p. 270a. Available at: https://doi.org/10.1016/j.bpj.2018.11.1462. 
  29. Parent, K.N. et al. (2018) “A Gateway into Understanding the Unique Vertex of Samba Virus,” Microscopy and Microanalysis, 24(S1), pp. 1438–1439. Available at: https://doi.org/10.1017/S1431927618007675. 
  30. Doore, S.M. et al. (2018) “Shigella Phages Isolated during a Dysentery Outbreak Reveal Uncommon Structures and Broad Species Diversity,” Journal of Virology, 92(8). Available at: https://doi.org/10.1128/JVI.02117-17. 
  31. Schrad, J. et al. (2017) “Microscopic Characterization of the Brazilian Giant Samba Virus,” Viruses, 9(2), p. 30. Available at: https://doi.org/10.3390/v9020030. 
  32. Schrad, J.R. et al. (2016) “Microscopic Evidence for a Stargate Structure in the Giant Virus, Samba Virus.,” Microscopy and Microanalysis, 22(S3), pp. 1114–1115. Available at: https://doi.org/10.1017/S1431927616006413.