Cueva Tamanaha, M.d.l, Cabrera, E. F., Sargeant, J., Gershon, P. D., Samuel Russell, P.P., and Cocco, M. J. (2025) Voxelotor (Oxbryta) binds multiple hemoglobin sites and influences protein structure. bioRxiv 2025.05.12.653546.
Samuel Russell, P.P., Rickard, M.M., Pogorelov, T.V., and Gruebele, M. (2025) Enzymes in a human cytoplasm model organize into submetabolon complexes. Proceedings of the National Academy of Science 122(5):e2414206122.
Premila's publications prior to SLU
Samuel Russell, P.P., Maytin, A.K., Rickard, M.M., Russell, M.C., Pogorelov, T.V., and Gruebele, M. (2024) Metastable states in the hinge-bending landscape of an enzyme in an atomistic cytoplasm simulation. The Journal of Physical Chemistry Letters 15: 940-946.
Scaletti, C., Samuel Russell, P. P., Hebel, K. J., Rickard, M.M., Boob, M., Danksagmüller, F., Taylor, S. A., Pogorelov, T.V., and Gruebele, M. (2024) Hydrogen bonding heterogeneity correlates with protein folding transition state passage time as revealed by data sonification. Proceedings of the National Academy of Science 121(22):e2319094121.
Samuel Russell, P.P., Rickard, M.M., Boob, M., Gruebele, M., and Pogorelov, T.V. (2023) In silico protein dynamics in the human cytoplasm: partial folding, misfolding, fold switching, and non-native interactions. Protein Science 32(11):e4790.
Samuel Russell, P.P., Alaeen, S., and Pogorelov, T.V. (2023) In-cell dynamics: the next focus of all-atom simulations. The Journal of Physical Chemistry B 127 (46): 9863–9872. Selected as journal’s cover article.
Samuel Russell, P.P., Rickard, M.M., Pogorelov, T.V., and Gruebele, M. (2022) Metabolons, quinary structure, and domain motion: enzyme choreography in the cytoplasm. bioRxiv 2022.09.13.507800.
Samuel, P.P., and Case, D.A. (2020) Atomistic simulations of heme dissociation pathways in human methemoglobins reveal hidden intermediates. Biochemistry 59: 4093–4107.
Samuel, P.P.*, White, M.A., Ou, W.C., Case, D.A., Phillips, G.N. Jr., and Olson, J.S.* (2020) The interplay between molten globules and heme disassociations defines human hemoglobin disassembly. Biophysical Journal 118: 1381–1400. (*Co-corresponding authors.) Highlighted as New and Notable by Professor Juliette T.J. Lecomte in the journal.
Cardenas, A.S.B., Samuel, P.P., and Olson, J.S. (2019) 2019 Military Supplement: Current challenges in the development of acellular hemoglobin oxygen carriers by protein engineering. Shock 52: 28–40.
Samuel, P.P., Ou, W.C., Phillips, G.N. Jr., and Olson, J.S. (2017) The Mechanism of Human Apohemoglobin Unfolding. Biochemistry 56: 1444–1459.
Bissé, E., Schaeffer-Reiss, C., Van Dorsselaer, A., Alayi, T.D., Epting, T., Winkler, K., Benitez Cardenas, A.S., Soman, J., Birukou, I., Samuel, P.P., and Olson, J.S. (2017) Hemoglobin Kirklareli (αH58L), a New Variant Associated with Fe Deficiency and Increased CO Binding. Journal of Biological Chemistry 292: 2542–2555.
Strader, M.B., Bangle, R., Parker Siburt, C.J., Varnado, C.L., Soman, J., Benitez Cardenas, A.S., Samuel, P.P., Singleton, E.W., Crumbliss, A.L., Olson, J.S., Alayash, A.I. (2017) Engineering oxidative stability in human hemoglobin based on the Hb providence (βK82D) mutation and genetic cross-linking. Biochemical Journal 474: 4171–4192.
Samuel, P.P., Smith, L.P., Phillips, G.N., Jr., and Olson, J.S. (2015) Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin. Journal of Biological Chemistry 290: 23479–23495. F1000Prime recommended by Professor Martin Gruebele; Paper of the Week awarded by Journal of Biological Chemistry.