The Role of Conformational Dynamics and Allostery in Modulating Protein Evolution

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Campitelli, P., Ross, D., Swint‐Kruse, L., & Ozkan, S. B. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.09.013 · Cited by 7 · see citing works

Allosteric Lever: Toward a Principle of Specific Allosteric Response

Vossel, M., de Groot, B. L., & Godec, A. (2025) · Physical Review X · doi:10.1103/wv2k-676p · Cited by 8 · see citing works

Prediction of structural variation

Kalakoti, Y., Sanjeev, A., & Wallner, B. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103003 · Cited by 7 · see citing works

Unlocking the Stereoselectivity and Substrate Acceptance of Enzymes: Proline‐Induced Loop Engineering Test

Qu, G., Bi, Y., Liu, B., Li, J., Han, X., Liu, W., Jiang, Y., Qin, Z., & Sun, Z. (2021) · Angewandte Chemie · doi:10.1002/ange.202110793 · Cited by 7 · see citing works

Intrinsic Dynamics of the ClpXP Proteolytic Machine Using Elastic Network Models

González-Paz, L. A., Lossada, C. A., Hurtado-León, M. L., Fernández-Materán, F. V., Paz, J. L., Parvizi, S., Castillo, R. E. C., Romero, F., & Alvarado, Y. J. (2023) · ACS Omega · doi:10.1021/acsomega.2c04347 · Cited by 7 · see citing works

An Assessment of Quaternary Structure Functionality in Homomer Protein Complexes

Abrusán, G., & Foguet, C. (2023) · Molecular Biology and Evolution · doi:10.1093/molbev/msad070 · Cited by 6 · see citing works

Identification of an Evolutionarily Conserved Allosteric Network in Steroid Receptors

Dube, N., Khan, S. H., Sasse, R. K., & Okafor, C. D. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c01096 · Cited by 6 · see citing works

Some mechanistic underpinnings of molecular adaptations of SARS-COV-2 spike protein by integrating candidate adaptive polymorphisms with protein dynamics

Ose, N. J., Campitelli, P., Modi, T., Kazan, I. C., Kumar, S., & Ozkan, S. B. (2024) · eLife · doi:10.7554/elife.92063.3 · Cited by 6 · see citing works

Engineering gain‐of‐function mutants of a WW domain by dynamics and structural analysis

Lu, J., Rahman, M. I., Kazan, I. C., Halloran, N. R., Bobkov, A. A., Ozkan, S. B., & Ghirlanda, G. (2023) · Protein Science · doi:10.1002/pro.4759 · Cited by 6 · see citing works

Unraveling the roles of aromatic cluster side-chain interactions on the structural stability and functional significance of psychrophilic Sphingomonas sp. glutaredoxin 3

Tran, T. V., Hoang, T., Jang, S., & Lee, C. (2023) · PLoS ONE · doi:10.1371/journal.pone.0290686 · Cited by 6 · see citing works

Protein Conformational Dynamics upon Association with the Surfaces of Lipid Membranes and Engineered Nanoparticles: Insights from Electron Paramagnetic Resonance Spectroscopy

Georgieva, E. R. (2020) · Molecules · doi:10.3390/molecules25225393 · Cited by 6 · see citing works

A protein dynamics–based deep learning model enhances predictions of fitness and epistasis

Huynh, N., Kazan, I. C., Lu, J., Kolbaba‐Kartchner, B., Mills, J. H., & Ozkan, S. B. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2502444122 · Cited by 6 · see citing works

Exploitation of active site flexibility-low temperature activity relation for engineering broad range temperature active enzymes

Dasetty, S., Zajac, J. W. P., & Sarupria, S. (2023) · Molecular Systems Design & Engineering · doi:10.1039/d3me00013c · Cited by 5 · see citing works

Molecular dynamics simulations suggest novel allosteric modes in the Hsp70 chaperone protein

Mahto, F. K., Bhattacharya, A., & Bhattacharya, S. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2290618 · Cited by 5 · see citing works

Synergy and anti‐cooperativity in allostery: Molecular dynamics study of WT and oncogenic KRAS‐RGL1

Hacisuleyman, A., & Erman, B. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26657 · Cited by 5 · see citing works

Reused Protein Segments Linked to Functional Dynamics

Kutlu, Y., Axel, G., Kolodny, R., Ben‐Tal, N., & Haliloǧlu, T. (2024) · Molecular Biology and Evolution · doi:10.1093/molbev/msae184 · Cited by 5 · see citing works

Dynamic Coupling and Entropy Changes in KRAS G12D Mutation: Insights into Molecular Flexibility, Allostery and Function

Hacisuleyman, A., Yüret, D., & Erman, B. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169075 · Cited by 5 · see citing works

Correlated Evolution of Low-Frequency Vibrations and Function in Enzymes

Modi, T., Campitelli, P., Heyden, M., & Ozkan, S. B. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c05983 · Cited by 5 · see citing works

Structural conservation in the glutathione binding in Sphingomonas sp. glutaredoxin Grx3 and variations for cold adaptation

Tran, T. V., Nguyen, H. P. A., Vu, L. O. C., & Lee, C. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140971 · Cited by 5 · see citing works

Water determines the intramolecular dynamics of proteins. En example of bovine serum albumin

Penkov, N. V. (2024) · Frontiers in Chemistry · doi:10.3389/fchem.2024.1444448 · Cited by 5 · see citing works

Allostery and Structural Dynamics in Protein Evolution

Campitelli, P., & Ozkan, S. B. (2019) · Springer eBooks · doi:10.1007/978-3-030-30363-1_9 · Cited by 2 · see citing works

Structural dynamics flexibility informs function and evolution at a proteome scale

Gerek, Z. N., Kumar, S., & Ozkan, S. B. (2013) · Evolutionary Applications · doi:10.1111/eva.12052 · Cited by 104 · see citing works

Allostery and Conformational Dynamics in Protein Evolution

Ozkan, S. B. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.2217

Dynamic Allostery: Evolution's Double-Edged Sword in Protein Function and Disease

Campitelli, P., Kazan, I. C., Hamilton, S., & Ozkan, S. B. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169175 · Cited by 22 · see citing works

Optimization of Conformational Dynamics in an Epistatic Evolutionary Trajectory

González, M. M., Abriata, L. A., Tomatis, P. E., & Vila, A. J. (2016) · Molecular Biology and Evolution · doi:10.1093/molbev/msw052 · Cited by 64 · see citing works