Source: https://www.englandlab.com/publications.html
Timestamp: 2019-04-21 03:07:46+00:00

Document:
Sarkar, S. and England, J. L., "Sufficient physical conditions for self-replication," submitted.
Bisker, Gili, and Jeremy L. England. "Nonequilibrium associative retrieval of multiple stored self-assembly targets." Proceedings of the National Academy of Sciences 115 E10531-E10538 (2018).
Marsland III, Robert, and England, J. L.. "Active regeneration unites high-and low-temperature features in cooperative self-assembly." Physical Review E 98, 022411 (2018).
Chvkykov, P. and England, J. L., "Least-rattling Feedback from Strong Time-scale Separation," Phys. Rev. E, 97, 032115 (2018).
Kachman, T., Owen, J. A., and England, J. L., "Self-organized Resonance during Search of a Diverse Chemical Space," Phys. Rev. Lett.​, 119, 038001 (2017).
Horowitz, J. M. and England, J. L. "Spontaneous Fine-tuning to Environment in Many-species Chemical Reaction Networks," Proc. Natl. Acad. Sci.​, 114, 7565 (2017).
Gura Sadovsky, R., Brielle, S., Kaganovich, D., and England, J. "Measurement of Rapid Protein Diffusion in the Cytoplasm by Photo-Converted Intensity Profile Expansion." Cell Reports, 18, 2795 (2017).
Horowitz, J. M., Zhou, K., and England, J. L. "Minimum Energetic Cost to Maintain a Target Nonequilibrium State." Phys. Rev. E, 95, 042102 (2017).
Perunov, N., Marsland, R., and England, J. "Statistical Physics of Adaptation", Phys. Rev. X​, 6, 021036 (2016).
Gingrich, T. R., Horowitz, J. M., Perunov, N., and England, J. L. "Dissipation Bounds All Steady-state Current Fluctuations." Phys. Rev. Lett., 116, 120601 (2016).
Brock, K. P., Abraham, A., Amen, T., Kaganovich, D. and England, J. L. "Structural Basis for Modulation of Quality Control Fate in a Marginally Stable Protein." Structure, 23, 1169 (2015).
Perunov, N. and England, J. L. “Quantitative Theory of Hydrophobic Effect as a Driving Force of Protein Structure.” Protein Science, 23, 387 (2014).
England, J. L. "Statistical Physics of self-replication." J. Chem. Phys., 139, 121923 (2013).
England, J. L., “Allostery in protein domains reflects a balance of steric and hydrophobic effects.” Structure, 19, 967 (2011).
England, J. L. and Haran, G., “To fold or expand – a charged question,” Proc. Natl. Acad. Sci., 107, 14519 (2010).
England, J. L. and Haran, G., “Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back.” Ann. Rev. Phys. Chem., 62, 257 (2010).
England, J. L. and Kaganovich, D., “Polyglutamine shows a urea-like affinity for unfolded cytosolic protein.” FEBS Lett., 585, 381 (2010).
England, J. L. and Pande, V. S., “Charge, hydrophobicity, and confined water: putting past simulations into a simple theoretical framework.” Biochem. and Cell Biol., 88, 359 (2010).
England, J. L., Pande V. S., and Haran, G., “Chemical denaturants inhibit the onset of dewetting.” J. Am. Chem. Soc., 130, 11854 (2008).
Lucent, D., England, J. L., and Pande, V. S., “Inside the Chaperonin toolbox: theoretical and computational models for chaperonin mechanism.” Phys. Biol. 6, 015003 (2008).
England, J. L., Lucent, D., and Pande, V. S., “A Role for Confined Water in Chaperonin Function.” J. Am. Chem. Soc. 130, 11838 (2008).
England, J. L. and Pande, V. S., “Potential for modulation of the hydrophobic effect inside chaperonins.” Biophys. J. 95, 3391 (2008).
England, J. et. al., “Rattling the cage: computational models of chaperonin-mediated protein folding.” Curr. Opin. Struct. Biol. 18, 163 (2008).
England, J. L., Park, S., and Pande, V. S., “Theory for an order-driven disruption of the liquid state in water.” J. Chem. Phys. 128, 044503 (2008).
England, J. L. and Cardy, J., “Morphogen gradient from a noisy source.” Phys. Rev. Lett. 94, 078101 (2005).
England, J. L. et. al., “Natural selection of more designable folds: A mechanism for thermophilic adaptation.” Proc. Natl. Acad. Sci. 100,15 (2003).
England, J. L. and Shakhnovich, E. I., “Structural Determinant of Protein Designability.” Phys. Rev. Lett. 90, 21 (2003).
Larson, S. M., England, J. L., Desjarlais, J. R., and Pande, V. S., “Thoroughly sampling sequence space: Large-scale protein design of structural ensembles.” Prot. Sci. 11, 2804 (2002).

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