Year |
Citation |
Score |
2019 |
Sarkar S, England JL. Design of conditions for self-replication. Physical Review. E. 100: 022414. PMID 31574610 DOI: 10.1103/Physreve.100.022414 |
0.302 |
|
2018 |
Bisker G, England JL. Nonequilibrium associative retrieval of multiple stored self-assembly targets. Proceedings of the National Academy of Sciences of the United States of America. PMID 30348806 DOI: 10.1073/Pnas.1805769115 |
0.323 |
|
2018 |
Marsland R, England JL. Active regeneration unites high- and low-temperature features in cooperative self-assembly. Physical Review. E. 98: 022411. PMID 30253561 DOI: 10.1103/Physreve.98.022411 |
0.367 |
|
2018 |
Marsland R, England JL. Limits of predictions in thermodynamic systems: a review. Reports On Progress in Physics. 81: 16601. PMID 28976362 DOI: 10.1088/1361-6633/Aa9101 |
0.344 |
|
2017 |
Kachman T, Owen JA, England JL. Self-Organized Resonance during Search of a Diverse Chemical Space. Physical Review Letters. 119: 038001. PMID 28777611 DOI: 10.1103/Physrevlett.119.038001 |
0.329 |
|
2017 |
Horowitz JM, England JL. Spontaneous fine-tuning to environment in many-species chemical reaction networks. Proceedings of the National Academy of Sciences of the United States of America. PMID 28674005 DOI: 10.1073/Pnas.1700617114 |
0.309 |
|
2017 |
Horowitz JM, Zhou K, England JL. Minimum energetic cost to maintain a target nonequilibrium state. Physical Review. E. 95: 042102. PMID 28505816 DOI: 10.1103/Physreve.95.042102 |
0.352 |
|
2017 |
Gura Sadovsky R, Brielle S, Kaganovich D, England JL. Measurement of Rapid Protein Diffusion in the Cytoplasm by Photo-Converted Intensity Profile Expansion. Cell Reports. 18: 2795-2806. PMID 28297680 DOI: 10.1016/J.Celrep.2017.02.063 |
0.327 |
|
2016 |
Perunov N, Marsland RA, England JL. Statistical physics of adaptation Physical Review X. 6. DOI: 10.1103/Physrevx.6.021036 |
0.34 |
|
2015 |
England JL. Dissipative adaptation in driven self-assembly. Nature Nanotechnology. 10: 919-23. PMID 26530021 DOI: 10.1038/Nnano.2015.250 |
0.347 |
|
2015 |
Brock KP, Abraham AC, Amen T, Kaganovich D, England JL. Structural Basis for Modulation of Quality Control Fate in a Marginally Stable Protein. Structure (London, England : 1993). 23: 1169-78. PMID 26027734 DOI: 10.1016/J.Str.2015.04.015 |
0.386 |
|
2015 |
Marsland R, England J. Far-from-equilibrium distribution from near-steady-state work fluctuations Physical Review E - Statistical, Nonlinear, and Soft Matter Physics. 92. DOI: 10.1103/Physreve.92.052120 |
0.32 |
|
2014 |
Perunov N, England JL. Quantitative theory of hydrophobic effect as a driving force of protein structure. Protein Science : a Publication of the Protein Society. 23: 387-99. PMID 24408023 DOI: 10.1002/Pro.2420 |
0.437 |
|
2012 |
Spokoini R, Moldavski O, Nahmias Y, England JL, Schuldiner M, Kaganovich D. Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast. Cell Reports. 2: 738-47. PMID 23022486 DOI: 10.1016/J.Celrep.2012.08.024 |
0.34 |
|
2011 |
England JL. Allostery in protein domains reflects a balance of steric and hydrophobic effects. Structure (London, England : 1993). 19: 967-75. PMID 21742263 DOI: 10.1016/J.Str.2011.04.009 |
0.45 |
|
2011 |
England JL, Haran G. Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back. Annual Review of Physical Chemistry. 62: 257-77. PMID 21219136 DOI: 10.1146/Annurev-Physchem-032210-103531 |
0.462 |
|
2011 |
England JL, Kaganovich D. Polyglutamine shows a urea-like affinity for unfolded cytosolic protein. Febs Letters. 585: 381-4. PMID 21176779 DOI: 10.1016/J.Febslet.2010.12.023 |
0.386 |
|
2010 |
England JL, Haran G. To fold or expand--a charged question. Proceedings of the National Academy of Sciences of the United States of America. 107: 14519-20. PMID 20682745 DOI: 10.1073/Pnas.1008673107 |
0.427 |
|
2010 |
England JL, Pande VS. Charge, hydrophobicity, and confined water: putting past simulations into a simple theoretical framework. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: 359-69. PMID 20453936 DOI: 10.1139/o09-187 |
0.502 |
|
2009 |
Lucent D, England J, Pande V. Inside the chaperonin toolbox: theoretical and computational models for chaperonin mechanism. Physical Biology. 6: 015003. PMID 19208937 DOI: 10.1088/1478-3975/6/1/015003 |
0.541 |
|
2008 |
England JL, Lucent D, Pande VS. A role for confined water in chaperonin function. Journal of the American Chemical Society. 130: 11838-9. PMID 18710231 DOI: 10.1021/Ja802248M |
0.574 |
|
2008 |
England JL, Pande VS, Haran G. Chemical denaturants inhibit the onset of dewetting. Journal of the American Chemical Society. 130: 11854-5. PMID 18707183 DOI: 10.1021/Ja803972G |
0.562 |
|
2008 |
England JL, Pande VS. Potential for modulation of the hydrophobic effect inside chaperonins. Biophysical Journal. 95: 3391-9. PMID 18599630 DOI: 10.1529/Biophysj.108.131037 |
0.579 |
|
2008 |
England J, Lucent D, Pande V. Rattling the cage: computational models of chaperonin-mediated protein folding. Current Opinion in Structural Biology. 18: 163-9. PMID 18291636 DOI: 10.1016/J.Sbi.2007.12.013 |
0.583 |
|
2008 |
England JL, Park S, Pande VS. Theory for an order-driven disruption of the liquid state in water. The Journal of Chemical Physics. 128: 044503. PMID 18247965 DOI: 10.1063/1.2823129 |
0.498 |
|
2003 |
England JL, Shakhnovich BE, Shakhnovich EI. Natural selection of more designable folds: a mechanism for thermophilic adaptation. Proceedings of the National Academy of Sciences of the United States of America. 100: 8727-31. PMID 12843403 DOI: 10.1073/Pnas.1530713100 |
0.42 |
|
2003 |
England JL, Shakhnovich EI. Structural determinant of protein designability. Physical Review Letters. 90: 218101. PMID 12786593 DOI: 10.1103/Physrevlett.90.218101 |
0.408 |
|
2002 |
Larson SM, England JL, Desjarlais JR, Pande VS. Thoroughly sampling sequence space: large-scale protein design of structural ensembles. Protein Science : a Publication of the Protein Society. 11: 2804-13. PMID 12441379 DOI: 10.1110/Ps.0203902 |
0.605 |
|
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