Year |
Citation |
Score |
2018 |
Soranno A, Cabassi F, Orselli ME, Cellmer T, Gori A, Longhi R, Buscaglia M. Dynamics of Structural Elements of GB1 β-Hairpin Revealed by Tryptophan-Cysteine Contact Formation Experiments. The Journal of Physical Chemistry. B. 122: 11468-11477. PMID 30215522 DOI: 10.1021/Acs.Jpcb.8B07399 |
0.414 |
|
2018 |
Dunkelberger EB, Metaferia B, Cellmer T, Henry ER. Theoretical Simulation of Red Cell Sickling Upon Deoxygenation Based on the Physical Chemistry of Sickle Hemoglobin Fiber Formation. The Journal of Physical Chemistry. B. PMID 30179501 DOI: 10.1021/Acs.Jpcb.8B07638 |
0.314 |
|
2016 |
Cellmer T, Ferrone FA, Eaton WA. Universality of supersaturation in protein-fiber formation. Nature Structural & Molecular Biology. PMID 27018803 DOI: 10.1038/Nsmb.3197 |
0.387 |
|
2013 |
Chung HS, Cellmer T, Louis JM, Eaton WA. Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories. Chemical Physics. 422: 229-237. PMID 24443626 DOI: 10.1016/J.Chemphys.2012.08.005 |
0.37 |
|
2012 |
Cellmer T, Fawzi NL. Coarse-grained simulations of protein aggregation. Methods in Molecular Biology (Clifton, N.J.). 899: 453-70. PMID 22735969 DOI: 10.1007/978-1-61779-921-1_27 |
0.545 |
|
2011 |
Zhu L, Ghosh K, King M, Cellmer T, Bakajin O, Lapidus LJ. Evidence of multiple folding pathways for the villin headpiece subdomain. The Journal of Physical Chemistry. B. 115: 12632-7. PMID 21923150 DOI: 10.1021/Jp206238Y |
0.432 |
|
2011 |
Cellmer T, Buscaglia M, Henry ER, Hofrichter J, Eaton WA. Making connections between ultrafast protein folding kinetics and molecular dynamics simulations Proceedings of the National Academy of Sciences of the United States of America. 108: 6103-6108. PMID 21441105 DOI: 10.1073/Pnas.1019552108 |
0.543 |
|
2011 |
Chung HS, Gopich IV, McHale K, Cellmer T, Louis JM, Eaton WA. Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein Journal of Physical Chemistry A. 115: 3642-3656. PMID 20509636 DOI: 10.1021/Jp1009669 |
0.401 |
|
2011 |
Cellmer T, Buscaglia M, Henry E, Hofrichter J, Eaton W. Measuring Sub-Microsceond Protein Folding Kinetics with Independent Probes Biophysical Journal. 100: 400a. DOI: 10.1016/J.Bpj.2010.12.2378 |
0.517 |
|
2011 |
Buscaglia M, Soranno A, Cellmer T, Longhi R, Bellini T. Folding Kinetics of Small Proteins Revealed by Tryptophan-Cysteine Contact Formation Experiments Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.1360 |
0.51 |
|
2010 |
Chung HS, Gopich IV, Louis JM, McHale K, Cellmer T, Eaton WA. Photon-By-Photon Analysis of Single Molecule Fluorescence Trajectories of a Fast Folding Protein Biophysical Journal. 98: 29a-30a. DOI: 10.1016/J.Bpj.2009.12.174 |
0.413 |
|
2008 |
Kubelka J, Henry ER, Cellmer T, Hofrichter J, Eaton WA. Chemical, physical, and theoretical kinetics of an ultrafast folding protein Proceedings of the National Academy of Sciences of the United States of America. 105: 18655-18662. PMID 19033473 DOI: 10.1073/Pnas.0808600105 |
0.404 |
|
2008 |
Cellmer T, Henry ER, Hofrichter J, Eaton WA. Measuring internal friction of an ultrafast-folding protein Proceedings of the National Academy of Sciences of the United States of America. 105: 18320-18325. PMID 19020085 DOI: 10.1073/Pnas.0806154105 |
0.433 |
|
2007 |
Cellmer T, Henry ER, Kubelka J, Hofrichter J, Eaton WA. Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration Journal of the American Chemical Society. 129: 14564-14565. PMID 17983235 DOI: 10.1021/Ja0761939 |
0.481 |
|
2007 |
Cellmer T, Bratko D, Prausnitz JM, Blanch HW. Protein aggregation in silico. Trends in Biotechnology. 25: 254-61. PMID 17433843 DOI: 10.1016/J.Tibtech.2007.03.011 |
0.653 |
|
2007 |
Bratko D, Cellmer T, Prausnitz JM, Blanch HW. Molecular simulation of protein aggregation. Biotechnology and Bioengineering. 96: 1-8. PMID 17136749 DOI: 10.1002/Bit.21232 |
0.645 |
|
2007 |
Cellmer T, Douma R, Huebner A, Prausnitz J, Blanch H. Kinetic studies of protein L aggregation and disaggregation Biophysical Chemistry. 125: 350-359. PMID 17055144 DOI: 10.1016/J.Bpc.2006.09.010 |
0.592 |
|
2006 |
Bratko D, Cellmer T, Prausnitz JM, Blanch HW. Effect of single-point sequence alterations on the aggregation propensity of a model protein. Journal of the American Chemical Society. 128: 1683-91. PMID 16448142 DOI: 10.1021/Ja056837H |
0.638 |
|
2005 |
Cellmer T, Bratko D, Prausnitz JM, Blanch H. Protein-folding landscapes in multichain systems. Proceedings of the National Academy of Sciences of the United States of America. 102: 11692-7. PMID 16081531 DOI: 10.1073/Pnas.0505342102 |
0.618 |
|
2005 |
Cellmer T, Bratko D, Prausnitz JM, Blanch H. Thermodynamics of folding and association of lattice-model proteins. The Journal of Chemical Physics. 122: 174908. PMID 15910070 DOI: 10.1063/1.1888545 |
0.653 |
|
2005 |
Liu W, Cellmer T, Keerl D, Prausnitz JM, Blanch HW. Interactions of lysozyme in guanidinium chloride solutions from static and dynamic light-scattering measurements. Biotechnology and Bioengineering. 90: 482-90. PMID 15778988 DOI: 10.1002/Bit.20442 |
0.579 |
|
2005 |
Cellmer T, Bratko D, Prausnitz JM, Blanch H. The competition between protein folding and aggregation: off-lattice minimalist model studies. Biotechnology and Bioengineering. 89: 78-87. PMID 15540197 DOI: 10.1002/Bit.20302 |
0.669 |
|
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