Year |
Citation |
Score |
2018 |
Zhang C, Samad M, Yu H, Chakroun N, Hilton D, Dalby PA. Computational-design to reduce conformational flexibility and aggregation rates of an antibody Fab fragment. Molecular Pharmaceutics. PMID 29897777 DOI: 10.1021/acs.molpharmaceut.8b00186 |
0.307 |
|
2017 |
Robinson MJ, Matejtschuk P, Bristow AF, Dalby PA. Tm-values and unfolded fraction can predict aggregation rates for GCSF variant formulations, but not under predominantly native conditions. Molecular Pharmaceutics. PMID 29141152 DOI: 10.1021/acs.molpharmaceut.7b00876 |
0.326 |
|
2016 |
Morris P, Rios-Solis L, García-Arrazola R, Lye GJ, Dalby PA. Impact of cofactor-binding loop mutations on thermotolerance and activity of E. coli transketolase. Enzyme and Microbial Technology. 89: 85-91. PMID 27233131 DOI: 10.1016/j.enzmictec.2016.04.003 |
0.308 |
|
2008 |
Aucamp JP, Martinez-Torres RJ, Hibbert EG, Dalby PA. A microplate-based evaluation of complex denaturation pathways: structural stability of Escherichia coli transketolase. Biotechnology and Bioengineering. 99: 1303-10. PMID 17969139 DOI: 10.1002/bit.21705 |
0.313 |
|
2001 |
Dalby PA, Hoess RH, DeGrado WF. Evolution of binding affinity in a WW domain probed by phage display. Protein Science : a Publication of the Protein Society. 9: 2366-76. PMID 11206058 DOI: 10.1110/Ps.9.12.2366 |
0.325 |
|
1998 |
Dalby PA, Clarke J, Johnson CM, Fersht AR. Folding intermediates of wild-type and mutants of barnase. II. Correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate. Journal of Molecular Biology. 276: 647-56. PMID 9551102 DOI: 10.1006/Jmbi.1997.1547 |
0.427 |
|
1998 |
Dalby PA, Oliveberg M, Fersht AR. Folding intermediates of wild-type and mutants of barnase. I. use of @f-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium Journal of Molecular Biology. 276: 625-646. PMID 9551101 DOI: 10.1006/Jmbi.1997.1546 |
0.454 |
|
1998 |
Dalby PA, Oliveberg M, Fersht AR. Movement of the Intermediate and Rate Determining Transition State of Barnase on the Energy Landscape with Changing Temperature Biochemistry. 37: 4674-4679. PMID 9521788 DOI: 10.1021/Bi972798D |
0.414 |
|
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