Year |
Citation |
Score |
2019 |
Mydy LS, Cristobal JR, Katigbak RD, Bauer P, Reyes AC, Kamerlin SCL, Richard JP, Gulick AM. Human Glycerol 3-Phosphate Dehydrogenase: X-Ray Crystal Structures that Guide the Interpretation of Mutagenesis Studies. Biochemistry. PMID 30640445 DOI: 10.1021/acs.biochem.8b01103 |
0.376 |
|
2019 |
Mydy LS, Cristobal JR, Katigbak RD, Bauer P, Reyes AC, Kamerlin SCL, Richard JP, Gulick AM. Human Glycerol 3-Phosphate Dehydrogenase : X-ray Crystal Structures That Guide the Interpretation of Mutagenesis Studies Biochemistry. 58: 1061-1073. DOI: 10.2210/Pdb6E8Z/Pdb |
0.439 |
|
2018 |
Hong NS, Petrović D, Lee R, Gryn'ova G, Purg M, Saunders J, Bauer P, Carr PD, Lin CY, Mabbitt PD, Zhang W, Altamore T, Easton C, Coote ML, Kamerlin SCL, et al. The evolution of multiple active site configurations in a designed enzyme. Nature Communications. 9: 3900. PMID 30254369 DOI: 10.1038/S41467-018-06305-Y |
0.778 |
|
2018 |
Maršavelski A, Petrović D, Bauer P, Vianello R, Kamerlin SCL. Empirical Valence Bond Simulations Suggest a Direct Hydride Transfer Mechanism for Human Diamine Oxidase. Acs Omega. 3: 3665-3674. PMID 30023875 DOI: 10.1021/acsomega.8b00346 |
0.69 |
|
2018 |
Janfalk Carlsson Å, Bauer P, Dobritzsch D, Kamerlin SCL, Widersten M. Epoxide hydrolysis as a model system for understanding flux through a branched reaction scheme. Iucrj. 5: 269-282. PMID 29755743 DOI: 10.1107/S2052252518003573 |
0.438 |
|
2018 |
Maurer D, Enugala TR, Hamnevik E, Bauer P, Lüking M, Petrović D, Hillier H, Kamerlin SCL, Dobritzsch D, Widersten M. Stereo- and Regioselectivity in Catalyzed Transformation of a 1,2-Disubstituted Vicinal Diol and the Corresponding Diketone by Wild Type and Laboratory Evolved Alcohol Dehydrogenases Acs Catalysis. 8: 7526-7538. DOI: 10.1021/Acscatal.8B01762 |
0.708 |
|
2018 |
Bauer P, Barrozo A, Amrein BA, Purg M, Esguerra M, Wilson PB, Major DT, Aqvist J, Kamerlin SCL. Q6: A comprehensive toolkit for empirical valence bond and related free energy calculations Softwarex. DOI: 10.1016/J.Softx.2017.12.001 |
0.626 |
|
2016 |
Janfalk Carlsson Å, Bauer P, Dobritzsch D, Nilsson M, Kamerlin SC, Widersten M. Laboratory Evolved Enzymes Provide Snapshots of the Development of Enantioconvergence in Enzyme-Catalyzed Epoxide Hydrolysis. Chembiochem : a European Journal of Chemical Biology. PMID 27383542 DOI: 10.1002/Cbic.201600330 |
0.733 |
|
2016 |
Bauer P, Carlsson ÅJ, Amrein BA, Dobritzsch D, Widersten M, Kamerlin SC. Conformational diversity and enantioconvergence in potato epoxide hydrolase 1. Organic & Biomolecular Chemistry. 14: 5639-51. PMID 27049844 DOI: 10.1039/C6Ob00060F |
0.768 |
|
2015 |
Amrein BA, Bauer P, Duarte F, Janfalk Carlsson Å, Naworyta A, Mowbray SL, Widersten M, Kamerlin SC. Expanding the Catalytic Triad in Epoxide Hydrolases and Related Enzymes. Acs Catalysis. 5: 5702-5713. PMID 26527505 DOI: 10.1021/Acscatal.5B01639 |
0.765 |
|
2015 |
Barrozo A, Duarte F, Bauer P, Carvalho AT, Kamerlin SC. Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily. Journal of the American Chemical Society. PMID 26091851 DOI: 10.1021/Jacs.5B03945 |
0.77 |
|
2014 |
Repi? M, Vianello R, Purg M, Duarte F, Bauer P, Kamerlin SC, Mavri J. Empirical valence bond simulations of the hydride transfer step in the monoamine oxidase B catalyzed metabolism of dopamine. Proteins. 82: 3347-55. PMID 25220264 DOI: 10.1002/Prot.24690 |
0.751 |
|
2014 |
Satpati P, Bauer P, Aqvist J. Energetic tuning by tRNA modifications ensures correct decoding of isoleucine and methionine on the ribosome. Chemistry (Weinheim An Der Bergstrasse, Germany). 20: 10271-5. PMID 25043149 DOI: 10.1002/Chem.201404016 |
0.306 |
|
2014 |
Duarte F, Bauer P, Barrozo A, Amrein BA, Purg M, Aqvist J, Kamerlin SC. Force field independent metal parameters using a nonbonded dummy model. The Journal of Physical Chemistry. B. 118: 4351-62. PMID 24670003 DOI: 10.1021/Jp501737X |
0.651 |
|
2012 |
Carlsson ÅJ, Bauer P, Ma H, Widersten M. Obtaining optical purity for product diols in enzyme-catalyzed epoxide hydrolysis: contributions from changes in both enantio- and regioselectivity. Biochemistry. 51: 7627-37. PMID 22931287 DOI: 10.1021/Bi3007725 |
0.433 |
|
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