| Year |
Citation |
Score |
| 2019 |
Baier F, Hong N, Yang G, Pabis A, Miton CM, Barrozo A, Carr PD, Kamerlin SC, Jackson CJ, Tokuriki N. Cryptic genetic variation shapes the adaptive evolutionary potential of enzymes. Elife. 8. PMID 30719972 DOI: 10.7554/Elife.40789 |
0.779 |
|
| 2019 |
Burke JR, La Clair JJ, Philippe RN, Pabis A, Corbella M, Jez JM, Cortina GA, Kaltenbach M, Bowman ME, Louie GV, Woods KB, Nelson AT, Tawfik DS, Kamerlin SC, Noel JP. Bifunctional Substrate Activation via an Arginine Residue Drives Catalysis in Chalcone Isomerases Acs Catalysis. 9: 8388-8396. DOI: 10.1021/Acscatal.9B01926 |
0.806 |
|
| 2018 |
Pabis A, Risso VA, Sanchez-Ruiz JM, Kamerlin SC. Cooperativity and flexibility in enzyme evolution. Current Opinion in Structural Biology. 48: 83-92. PMID 29141202 DOI: 10.1016/J.Sbi.2017.10.020 |
0.793 |
|
| 2017 |
Amrein BA, Steffen-Munsberg F, Szeler I, Purg M, Kulkarni Y, Kamerlin SC.
: Computer-Aided Directed Evolution of Enzymes. Iucrj. 4: 50-64. PMID 28250941 DOI: 10.1107/S2052252516018017 |
0.774 |
|
| 2016 |
Blaha-Nelson D, Krüger DM, Szeler K, Ben-David M, Kamerlin SC. Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1. Journal of the American Chemical Society. PMID 28026940 DOI: 10.1021/Jacs.6B10801 |
0.79 |
|
| 2016 |
Purg M, Pabis A, Baier F, Tokuriki N, Jackson C, Kamerlin SC. Probing the mechanisms for the selectivity and promiscuity of methyl parathion hydrolase. Philosophical Transactions. Series a, Mathematical, Physical, and Engineering Sciences. 374. PMID 27698033 DOI: 10.1098/Rsta.2016.0150 |
0.802 |
|
| 2016 |
Duarte F, Barrozo A, Aqvist J, Williams NH, Kamerlin SC. The Competing Mechanisms of Phosphate Monoester Dianion Hydrolysis. Journal of the American Chemical Society. PMID 27471914 DOI: 10.1021/Jacs.6B06277 |
0.801 |
|
| 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 |
0.726 |
|
| 2016 |
Pabis A, Duarte F, Kamerlin SC. Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer. Biochemistry. PMID 27187273 DOI: 10.1021/Acs.Biochem.6B00297 |
0.836 |
|
| 2016 |
Wallin C, Kulkarni YS, Abelein A, Jarvet J, Liao Q, Strodel B, Olsson L, Luo J, Abrahams JP, Sholts SB, Roos PM, Kamerlin SC, Gräslund A, Wärmländer SK. Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer's disease. Journal of Trace Elements in Medicine and Biology : Organ of the Society For Minerals and Trace Elements (Gms). PMID 27085215 DOI: 10.1016/J.Jtemb.2016.03.009 |
0.747 |
|
| 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 |
0.812 |
|
| 2016 |
Pabis A, Kamerlin SC. Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily. Current Opinion in Structural Biology. 37: 14-21. PMID 26716576 DOI: 10.1016/J.Sbi.2015.11.008 |
0.817 |
|
| 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 |
0.826 |
|
| 2015 |
Åqvist J, Kamerlin SC. Exceptionally large entropy contributions enable the high rates of GTP hydrolysis on the ribosome. Scientific Reports. 5: 15817. PMID 26497916 DOI: 10.1038/Srep15817 |
0.355 |
|
| 2015 |
Carvalho AT, Gouveia ML, Raju Kanna C, Wärmländer SK, Platts J, Kamerlin SC. Theoretical modelling of epigenetically modified DNA sequences. F1000research. 4: 52. PMID 26448859 DOI: 10.12688/F1000Research.6148.1 |
0.63 |
|
| 2015 |
Liao Q, Kamerlin SC, Strodel B. Development and Application of a Nonbonded Cu(2+) Model That Includes the Jahn-Teller Effect. The Journal of Physical Chemistry Letters. 6: 2657-62. PMID 26167255 DOI: 10.1021/Acs.Jpclett.5B01122 |
0.683 |
|
| 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 |
0.833 |
|
| 2015 |
Carvalho AT, O'Donoghue AC, Hodgson DR, Kamerlin SC. Understanding thio-effects in simple phosphoryl systems: role of solvent effects and nucleophile charge. Organic & Biomolecular Chemistry. 13: 5391-8. PMID 25797408 DOI: 10.1039/C5Ob00309A |
0.639 |
|
| 2015 |
Carvalho AT, Szeler K, Vavitsas K, Qvist J, Kamerlin SC. Modeling the mechanisms of biological GTP hydrolysis. Archives of Biochemistry and Biophysics. PMID 25731854 DOI: 10.1016/J.Abb.2015.02.027 |
0.811 |
|
| 2015 |
Ben-David M, Sussman JL, Maxwell CI, Szeler K, Kamerlin SC, Tawfik DS. Catalytic stimulation by restrained active-site floppiness--the case of high density lipoprotein-bound serum paraoxonase-1. Journal of Molecular Biology. 427: 1359-74. PMID 25644661 DOI: 10.1016/J.Jmb.2015.01.013 |
0.784 |
|
| 2015 |
Åqvist J, Kamerlin SC. The conformation of a catalytic loop is central to GTPase activity on the ribosome. Biochemistry. 54: 546-56. PMID 25515218 DOI: 10.1021/Bi501373G |
0.447 |
|
| 2015 |
Duarte F, Åqvist J, Williams NH, Kamerlin SC. Resolving apparent conflicts between theoretical and experimental models of phosphate monoester hydrolysis. Journal of the American Chemical Society. 137: 1081-93. PMID 25423607 DOI: 10.1021/Ja5082712 |
0.659 |
|
| 2015 |
Shurki A, Derat E, Barrozo A, Kamerlin SC. How valence bond theory can help you understand your (bio)chemical reaction. Chemical Society Reviews. 44: 1037-52. PMID 25352378 DOI: 10.1039/C4Cs00241E |
0.731 |
|
| 2015 |
Duarte F, Amrein BA, Blaha-Nelson D, Kamerlin SC. Recent advances in QM/MM free energy calculations using reference potentials. Biochimica Et Biophysica Acta. 1850: 954-965. PMID 25038480 DOI: 10.1016/J.Bbagen.2014.07.008 |
0.783 |
|
| 2014 |
Carvalho AT, Gouveia L, Kanna CR, Wärmländer SK, Platts JA, Kamerlin SC. Understanding the structural and dynamic consequences of DNA epigenetic modifications: computational insights into cytosine methylation and hydroxymethylation. Epigenetics : Official Journal of the Dna Methylation Society. 9: 1604-12. PMID 25625845 DOI: 10.4161/15592294.2014.988043 |
0.596 |
|
| 2014 |
Carvalho AT, Barrozo A, Doron D, Kilshtain AV, Major DT, Kamerlin SC. Challenges in computational studies of enzyme structure, function and dynamics. Journal of Molecular Graphics & Modelling. 54: 62-79. PMID 25306098 DOI: 10.1016/J.Jmgm.2014.09.003 |
0.81 |
|
| 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 |
0.795 |
|
| 2014 |
O'Donoghue AC, Kamerlin SC. Editorial overview: Mechanisms: Chemical and computational probes of biological mechanism. Current Opinion in Chemical Biology. 21: viii-x. PMID 25129687 DOI: 10.1016/J.Cbpa.2014.07.025 |
0.31 |
|
| 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 |
0.753 |
|
| 2014 |
Duarte F, Gronert S, Kamerlin SC. Concerted or stepwise: how much do free-energy landscapes tell us about the mechanisms of elimination reactions? The Journal of Organic Chemistry. 79: 1280-8. PMID 24404911 DOI: 10.1021/Jo402702M |
0.615 |
|
| 2014 |
Duarte F, Geng T, Marloie G, Al Hussain AO, Williams NH, Kamerlin SC. The alkaline hydrolysis of sulfonate esters: challenges in interpreting experimental and theoretical data. The Journal of Organic Chemistry. 79: 2816-28. PMID 24279349 DOI: 10.1021/Jo402420T |
0.757 |
|
| 2013 |
Duarte F, Amrein BA, Kamerlin SC. Modeling catalytic promiscuity in the alkaline phosphatase superfamily. Physical Chemistry Chemical Physics : Pccp. 15: 11160-77. PMID 23728154 DOI: 10.1039/C3Cp51179K |
0.827 |
|
| 2013 |
Wallin G, Kamerlin SC, Aqvist J. Energetics of activation of GTP hydrolysis on the ribosome. Nature Communications. 4: 1733. PMID 23591900 DOI: 10.1038/Ncomms2741 |
0.414 |
|
| 2013 |
Kamerlin SC, Sharma PK, Prasad RB, Warshel A. Why nature really chose phosphate. Quarterly Reviews of Biophysics. 46: 1-132. PMID 23318152 DOI: 10.1017/S0033583512000157 |
0.687 |
|
| 2012 |
Borštnar R, Repič M, Kamerlin SC, Vianello R, Mavri J. Computational Study of the pKa Values of Potential Catalytic Residues in the Active Site of Monoamine Oxidase B. Journal of Chemical Theory and Computation. 8: 3864-70. PMID 26593027 DOI: 10.1021/Ct300119U |
0.395 |
|
| 2012 |
Barrozo A, Borstnar R, Marloie G, Kamerlin SC. Computational protein engineering: bridging the gap between rational design and laboratory evolution. International Journal of Molecular Sciences. 13: 12428-60. PMID 23202907 DOI: 10.3390/Ijms131012428 |
0.8 |
|
| 2012 |
Kudavalli JS, Rao SN, Bean DE, Sharma ND, Boyd DR, Fowler PW, Gronert S, Kamerlin SC, Keeffe JR, More O'Ferrall RA. Base-catalyzed dehydration of 3-substituted benzene cis-1,2-dihydrodiols: stabilization of a cyclohexadienide anion intermediate by negative aromatic hyperconjugation. Journal of the American Chemical Society. 134: 14056-69. PMID 22830996 DOI: 10.1021/Ja304366J |
0.317 |
|
| 2012 |
Luo J, van Loo B, Kamerlin SC. Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution. Febs Letters. 586: 1622-30. PMID 22673572 DOI: 10.1016/J.Febslet.2012.04.012 |
0.5 |
|
| 2012 |
Luo J, van Loo B, Kamerlin SC. Examining the promiscuous phosphatase activity of Pseudomonas aeruginosa arylsulfatase: a comparison to analogous phosphatases. Proteins. 80: 1211-26. PMID 22275090 DOI: 10.1002/Prot.24020 |
0.538 |
|
| 2011 |
Kamerlin SC. Theoretical comparison of p-nitrophenyl phosphate and sulfate hydrolysis in aqueous solution: implications for enzyme-catalyzed sulfuryl transfer. The Journal of Organic Chemistry. 76: 9228-38. PMID 21981415 DOI: 10.1021/Jo201104V |
0.478 |
|
| 2011 |
Adamczyk AJ, Cao J, Kamerlin SC, Warshel A. Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions. Proceedings of the National Academy of Sciences of the United States of America. 108: 14115-20. PMID 21831831 DOI: 10.1073/Pnas.1111252108 |
0.781 |
|
| 2011 |
Kamerlin SC, Wilkie J. The effect of leaving group on mechanistic preference in phosphate monoester hydrolysis. Organic & Biomolecular Chemistry. 9: 5394-406. PMID 21655563 DOI: 10.1039/C0Ob01210F |
0.565 |
|
| 2011 |
Plotnikov NV, Kamerlin SC, Warshel A. Paradynamics: an effective and reliable model for ab initio QM/MM free-energy calculations and related tasks. The Journal of Physical Chemistry. B. 115: 7950-62. PMID 21618985 DOI: 10.1021/Jp201217B |
0.772 |
|
| 2011 |
Kamerlin SC, Warshel A. Multiscale modeling of biological functions. Physical Chemistry Chemical Physics : Pccp. 13: 10401-11. PMID 21526232 DOI: 10.1039/C0Cp02823A |
0.531 |
|
| 2011 |
Kamerlin SC, Vicatos S, Dryga A, Warshel A. Coarse-grained (multiscale) simulations in studies of biophysical and chemical systems. Annual Review of Physical Chemistry. 62: 41-64. PMID 21034218 DOI: 10.1146/Annurev-Physchem-032210-103335 |
0.77 |
|
| 2010 |
Kamerlin SC, Warshel A. The EVB as a quantitative tool for formulating simulations and analyzing biological and chemical reactions. Faraday Discussions. 145: 71-106. PMID 25285029 DOI: 10.1039/B907354J |
0.593 |
|
| 2010 |
Kamerlin SC, Warshel A. An Analysis of All the Relevant Facts and Arguments Indicates that Enzyme Catalysis Does Not Involve Large Contributions from Nuclear Tunneling. Journal of Physical Organic Chemistry. 23: 677-684. PMID 21494414 DOI: 10.1002/Poc.1620 |
0.654 |
|
| 2010 |
Kamerlin SC, Chu ZT, Warshel A. On catalytic preorganization in oxyanion holes: highlighting the problems with the gas-phase modeling of oxyanion holes and illustrating the need for complete enzyme models. The Journal of Organic Chemistry. 75: 6391-401. PMID 20825150 DOI: 10.1021/Jo100651S |
0.561 |
|
| 2010 |
Kamerlin SC, Mavri J, Warshel A. Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues. Febs Letters. 584: 2759-66. PMID 20433839 DOI: 10.1016/J.Febslet.2010.04.062 |
0.502 |
|
| 2010 |
Kamerlin SC, Sharma PK, Chu ZT, Warshel A. Ketosteroid isomerase provides further support for the idea that enzymes work by electrostatic preorganization. Proceedings of the National Academy of Sciences of the United States of America. 107: 4075-80. PMID 20150513 DOI: 10.1073/Pnas.0914579107 |
0.724 |
|
| 2010 |
Kamerlin SC, Warshel A. At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins. 78: 1339-75. PMID 20099310 DOI: 10.1002/Prot.22654 |
0.634 |
|
| 2009 |
Kamerlin SC, Warshel A. On the energetics of ATP hydrolysis in solution. The Journal of Physical Chemistry. B. 113: 15692-8. PMID 19888735 DOI: 10.1021/Jp907223T |
0.537 |
|
| 2009 |
Pisliakov AV, Cao J, Kamerlin SC, Warshel A. Enzyme millisecond conformational dynamics do not catalyze the chemical step. Proceedings of the National Academy of Sciences of the United States of America. 106: 17359-64. PMID 19805169 DOI: 10.1073/Pnas.0909150106 |
0.656 |
|
| 2009 |
Kamerlin SC, Cao J, Rosta E, Warshel A. On unjustifiably misrepresenting the EVB approach while simultaneously adopting it. The Journal of Physical Chemistry. B. 113: 10905-15. PMID 19606825 DOI: 10.1021/Jp901709F |
0.707 |
|
| 2009 |
Kamerlin SC, McKenna CE, Goodman MF, Goondman MF, Warshel A. A computational study of the hydrolysis of dGTP analogues with halomethylene-modified leaving groups in solution: implications for the mechanism of DNA polymerases. Biochemistry. 48: 5963-71. PMID 19391628 DOI: 10.1021/Bi900140C |
0.573 |
|
| 2009 |
Kamerlin SC, Haranczyk M, Warshel A. Are mixed explicit/implicit solvation models reliable for studying phosphate hydrolysis? A comparative study of continuum, explicit and mixed solvation models. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 10: 1125-34. PMID 19301306 DOI: 10.1002/Cphc.200800753 |
0.534 |
|
| 2009 |
Kamerlin SC, Haranczyk M, Warshel A. Progress in ab initio QM/MM free-energy simulations of electrostatic energies in proteins: accelerated QM/MM studies of pKa, redox reactions and solvation free energies. The Journal of Physical Chemistry. B. 113: 1253-72. PMID 19055405 DOI: 10.1021/Jp8071712 |
0.567 |
|
| 2008 |
Kamerlin SC, Williams NH, Warshel A. Dineopentyl phosphate hydrolysis: evidence for stepwise water attack. The Journal of Organic Chemistry. 73: 6960-9. PMID 18729515 DOI: 10.1021/Jo801207Q |
0.595 |
|
| 2008 |
Kamerlin SC, Florián J, Warshel A. Associative versus dissociative mechanisms of phosphate monoester hydrolysis: on the interpretation of activation entropies. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 9: 1767-73. PMID 18666265 DOI: 10.1002/Cphc.200800356 |
0.547 |
|
| 2008 |
Rosta E, Kamerlin SC, Warshel A. On the interpretation of the observed linear free energy relationship in phosphate hydrolysis: a thorough computational study of phosphate diester hydrolysis in solution. Biochemistry. 47: 3725-35. PMID 18307312 DOI: 10.1021/Bi702106M |
0.711 |
|
| 2007 |
Kamerlin SC, Wilkie J. The role of metal ions in phosphate ester hydrolysis. Organic & Biomolecular Chemistry. 5: 2098-108. PMID 17581653 DOI: 10.1039/B701274H |
0.562 |
|
| 2007 |
Kamerlin SC, Rucker R, Boresch S. A molecular dynamics study of WPD-loop flexibility in PTP1B. Biochemical and Biophysical Research Communications. 356: 1011-6. PMID 17408595 DOI: 10.1016/J.Bbrc.2007.03.093 |
0.661 |
|
| 2006 |
Kamerlin SC, Rucker R, Boresch S. A targeted molecular dynamics study of WPD loop movement in PTP1B. Biochemical and Biophysical Research Communications. 345: 1161-6. PMID 16713994 DOI: 10.1016/J.Bbrc.2006.04.181 |
0.663 |
|
| Show low-probability matches. |
