Abstract
Kerstin Steiner, Helmut Schwab
Abstract
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10.1038/nature11117
10.1038/nature11117
10.1002/9783527639861
10.1002/9783527639861 · 2012
10.1002/adsc.201100446
10.1002/adsc.201100446
10.1016/j.cbpa.2010.11.011
10.1016/j.cbpa.2010.11.011
10.1016/j.cbpa.2010.11.020
10.1016/j.cbpa.2010.11.020
10.1016/j.cbpa.2009.01.014
10.1016/j.cbpa.2009.01.014
10.1016/j.copbio.2010.08.011
10.1016/j.copbio.2010.08.011
10.1002/anie.201000826
10.1002/anie.201000826
10.1021/cr100386u
10.1021/cr100386u
10.1016/j.copbio.2005.06.004
10.1016/j.copbio.2005.06.004
10.1002/anie.201107813
10.1002/anie.201107813
Mapping the Substrate Binding Site of Phenylacetone Monooxygenase from Thermobifida fusca by Mutational Analysis
10.1128/aem.00687-11 · 2011
Directed Evolution of Enantioselective Enzymes: Iterative Cycles of CASTing for Probing Protein-Sequence Space
10.1002/anie.200502746 · 2006
10.1073/pnas.1012985107
10.1073/pnas.1012985107
10.1002/pro.2096
10.1002/pro.2096
10.1016/j.copbio.2009.07.008
10.1016/j.copbio.2009.07.008
10.1016/j.chembiol.2010.10.012
10.1016/j.chembiol.2010.10.012
10.1073/pnas.0609647103
10.1073/pnas.0609647103
Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution
10.1016/s0958-1669(00)00229-9 · 2001
The consensus concept for thermostability engineering of proteins: further proof of concept
10.1093/protein/15.5.403 · 2002
10.1128/aem.07985-11
10.1128/aem.07985-11
The effect of proline insertions on the thermostability of a barley α-glucosidase
10.1093/protein/15.1.29 · 2002
Enhanced thermostability of methyl parathion hydrolase from Ochrobactrum sp. M231 by rational engineering of a glycine to proline mutation
10.1111/j.1742-4658.2010.07895.x · 2010
10.1016/j.tibtech.2005.03.005
10.1016/j.tibtech.2005.03.005
10.1002/biot.200600029
10.1002/biot.200600029
Sequence statistics reliably predict stabilizing mutations in a protein domain
10.1006/jmbi.1994.1434 · 1994
10.1002/cbic.200700500
10.1002/cbic.200700500
10.1093/protein/gzn048
10.1093/protein/gzn048
Improved thermostability of AEH by combining B-FIT analysis and structure-guided consensus method
10.1016/j.jbiotec.2012.02.014 · 2012
Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention
10.1002/pro.2031 · 2012
Protein thermal stability: insights from atomic displacement parameters (B values)
10.1093/protein/13.1.9 · 2000
10.1002/ange.200602795
10.1002/ange.200602795
Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method
10.1039/c0cc02657c · 2010
10.1016/j.cbpa.2011.03.005
10.1016/j.cbpa.2011.03.005
10.1038/nature06510
10.1038/nature06510
10.1073/pnas.0707158104
10.1073/pnas.0707158104
10.1016/j.jmb.2005.10.011
10.1016/j.jmb.2005.10.011
10.1093/protein/gzq021
10.1093/protein/gzq021
The α/β-Hydrolase Fold 3DM Database (ABHDB) as a Tool for Protein Engineering
10.1002/cbic.201000213 · 2010
10.1002/prot.22374
10.1002/prot.22374
Hydroxynitrile Lyases: Insights into Biochemistry, Discovery and Engineering
10.1021/cs200325q · doi-reference
Correlated Mutations: A Hallmark of Phenotypic Amino Acid Substitutions
10.1371/journal.pcbi.1000923 · doi-reference
10.1371/journal.pcbi.1000002
10.1371/journal.pcbi.1000002 · doi-reference
The tryptophane residues of dimeric arginine kinase: roles of Trp-208 and Trp-218 in active site and conformation stability
10.1016/j.biochi.2004.05.006 · doi-reference
10.1038/nchembio.777
10.1038/nchembio.777 · doi-reference
Rational design of a nitrite reductase based on myoglobin: a molecular modeling and dynamics simulation study
10.1007/s00894-012-1451-y · doi-reference
10.1038/nature08620
10.1038/nature08620 · doi-reference
10.1073/pnas.1000526107
10.1073/pnas.1000526107 · doi-reference
Introducing a 2-His-1-Glu Nonheme Iron Center into Myoglobin Confers Nitric Oxide Reductase Activity
10.1021/ja103516n · doi-reference
10.1002/anie.201002106
10.1002/anie.201002106 · doi-reference
Artificial Dicopper Oxidase: Rational Reprogramming of Bacterial Metallo-β-lactamase into a Catechol Oxidase
10.1002/asia.201101014 · doi-reference
10.1002/cctc.201000159
10.1002/cctc.201000159 · doi-reference
Stereoselective Hydrogenation of Olefins Using Rhodium-Substituted Carbonic Anhydrase-A New Reductase
10.1002/chem.200801673 · doi-reference
Manganese-Substituted Carbonic Anhydrase as a New Peroxidase
10.1002/chem.200501413 · doi-reference
Transforming Carbonic Anhydrase into Epoxide Synthase by Metal Exchange
10.1002/cbic.200600127 · doi-reference
Directed evolution of the promiscuous esterase activity of carbonic anhydrase II
10.1021/bi0475471 · doi-reference
From Kinase to Cyclase: An Unusual Example of Catalytic Promiscuity Modulated by Metal Switching
10.1002/cbic.200800573 · doi-reference
10.1002/cbic.200900688
10.1002/cbic.200900688 · doi-reference
10.1002/chem.201003646
10.1002/chem.201003646 · doi-reference
10.1002/cctc.201000011
10.1002/cctc.201000011 · doi-reference
10.1073/pnas.1118082108
10.1073/pnas.1118082108 · doi-reference
10.1073/pnas.0607691103
10.1073/pnas.0607691103 · doi-reference
10.1073/pnas.1121063109
10.1073/pnas.1121063109 · doi-reference
10.1038/nature06879
10.1038/nature06879 · doi-reference
10.1016/j.jmb.2011.01.041
10.1016/j.jmb.2011.01.041 · doi-reference
10.1016/j.jmb.2009.12.031
10.1016/j.jmb.2009.12.031 · doi-reference
10.1126/science.1152692
10.1126/science.1152692 · doi-reference
10.1002/pro.2059
10.1002/pro.2059 · doi-reference
10.1016/j.jmb.2011.10.043
10.1016/j.jmb.2011.10.043 · doi-reference
10.1021/ja905396s
10.1021/ja905396s · doi-reference
10.1073/pnas.0913638107
10.1073/pnas.0913638107 · doi-reference
10.1002/pro.462
10.1002/pro.462 · doi-reference
Challenges and advances in validating enzyme design proposals: The case of the kemp eliminase catalysis
10.1021/bi200063a · doi-reference
Exploring challenges in rational enzyme design by simulating the catalysis in artificial kemp eliminase
10.1073/pnas.1010381107 · doi-reference
10.1002/pro.481
10.1002/pro.481 · doi-reference
10.1016/j.biortech.2012.01.054
10.1016/j.biortech.2012.01.054 · doi-reference
10.1002/pro.2055
10.1002/pro.2055 · doi-reference
10.1371/journal.pone.0019230
10.1371/journal.pone.0019230 · doi-reference
10.1016/b978-0-12-381270-4.00019-6
10.1016/b978-0-12-381270-4.00019-6 · doi-reference
10.1110/ps.062353106
10.1110/ps.062353106 · doi-reference