Research graph
References from RECENT ADVANCES IN RATIONAL APPROACHES FOR ENZYME ENGINEERING. Local targets link to admitted publications; unresolved targets remain external evidence.
10.1038/nature11117
10.1038/nature11117 · External reference
10.1002/9783527639861
10.1002/9783527639861 · 2012 · External reference
10.1002/adsc.201100446
10.1002/adsc.201100446 · External reference
10.1016/j.cbpa.2010.11.011
10.1016/j.cbpa.2010.11.011 · External reference
10.1016/j.cbpa.2010.11.020
10.1016/j.cbpa.2010.11.020 · External reference
10.1016/j.cbpa.2009.01.014
10.1016/j.cbpa.2009.01.014 · External reference
10.1016/j.copbio.2010.08.011
10.1016/j.copbio.2010.08.011 · External reference
10.1002/anie.201000826
10.1002/anie.201000826 · External reference
10.1021/cr100386u
10.1021/cr100386u · External reference
10.1016/j.copbio.2005.06.004
10.1016/j.copbio.2005.06.004 · External reference
10.1002/anie.201107813
10.1002/anie.201107813 · External reference
Mapping the Substrate Binding Site of Phenylacetone Monooxygenase from Thermobifida fusca by Mutational Analysis
10.1128/aem.00687-11 · 2011 · External reference
Directed Evolution of Enantioselective Enzymes: Iterative Cycles of CASTing for Probing Protein-Sequence Space
10.1002/anie.200502746 · 2006 · External reference
10.1073/pnas.1012985107
10.1073/pnas.1012985107 · External reference
10.1002/pro.2096
10.1002/pro.2096 · External reference
10.1016/j.copbio.2009.07.008
10.1016/j.copbio.2009.07.008 · External reference
10.1016/j.chembiol.2010.10.012
10.1016/j.chembiol.2010.10.012 · External reference
10.1073/pnas.0609647103
10.1073/pnas.0609647103 · External reference
Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution
10.1016/s0958-1669(00)00229-9 · 2001 · External reference
The consensus concept for thermostability engineering of proteins: further proof of concept
10.1093/protein/15.5.403 · 2002 · External reference
10.1128/aem.07985-11
10.1128/aem.07985-11 · External reference
The effect of proline insertions on the thermostability of a barley α-glucosidase
10.1093/protein/15.1.29 · 2002 · External reference
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 · External reference
10.1016/j.tibtech.2005.03.005
10.1016/j.tibtech.2005.03.005 · External reference
10.1002/biot.200600029
10.1002/biot.200600029 · External reference
Sequence statistics reliably predict stabilizing mutations in a protein domain
10.1006/jmbi.1994.1434 · 1994 · External reference
10.1002/cbic.200700500
10.1002/cbic.200700500 · External reference
10.1093/protein/gzn048
10.1093/protein/gzn048 · External reference
Improved thermostability of AEH by combining B-FIT analysis and structure-guided consensus method
10.1016/j.jbiotec.2012.02.014 · 2012 · External reference
Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention
10.1002/pro.2031 · 2012 · External reference
Protein thermal stability: insights from atomic displacement parameters (B values)
10.1093/protein/13.1.9 · 2000 · External reference
10.1002/ange.200602795
10.1002/ange.200602795 · External reference
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 · External reference
10.1016/j.cbpa.2011.03.005
10.1016/j.cbpa.2011.03.005 · External reference
10.1038/nature06510
10.1038/nature06510 · External reference
10.1073/pnas.0707158104
10.1073/pnas.0707158104 · External reference
10.1016/j.jmb.2005.10.011
10.1016/j.jmb.2005.10.011 · External reference
10.1093/protein/gzq021
10.1093/protein/gzq021 · External reference
The α/β-Hydrolase Fold 3DM Database (ABHDB) as a Tool for Protein Engineering
10.1002/cbic.201000213 · 2010 · External reference
10.1002/prot.22374
10.1002/prot.22374 · External reference
3DM: Systematic analysis of heterogeneous superfamily data to discover protein functionalities
2010 · External reference
Natural Diversity to Guide Focused Directed Evolution
10.1002/cbic.201000284 · 2010 · External reference
10.1093/protein/gzq071
10.1093/protein/gzq071 · External reference
Rational Protein Design of Paenibacillus barcinonensis Esterase EstA for Kinetic Resolution of Tertiary Alcohols
10.1002/cctc.201000053 · 2010 · External reference
Increasing the thermostability of sucrose phosphorylase by a combination of sequence- and structure-based mutagenesis
10.1093/protein/gzr042 · 2011 · External reference
Identification of a Gatekeeper Residue That Prevents Dehydrogenases from Acting as Oxidases
10.1074/jbc.m808202200 · 2009 · External reference
Molecular Characterization of the C-Methyltransferase NovO of Streptomyces spheroides, a valuable enzyme for performing Friedel-Crafts alkylation
10.1016/j.molcatb.2012.03.016 · 2012 · External reference
Library analysis of SCHEMA-guided protein recombination
10.1110/ps.0306603 · 2003 · External reference
Structure-guided SCHEMA recombination of distantly related beta-lactamases
10.1093/protein/gzl045 · 2006 · External reference
Structure-guided recombination creates an artificial family of cytochromes P450
2006 · External reference
10.1074/jbc.c109.034058
10.1074/jbc.c109.034058 · External reference
Efficient screening of fungal cellobiohydrolase class I enzymes for thermostabilizing sequence blocks by SCHEMA structure-guided recombination
10.1093/protein/gzq063 · 2010 · External reference
A diverse family of thermostable cytochrome P450s created by recombination of stabilizing fragments
10.1038/nbt1333 · 2007 · External reference
10.1016/j.chembiol.2007.01.009
10.1016/j.chembiol.2007.01.009 · External reference
Blending Baeyer-Villiger monooxygenases: using a robust BVMO as a scaffold for creating chimeric enzymes with novel catalytic properties
10.1039/c2cc17656d · 2012 · External reference
10.1016/j.sbi.2011.05.002
10.1016/j.sbi.2011.05.002 · External reference
Biocatalytic Promiscuity
2011 · External reference
10.1002/anie.200460416
10.1002/anie.200460416 · External reference
Enzyme promiscuity: mechanism and applications
10.1016/j.tibtech.2007.03.002 · 2007 · External reference
10.1016/j.cbpa.2005.02.008
10.1016/j.cbpa.2005.02.008 · External reference
Introduction of single mutation changes arylmalonate decarboxylase to racemase
10.1039/b607211a · 2006 · External reference
Conversion of Pyruvate Decarboxylase into an Enantioselective Carboligase with Biosynthetic Potential
10.1021/ja110236w · 2011 · External reference
10.1021/ja036707d
10.1021/ja036707d · External reference
10.1002/anie.200602529
10.1002/anie.200602529 · External reference
10.1002/anie.200700710
10.1002/anie.200700710 · External reference
Conversion of the catalytic specificity of alanine racemase to a D-amino acid aminotransferase activity by a double active-site mutation
10.1016/s1381-1177(03)00094-8 · 2003 · External reference
Protein Engineering of alpha/beta-Hydrolase Fold Enzymes
10.1002/cbic.201000771 · 2011 · External reference
Molecular basis of perhydrolase activity in serine hydrolases
10.1002/anie.200463006 · 2005 · External reference
Revised Molecular Basis of the Promiscuous Carboxylic Acid Perhydrolase Activity in Serine Hydrolases
10.1002/chem.201200052 · 2012 · External reference
Unresolved reference
External reference
10.1016/j.chembiol.2010.06.013
10.1016/j.chembiol.2010.06.013 · External reference
10.1002/anie.200806276
10.1002/anie.200806276 · External reference
Understanding promiscuous amidase activity of an esterase from Bacillus subtilis
10.1002/cbic.200700521 · 2008 · External reference
Promiscuous enantioselective (-)- γ-lactamase activity in the Pseudomonas fluorescens esterase I
10.1039/c2ob06887g · 2012 · External reference
10.1002/cctc.201000448
10.1002/cctc.201000448 · External reference
Rational redesign of a lipase to an aldolase
2003 · External reference
10.1002/cbic.200400213
10.1002/cbic.200400213 · External reference
10.1021/ja056660r
10.1021/ja056660r · External reference
Suppressed Native Hydrolytic Activity of a Lipase to Reveal Promiscuous Michael Addition Activity in Water
10.1002/cctc.200900041 · 2009 · External reference
Investigation of lipase-catalyzed Michael-type carbon-carbon bond formations
10.1016/j.tet.2009.05.042 · 2009 · External reference
10.1002/chem.201002265
10.1002/chem.201002265 · External reference
Screening for hydroxynitrile lyases in plants
10.1007/bf02764453 · 1997 · External reference
Lipase CAL-B does not catalyze a promiscuous decarboxylative aldol addition or Knoevenagel reaction
10.1039/c0gc00505c · 2011 · External reference
Carving the active site of almond R-HNL for increased enantioselectivity
10.1002/anie.200500435 · 2005 · External reference
Substrate specificity of mutants of the hydroxynitrile lyase from Manihot esculenta
10.1002/cbic.200390033 · 2003 · External reference
Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta
10.1110/ps.33702 · 2002 · External reference
Unresolved reference
2012 · External reference
Redesigning dehalogenase access tunnels as a strategy for degrading an anthropogenic substrate
10.1038/nchembio.205 · 2009 · External reference
Redesign of enzyme for improving catalytic activity and enantioselectivity toward poor substrates: manipulation of the transition state
10.1039/c2ob25614b · 2012 · External reference
10.1039/c0cc02961k
10.1039/c0cc02961k · External reference
Biocatalytic Asymmetric Synthesis of Chiral Amines from Ketones Applied to Sitagliptin Manufacture
10.1126/science.1188934 · 2010 · External reference
10.1002/bit.21591
10.1002/bit.21591 · External reference
Key Amino Acid Residues for Reversed or Improved Enantiospecificity of an ω-Transaminase
10.1002/cctc.201100487 · 2012 · External reference
Reversed Enantiopreference of an omega-Transaminase by a Single-Point Mutation
10.1002/cctc.201000107 · 2010 · External reference
10.1021/cs300116n
10.1021/cs300116n · External reference
Inverting enantioselectivity of Burkholderia gladioli esterase EstB by directed and designed evolution
10.1016/j.jbiotec.2006.10.007 · 2007 · External reference
Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a Bacillus subtilis esterase
10.1002/anie.200704606 · 2008 · External reference
Engineering Candida tenuis xylose reductase for improved utilization of NADH: Antagonistic effects of multiple side chain replacements and performance of site-directed mutants under simulated in vivo conditions
10.1128/aem.71.10.6390-6393.2005 · 2005 · External reference
Altering the coenzyme preference of xylose reductase to favor utilization of NADH enhances ethanol yield from xylose in a metabolically engineered strain of Saccharomyces cerevisiae
10.1186/1475-2859-7-9 · 2008 · External reference
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
10.1021/bi035018b · 2003 · External reference
Conversion of cofactor specificities of alanine dehydrogenases by site-directed mutagenesis
10.1016/j.molcatb.2004.04.008 · 2004 · External reference
Investigating the coenzyme specificity of phenylacetone monooxygenase from Thermobifida fusca
10.1007/s00253-010-2769-y · 2010 · External reference
NAD(P)H oxidase V from Lactobacillus plantarum (NoxV) displays enhanced operational stability even in absence of reducing agents
10.1016/j.molcatb.2011.04.013 · 2011 · External reference
10.1126/science.278.5335.82
10.1126/science.278.5335.82 · External reference
10.1038/nature08304
10.1038/nature08304 · External reference
10.1038/nchem.473
10.1038/nchem.473 · External reference
10.1016/j.cbpa.2011.03.006
10.1016/j.cbpa.2011.03.006 · External reference
10.1073/pnas.251555398
10.1073/pnas.251555398 · External reference
10.1016/j.cbpa.2009.02.021
10.1016/j.cbpa.2009.02.021 · External reference
10.1016/j.sbi.2011.04.005
10.1016/j.sbi.2011.04.005 · External reference
Challenges in the computational design of proteins
10.1098/rsif.2008.0508.focus · 2009 · External reference
10.1110/ps.062353106
10.1110/ps.062353106 · External reference
10.1016/b978-0-12-381270-4.00019-6
10.1016/b978-0-12-381270-4.00019-6 · External reference
10.1371/journal.pone.0019230
10.1371/journal.pone.0019230 · External reference
10.1002/pro.2055
10.1002/pro.2055 · External reference
10.1016/j.biortech.2012.01.054
10.1016/j.biortech.2012.01.054 · External reference
10.1002/pro.481
10.1002/pro.481 · External reference
Exploring challenges in rational enzyme design by simulating the catalysis in artificial kemp eliminase
10.1073/pnas.1010381107 · 2010 · External reference
Challenges and advances in validating enzyme design proposals: The case of the kemp eliminase catalysis
10.1021/bi200063a · 2011 · External reference
10.1002/pro.462
10.1002/pro.462 · External reference
10.1073/pnas.0913638107
10.1073/pnas.0913638107 · External reference
10.1021/ja905396s
10.1021/ja905396s · External reference
10.1016/j.jmb.2011.10.043
10.1016/j.jmb.2011.10.043 · External reference
10.1002/pro.2059
10.1002/pro.2059 · External reference
10.1126/science.1152692
10.1126/science.1152692 · External reference
10.1016/j.jmb.2009.12.031
10.1016/j.jmb.2009.12.031 · External reference
10.1016/j.jmb.2011.01.041
10.1016/j.jmb.2011.01.041 · External reference
10.1038/nature06879
10.1038/nature06879 · External reference
10.1073/pnas.1121063109
10.1073/pnas.1121063109 · External reference
10.1073/pnas.0607691103
10.1073/pnas.0607691103 · External reference
10.1073/pnas.1118082108
10.1073/pnas.1118082108 · External reference
10.1073/pnas.1018191108
10.1073/pnas.1018191108 · External reference
Engineering a model protein cavity to catalyze the Kemp elimination
2012 · External reference
10.1038/373228a0
10.1038/373228a0 · External reference
10.1038/383060a0
10.1038/383060a0 · External reference
10.1126/science.1190239
10.1126/science.1190239 · External reference
10.1038/nature09304
10.1038/nature09304 · External reference
10.1038/nbt.2109
10.1038/nbt.2109 · External reference
Computational design of catalytic dyads and oxyanion holes for ester hydrolysis
2012 · External reference
10.1002/cctc.201000011
10.1002/cctc.201000011 · External reference
10.1002/chem.201003646
10.1002/chem.201003646 · External reference
10.1002/cbic.200900688
10.1002/cbic.200900688 · External reference
From Kinase to Cyclase: An Unusual Example of Catalytic Promiscuity Modulated by Metal Switching
10.1002/cbic.200800573 · 2009 · External reference
Directed evolution of the promiscuous esterase activity of carbonic anhydrase II
10.1021/bi0475471 · 2005 · External reference
Transforming Carbonic Anhydrase into Epoxide Synthase by Metal Exchange
10.1002/cbic.200600127 · 2006 · External reference
Manganese-Substituted Carbonic Anhydrase as a New Peroxidase
10.1002/chem.200501413 · 2006 · External reference
Stereoselective Hydrogenation of Olefins Using Rhodium-Substituted Carbonic Anhydrase-A New Reductase
10.1002/chem.200801673 · 2009 · External reference
10.1002/cctc.201000159
10.1002/cctc.201000159 · External reference
Artificial Dicopper Oxidase: Rational Reprogramming of Bacterial Metallo-β-lactamase into a Catechol Oxidase
10.1002/asia.201101014 · 2012 · External reference
10.1002/anie.201002106
10.1002/anie.201002106 · External reference
Introducing a 2-His-1-Glu Nonheme Iron Center into Myoglobin Confers Nitric Oxide Reductase Activity
10.1021/ja103516n · 2010 · External reference
10.1073/pnas.1000526107
10.1073/pnas.1000526107 · External reference
10.1038/nature08620
10.1038/nature08620 · External reference
Rational design of a nitrite reductase based on myoglobin: a molecular modeling and dynamics simulation study
10.1007/s00894-012-1451-y · 2012 · External reference
10.1038/nchembio.777
10.1038/nchembio.777 · External 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 · 2004 · External reference
10.1371/journal.pcbi.1000002
10.1371/journal.pcbi.1000002 · External reference
Correlated Mutations: A Hallmark of Phenotypic Amino Acid Substitutions
10.1371/journal.pcbi.1000923 · 2010 · External reference
Hydroxynitrile Lyases: Insights into Biochemistry, Discovery and Engineering
10.1021/cs200325q · 2011 · External reference