Mikael Widersten

High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases

Blazic, Marija; Gautier, Candice; Norberg, Thomas; Widersten, Mikael

Part of Faraday discussions, p. 115-126, 2024

• DOI for High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases
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Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes

Hebert, Hans; Sönmez, Eda; Purhonen, Pasi; Widersten, Mikael

Part of Structure, p. 1322-13260000, 2024

• DOI for Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes
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Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD

Sridhar, Shruthi; Kiema, Tiila-Riikka Kiema; Schmitz, Werner; Widersten, Mikael et al.

Part of FEBS Open Bio, p. 655-674, 2024

• DOI for Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD
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Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics

Zavarise, Alberto; Sridhar, Shruthi; Kiema, Tiila-Riikka; Wierenga, Rikkert K. et al.

Part of The FEBS Journal, p. 465-481, 2023

• DOI for Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics
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Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity

Sridhar, Shruthi; Zavarise, Alberto; Kiema, Tiila-Riikka; Dalwani, Subhadra et al.

Part of IUCrJ, p. 437-447, 2023

• DOI for Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity
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High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases

Blazic, Marija; Gautier, Candice; Norberg, Thomas; Widersten, Mikael

Part of Faraday discussions, p. 115-126, 2024

• DOI for High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases
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Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes

Hebert, Hans; Sönmez, Eda; Purhonen, Pasi; Widersten, Mikael

Part of Structure, p. 1322-13260000, 2024

• DOI for Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes
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Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD

Sridhar, Shruthi; Kiema, Tiila-Riikka Kiema; Schmitz, Werner; Widersten, Mikael et al.

Part of FEBS Open Bio, p. 655-674, 2024

• DOI for Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD
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Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics

Zavarise, Alberto; Sridhar, Shruthi; Kiema, Tiila-Riikka; Wierenga, Rikkert K. et al.

Part of The FEBS Journal, p. 465-481, 2023

• DOI for Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics
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Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity

Sridhar, Shruthi; Zavarise, Alberto; Kiema, Tiila-Riikka; Dalwani, Subhadra et al.

Part of IUCrJ, p. 437-447, 2023

• DOI for Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity
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Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes

Cornelius Chukwu, Eugenia; Bartl, Michael; Persson, Louise J.; Xiong, Ruisheng et al.

Part of Catalysis Science & Technology, 2023

• DOI for Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes
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Structure and Mechanism of a Cold-Adapted Bacterial Lipase

van der Ent, Florian; Lund, Bjarte A.; Svalberg, Linn; Purg, Miha et al.

Part of Biochemistry, p. 933-942, 2022

• DOI for Structure and Mechanism of a Cold-Adapted Bacterial Lipase
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Facile Synthesis of 2-Hydroxyacetophenone from Racemic Styrene Oxide Catalyzed by Engineered Enzymes

Söderlund, Isac; Tjärnhage, Elias; Hamnevik, Emil; Widersten, Mikael

Part of Biotechnology letters, p. 985-990, 2022

• DOI for Facile Synthesis of 2-Hydroxyacetophenone from Racemic Styrene Oxide Catalyzed by Engineered Enzymes
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The Role of Substrate-Coenzyme Crosstalk in Determining Turnover Rates in Rhodococcus ruber Alcohol Dehydrogenase

Enugala, Thilak Reddy; Corbella Morató, Marina; Kamerlin, Shina C. L.; Widersten, Mikael

Part of ACS Catalysis, p. 9115-9128, 2020

• DOI for The Role of Substrate-Coenzyme Crosstalk in Determining Turnover Rates in Rhodococcus ruber Alcohol Dehydrogenase
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Engineering aldolases for asymmetric synthesis

Widersten, Mikael

Part of Methods in Enzymology, p. 149-167, 2020

• DOI for Engineering aldolases for asymmetric synthesis

Chemical and Biochemical Approaches for the Synthesis of Substituted Dihydroxybutanones and Di-, and Tri-Hydroxypentanones

Al-Smadi, Derar; Enugala, Thilak Reddy; Kessler, Vadim; Mhasal, Anil Rhanu et al.

Part of Journal of Organic Chemistry, p. 6982-6991, 2019

• DOI for Chemical and Biochemical Approaches for the Synthesis of Substituted Dihydroxybutanones and Di-, and Tri-Hydroxypentanones

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

Maurer, Dirk; Enugala, Thilak Reddy; Hamnevik, Emil; Bauer, Paul et al.

Part of ACS Catalysis, p. 7526-7538, 2018

• DOI for 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
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Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism

Maurer, Dirk; Lohkamp, Bernhard; Krumpel, Michael; Widersten, Mikael et al.

Part of Biochemical Journal, p. 2395-2416, 2018

• DOI for Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism

New Stereoselective Biocatalysts for Carboligation and Retro-Aldol Cleavage Reactions Derived from D-Fructose 6-Phosphate Aldolase

Ma, Huan; Engel, Sarah; Enugala, Thilak Reddy; Al-Smadi, Derar et al.

Part of Biochemistry, p. 5877-5885, 2018

• DOI for New Stereoselective Biocatalysts for Carboligation and Retro-Aldol Cleavage Reactions Derived from D-Fructose 6-Phosphate Aldolase

Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-Diol and Its Corresponding Acyloin

Hamnevik, Emil; Maurer, Dirk; Enugala, Thilak Reddy; Chu, Thao et al.

Part of Biochemistry, p. 1059-1062, 2018

• DOI for Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-Diol and Its Corresponding Acyloin

Epoxide Hydrolysis as a Model System for Understanding Flux Through a Branched Reaction Scheme

Janfalk Carlsson, Åsa; Bauer, Paul; Dobritzsch, Doreen; Kamerlin, Shina C Lynn et al.

Part of IUCrJ, p. 269-282, 2018

• DOI for Epoxide Hydrolysis as a Model System for Understanding Flux Through a Branched Reaction Scheme
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Synthesis of substrates for aldolase-catalyzed reactions: A comparison of methods for the synthesis of substituted phenylacetaldehydes

Al-Smadi, Derar; Enugala, Thilak Reddy; Norberg, Thomas; Kihlberg, Jan et al.

Part of Synlett, p. 1187-1190, 2018

• DOI for Synthesis of substrates for aldolase-catalyzed reactions: A comparison of methods for the synthesis of substituted phenylacetaldehydes

Relaxation of Nonproductive Binding and Increased Rate of Coenzyme Release in an Alcohol Dehydrogenase Increases Turnover With a Non-Preferred Alcohol Enantiomer

Hamnevik, Emil; Enugala, Thilak Reddy; Maurer, Dirk; Ntuku, Siphosethu et al.

Part of The FEBS Journal, p. 3895-3914, 2017

• DOI for Relaxation of Nonproductive Binding and Increased Rate of Coenzyme Release in an Alcohol Dehydrogenase Increases Turnover With a Non-Preferred Alcohol Enantiomer
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Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)

Ma, Huan; Szeler, Klaudia; Kamerlin, Shina Caroline Lynn; Widersten, Mikael

Part of Chemical Science, p. 1415-1421, 2016

• DOI for Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)
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Laboratory evolved enzymes provide snapshots of the development of enantioconvergence in enzyme-catalyzed epoxide hydrolysis

Janfalk Carlsson, Åsa; Bauer, Paul; Dobritzsch, Doreeen; Nilsson, Mikael et al.

Part of ChemBioChem, p. 1693-1697, 2016

• DOI for Laboratory evolved enzymes provide snapshots of the development of enantioconvergence in enzyme-catalyzed epoxide hydrolysis
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Conformational Diversity and Enantioconvergence in Potato Epoxide Hydrolase 1

Bauer, Paul; Janfalk Carlsson, Åsa; Amrein, Beat A.; Dobritzsch, Doreen et al.

Part of Organic and biomolecular chemistry, p. 5639-5651, 2016

• DOI for Conformational Diversity and Enantioconvergence in Potato Epoxide Hydrolase 1
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Expanding the catalytic triad in epoxide hydrolases and related enzymes

Amrein, Beat A.; Bauer, Paul; Duarte, Fernanda; Janfalk Carlsson, Åsa et al.

Part of ACS Catalysis, p. 5702-5713, 2015

• DOI for Expanding the catalytic triad in epoxide hydrolases and related enzymes
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A micro-plate format assay for real-time screening for new aldolases accepting aryl-substituted acceptor substrates

Ma, Huan; Enugala, Thilak Reddy; Widersten, Mikael

Part of ChemBioChem, p. 2595-2598, 2015

• DOI for A micro-plate format assay for real-time screening for new aldolases accepting aryl-substituted acceptor substrates

Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus

Karlsson, O. Andreas; Ramirez, Juan; Öberg, Daniel; Malmqvist, Tony et al.

Part of Scientific Reports, 2015

• DOI for Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus
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Directed evolution on FucO - structural explanations for changes in substrate scope

Dahlström, Kathe M.; Blikstad, Cecilia; Widersten, Mikael; Salminen, Tiina A.

Part of Protein Science, p. 199-200, 2015

Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A

Hamnevik, Emil; Blikstad, Cecilia; Norrehed, Sara; Widersten, Mikael

Part of Journal of Molecular Catalysis B, p. 68-78, 2014

• DOI for Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A

Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution

Blikstad, Cecilia; Dahlström, Käthe; Salminen, Tiina; Widersten, Mikael

Part of The FEBS Journal, p. 2387-2398, 2014

• DOI for Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution

Stereoselective oxidation of aryl-substituted vicinal diols into chiral α-hydroxy aldehydes by re-engineered propanediol oxidoreductase

Blikstad, Cecilia; Dahlström, Kärthe M.; Salminen, Tiina A.; Widersten, Mikael

Part of ACS Catalysis, p. 3016-3025, 2013

• DOI for Stereoselective oxidation of aryl-substituted vicinal diols into chiral α-hydroxy aldehydes by re-engineered propanediol oxidoreductase

Obtaining optical purity for product diols in enzyme-catalyzed epoxide hydrolysis: contributions from changes in both enantio- and regioselectivity

Janfalk Carlsson, Åsa; Bauer, Paul; Ma, Huan; Widersten, Mikael

Part of Biochemistry, p. 7627-7637, 2012

• DOI for Obtaining optical purity for product diols in enzyme-catalyzed epoxide hydrolysis: contributions from changes in both enantio- and regioselectivity

One-step enzyme extraction and immobilization for biocatalysis applications

Cassimjee, Karim Engelmark; Kourist, Robert; Lindberg, Diana; Wittrup Larsen, Marianne et al.

Part of Biotechnology Journal, p. 463-469, 2011

• DOI for One-step enzyme extraction and immobilization for biocatalysis applications

Mutations in salt-bridging residues at the interface of the core and lid domains of epoxide hydrolase StEH1 affect regioselectivity, protein stability and hysteresis

Lindberg, Diana; Ahmad, Shabbir; Widersten, Mikael

Part of Archives of Biochemistry and Biophysics, p. 165-173, 2010

• DOI for Mutations in salt-bridging residues at the interface of the core and lid domains of epoxide hydrolase StEH1 affect regioselectivity, protein stability and hysteresis

Modification of substrate specificity resulted in an epoxide hydrolase with shifted enantiopreference for (2,3-epoxypropyl)benzene

Gurell, Ann; Widersten, Mikael

Part of ChemBioChem, p. 1422-1429, 2010

• DOI for Modification of substrate specificity resulted in an epoxide hydrolase with shifted enantiopreference for (2,3-epoxypropyl)benzene

Deep eutectic solvents (DESs) are viable cosolvents for enzyme-catalyzed epoxide hydrolysis

Lindberg, Diana; de la Fuente Revenga, Mario; Widersten, Mikael

Part of Journal of Biotechnology, p. 169-171, 2010

• DOI for Deep eutectic solvents (DESs) are viable cosolvents for enzyme-catalyzed epoxide hydrolysis

Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis

Widersten, Mikael; Gurell, Ann; Lindberg, Diana

Part of Biochimica et Biophysica Acta, p. 316-326, 2010

• DOI for Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis

Functional characterization of a stereospecific diol dehydrogenase, FucO, from Escherichia coli: substrate specificity, pH dependence, kinetic isotope effects and influence of solvent viscosity

Blikstad, Cecilia; Widersten, Mikael

Part of Journal of Molecular Catalysis B, p. 148-155, 2010

• DOI for Functional characterization of a stereospecific diol dehydrogenase, FucO, from Escherichia coli: substrate specificity, pH dependence, kinetic isotope effects and influence of solvent viscosity

Temperature and pH dependence of enzyme catalyzed hydrolysis of trans-methylstyrene oxide: a unifying kinetic model for observed hysteresis, cooperativity and regioselectivity

Lindberg, Diana; de la Fuente Revenga, Mario; Widersten, Mikael

Part of Biochemistry, p. 2297-2304, 2010

• DOI for Temperature and pH dependence of enzyme catalyzed hydrolysis of trans-methylstyrene oxide: a unifying kinetic model for observed hysteresis, cooperativity and regioselectivity

Removal of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostability

Thomaeus, Ann; Naworyta, Agata; Mowbray, Sherry L.; Widersten, Mikael

Part of Protein Science, p. 1275-1284, 2008

• DOI for Removal of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostability
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Substrate-dependent hysteretic behavior in StEH1-catalyzed hydrolysis of styrene oxide derivatives

Lindberg, Diana; Gogoll, Adolf; Widersten, Mikael

Part of The FEBS Journal, p. 6309-6320, 2008

• DOI for Substrate-dependent hysteretic behavior in StEH1-catalyzed hydrolysis of styrene oxide derivatives

Active site of epoxide hydrolases revisited: A noncanonical residue in potato StEH1 promotes both formation and breakdown of the alkylenzyme intermediate

Thomaeus, Ann; Carlsson, Jens; Åqvist, Johan; Widersten, Mikael

Part of Biochemistry, p. 2466-2479, 2007

• DOI for Active site of epoxide hydrolases revisited: A noncanonical residue in potato StEH1 promotes both formation and breakdown of the alkylenzyme intermediate

Implications for an Ionized Alkyl-Enzyme Intermediate during StEH1-Catalyzed trans-Stilbene Oxide Hydrolysis

Elfström, Lisa; Widersten, Mikael

Part of Biochemistry, p. 205-212, 2006

• DOI for Implications for an Ionized Alkyl-Enzyme Intermediate during StEH1-Catalyzed trans-Stilbene Oxide Hydrolysis

X-ray structure of potato epoxide hydrolase sheds light on its substrate specificity

Mowbray, Sherry L.; Elfström, Lisa; Ahlgren, Kerstin; Andersson, Evalena et al.

Part of Protein Science, p. 1628-1637, 2006

• DOI for X-ray structure of potato epoxide hydrolase sheds light on its substrate specificity

Catalysis of potato epoxide hydrolase, StEH1

Elfström, Lisa; Widersten, Mikael

Part of Biochemical Journal, p. 633-640, 2005

• DOI for Catalysis of potato epoxide hydrolase, StEH1

Isolation of novel single-chain Cro proteins targeted for binding to the bcl-2 transcription initiation site by repertoire selection and subunit combinatorics

Jonas, Kristina; Van Der Vries, Erhard; Nilsson, Mikael T.I.; Widersten, Mikael

Part of Protein Engineering Design & Selection, p. 537-546, 2005

• DOI for Isolation of novel single-chain Cro proteins targeted for binding to the bcl-2 transcription initiation site by repertoire selection and subunit combinatorics

The Saccharomyces cerevisiae ORF YNR064c protein has characteristics of an 'orphaned' epoxide hydrolase

Elfström, Lisa; Widersten, Mikael

Part of Biochimica et Biophysica Acta - Proteins and Proteomics, p. 213-221, 2005

• DOI for The Saccharomyces cerevisiae ORF YNR064c protein has characteristics of an 'orphaned' epoxide hydrolase

Repertoire selection of variant single-chain Cro: towards directed DNA-binding specificity of helix-turn-helix proteins

Nilsson, Mikael T.I.; Widersten, Mikael

Part of Biochemistry, p. 12038-12047, 2004

• DOI for Repertoire selection of variant single-chain Cro: towards directed DNA-binding specificity of helix-turn-helix proteins

Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity.

Tsoi, Carrie; Widersten, Mikael; Morgenstern, Ralf; Swedmark, Stellan

Part of Biochemical Journal, 2004

• DOI for Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity.

Inhibition of glutathione S-transferases by antimalarial drugs: Possible implications for circumventing anticancer drug resistance

Mukanganyama, Stanley; Widersten, Mikael; Naik, Yogeshkumar S.; Mannervik, Bengt et al.

Part of Int J Cancer, p. 700-705, 2002

• DOI for Inhibition of glutathione S-transferases by antimalarial drugs: Possible implications for circumventing anticancer drug resistance

Yeast glyoxalase I is a monomeric enzyme with two active sites

Frickel, EM; Jemth, P; Widersten, M; Mannervik, B

Part of Journal of Biological Chemistry, p. 1845-1849, 2001

Proposed reductive metabolism of artemisinin by glutathione transferases in vitro

Mukanganyama, Stanley; Naik, Yogesh S.; Widersten, Mikael; Mannervik, Bengt et al.

Part of Free radical research, p. 427-434, 2001

Chlorine kinetic isotope effects on the haloalkane dehalogenase reaction

Lewandowicz, Andrzej; Rudzinski, Juliusz; Tronstad, Lisa; Widersten, Mikael et al.

Part of Journal of the American Chemical Society, p. 4550-4555, 2001

• DOI for Chlorine kinetic isotope effects on the haloalkane dehalogenase reaction

Functional expression and affinity selection of single-chain Cro by phage display: isolation of novel DNA-binding proteins

Nilsson, Mikael T.I.; Mossing, Michael C.; Widersten, Mikael

Part of Protein Engineering, p. 519-526, 2000

Examination of the transcription factor NtcA-binding motif by in vitro selection of DNA sequences from a random library

Jiang, FY; Wisen, S; Widersten, M; Bergman, B et al.

Part of Journal of Molecular Biology, p. 783-793, 2000

• DOI for Examination of the transcription factor NtcA-binding motif by in vitro selection of DNA sequences from a random library

An approach to optimizing the active site in a glutathione transferase by evolution in vitro

Hansson, Lars O.; Widersten, Mikael; Mannervik, Bengt

Part of Biochemical Journal, p. 93-100, 1999

Hydrophobic sequences can substitute for the wild-type N-terminal sequence of cystatin A (stefin A) in tight binding to cysteine proteinases. Selection of high-affinity N-terminal region variants by phage display

Ylinenjärvi, K.; Widersten, Mikael; Björk, Ingemar

Part of European Journal of Biochemistry, p. 682-688, 1999

Structural determinants in domain II of human glutathione transferase M2-2 govern the characteristic activities with aminochrome, 2-cyano-1,3-dimethyl-1-nitrosoguanidine, and 1,2-dichloro-4-nitrobenzene

Hansson, LO; Bolton-Grob, R; Widersten, M; Mannervik, B

Part of PROTEIN SCIENCE, p. 2742-2750, 1999

Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105

Johansson, Ann-Sofie; Stenberg, Gun; Widersten, Mikael; Mannervik, Bengt

Part of Journal of Molecular Cell Biology, p. 687-698, 1998

• DOI for Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105

Differences in the catalytic efficiencies of allelic variants of glutathione transferase P1-1 towards carcinogenic diol epoxides of polycyclic aromatic hydrocarbons

Sundberg, Kathrin; Johansson, Ann-Sofie; Stenberg, Gun; Widersten, Mikael et al.

Part of Carcinogenesis, p. 433-436, 1998

Heterologous Expression in Escherichia coli of SolubleActive-Site Random Mutants of Haloalkane Dehalogenase from Xanthobacter autotrophicus GJ10 by Coexpression of Molecular Chaperonins GroEL/ES

Widersten, Mikael

Part of Protein Expression and Purification, p. 389-395, 1998

• DOI for Heterologous Expression in Escherichia coli of SolubleActive-Site Random Mutants of Haloalkane Dehalogenase from Xanthobacter autotrophicus GJ10 by Coexpression of Molecular Chaperonins GroEL/ES

Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing S_NAr reactions

Hansson, Lars O.; Widersten, Mikael; Mannervik, Bengt

Part of Biochemistry, p. 11252-11260, 1997

Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes

Baez, Sofia; Segura-Aguilar, Juan; Widersten, Mikael; Johansson, Ann-Sofie et al.

Part of Biochemical Journal, p. 25-28, 1997

Conjugation of highly reactive aflatoxin B₁ exo-8,9-epoxide catalyzed by rat and human glutathione transferases: Estimation of kinetic parameters

Johnson, W. W.; Ueng, Y.-F.; Widersten, Mikael; Mannervik, Bengt et al.

Part of Biochemistry, p. 3056-3060, 1997

Glutathione conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferases M1-1 and P1-1

Sundberg, K.; Widersten, Mikael; Seidel, Albrecht; Mannervik, Bengt et al.

Part of Chemical Research in Toxicology, p. 1221-1227, 1997

Human class Mu glutathione transferases, in particular isoenzyme M2-2,catalyze detoxication of the dopamine metabolite aminochrome

Segura-Aguilar, Juan; Baez, Sofia; Widersten, Mikael; Welch, Christopher J et al.

Part of Journal of Biological Chemistry, p. 5727-5731, 1997

• DOI for Human class Mu glutathione transferases, in particular isoenzyme M2-2,catalyze detoxication of the dopamine metabolite aminochrome

Involvement of the carboxyl groups of glutathione in the catalytic mechanism of human glutathione transferase A1-1

Widersten, Mikael; Björnestedt, Robert; Mannervik, Bengt

Part of Biochemistry, p. 7731-7742, 1996

Optimized heterologous expression of the polymorphic human glutathione transferase M1-1 based on silent mutations in the corresponding cDNA

Widersten, Mikael; Huang, Mao; Mannervik, Bengt

Part of Protein Expression and Purification, p. 367-372, 1996

Glutathione transferases with novel active sites isolated by phage display from a library of random mutants

Widersten, Mikael; Mannervik, Bengt

Part of Journal of Molecular Biology, p. 115-122, 1995

High-level bacterial expression of human glutathione transferase P1-1 encoded by semisynthetic DNA

Kolm, Rüdiger H.; Stenberg, Gun; Widersten, Mikael; Mannervik, Bengt

Part of Protein Expression and Purification, p. 265-271, 1995

Generation of a Ni(II) binding site by introduction of a histidine cluster in the structure of human glutathione transferase A1-1

Yilmaz, Selma; Widersten, Mikael; Emahazion, Tesfai; Mannervik, Bengt

Part of Protein Engineering, p. 1163-1169, 1995

• DOI for Generation of a Ni(II) binding site by introduction of a histidine cluster in the structure of human glutathione transferase A1-1

FUNCTIONAL-SIGNIFICANCE OF ARGININE-15 IN THE ACTIVE-SITE OF HUMAN CLASS-ALPHA GLUTATHIONE TRANSFERASE A1-1

BJORNESTEDT, R; STENBERG, G; WIDERSTEN, M; BOARD, PG et al.

Part of JOURNAL OF MOLECULAR BIOLOGY, p. 765-773, 1995

Co-variation of glutathione transferase expression and cytostatic drug resistance in HeLa cells: establishment of class Mu glutathione transferase M3-3 as the dominating isoenzyme

Hao, Xiao-Yiao; Widersten, Mikael; Ridderström, Marianne; Hellman, Ulf et al.

Part of Biochemical Journal, p. 59-67, 1994

Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases

Berhane, Kiflu; Widersten, Mikael; Engström, Åke; Kozarich, John W. et al.

Part of Proceedings of the National Academy of Sciences of the United States of America, p. 1480-1484, 1994

A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes

Comstock, Kenine E.; Widersten, Mikael; Hao, Xiao-Yong; Henner, William D. et al.

Part of Archives of Biochemistry and Biophysics, p. 487-495, 1994

Contribution of amino acid residue 208 in the hydrophobic binding site to the catalytic mechanism of human glutathione transferase A 1-1

Widersten, Mikael; Björnestedt, Robert; Mannervik, Bengt

Part of Biochemistry, p. 11717-11723, 1994

Engineering of a metal coordinating site into human glutathione transferase M1-1 based on immobilized metal ion affinity chromatography of homologous rat enzymes

Chaga, Grigoriy; Widersten, Mikael; Andersson, Lennart; Porath, Jerker et al.

Part of Protein Engineering, p. 1115-1119, 1994

• DOI for Engineering of a metal coordinating site into human glutathione transferase M1-1 based on immobilized metal ion affinity chromatography of homologous rat enzymes

Contribution of five amino acid residues in the glutathione-binding site to the function of human glutathione transferase P1-1

Widersten, Mikael; Kolm, Rüdiger H.; Björnestedt, Robert; Mannervik, Bengt

Part of Biochemical Journal, 1992

A structural role of histidine 15 in juman gutathione transferase M1-1, an amino acid residue conserved in class Mu enzymes

Widersten, Mikael; Mannervik, Bengt

Part of Protein Engineering, 1992

NOMENCLATURE FOR HUMAN GLUTATHIONE TRANSFERASES

Mannervik, Bengt; Awasthi, Yogesh C.; Board, Philip G.; Hayes, John D. et al.

Part of Biochemical Journal, p. 305-306, 1992

DESIGN OF 2 CHIMERIC HUMAN RAT CLASS ALPHA-GLUTATHIONE TRANSFERASES FOR PROBING THE CONTRIBUTION OF C-TERMINAL SEGMENTS OF PROTEIN-STRUCTURE TO THE CATALYTIC PROPERTIES

Robert, Björnestedt; Widersten, Mikael; Board, Philip G.; Mannervik, Bengt

Part of Biochemical Journal, 1992

HETEROLOGOUS EXPRESSION OF THE ALLELIC VARIANT MU-CLASS GLUTATHIONE TRANSFERASES μ AND TRANSFERASES ψ

Widersten, Mikael; Pearson, William R.; Engström, Åke; Mannervik, Bengt

Part of Biochemical Journal, p. 519-524, 1991

CYSTEINE RESIDUES ARE NOT ESSENTIAL FOR THE CATALYTIC ACTIVITY OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE M1A-1A

Widersten, Mikael; Holmström, Eva; Mannervik, Bengt

Part of FEBS Letters, 1991

DIFFERENCES AMONG HUMAN TUMOR-CELL LINES IN THE EXPRESSION OF GLUTATHIONE TRANSFERASES AND OTHER GLUTATHIONE-LINKED ENZYMES

Castro, Victor; Söderström, Mats; Carlberg, Inger; Widersten, Mikael et al.

Part of Carcinogenesis, p. 1569-1576, 1990

Protein engineering for development of new hydrolytic biocatalysts

Widersten, Mikael

Part of Current opinion in chemical biology, p. 42-47, 2014

• DOI for Protein engineering for development of new hydrolytic biocatalysts
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Characterization and structure determination of human β-ureidopropionase reveal pH-dependent regulation by ligand-induced changes in oligomerization

Maurer, Dirk; Bernhard, Lohkamp; Krumpel, Michael; Widersten, Mikael et al.