Mikael Widersten

Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors

Gulyás, Kinga; Zhou, Liping; Salamonsen, Daniel; Prester, Andreas et al.

Part of Communications Chemistry, 2025

• DOI for Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors
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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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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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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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Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes

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

Part of Catalysis Science & Technology, p. 4978-4987, 2023

• DOI for Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes
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Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors

Gulyás, Kinga; Zhou, Liping; Salamonsen, Daniel; Prester, Andreas et al.

Part of Communications Chemistry, 2025

• DOI for Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors
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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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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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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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Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes

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

Part of Catalysis Science & Technology, p. 4978-4987, 2023

• DOI for Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes
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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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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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Engineering aldolases for asymmetric synthesis

Widersten, Mikael

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

• DOI for Engineering aldolases for asymmetric synthesis

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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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

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

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

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

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, p. 687-692, 2004

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

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

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

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

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

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

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

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.

Towards a fusion strategy for visualizing small proteins in Cryo-EM: fructose-6-phosphate aldolase as a carrier for an 18 kDa protein

Mutisya, Jennifer; Bodiscz, Szabolc; Leufstadius, Joel; Westenhoff, Sebastian et al.