(Q27640350)

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Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products

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17 December 2019

Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products (English)

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17 December 2019

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17 December 2019

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Paul A Tucker

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17 December 2019

Arie Schouten

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17 December 2019

Kevin Leonard

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17 December 2019

Belinda Bullard

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17 December 2019

Piet Gros

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17 December 2019

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1 February 2003

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17 December 2019

Journal of Molecular Biology

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17 December 2019

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17 December 2019

151-165

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17 December 2019

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17 December 2019

The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance

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Single amino acid changes outside the active site significantly affect activity of glutathione S-transferases.

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Isolation of a Drosophila gene encoding glutathione S-transferase

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A glutathione S-transferase gene of the vector mosquito, Anopheles gambiae

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Interaction of troponin-H and glutathione S-transferase-2 in the indirect flight muscles of Drosophila melanogaster.

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Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products

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4-Hydroxynonenal as a second messenger of free radicals and growth modifying factor

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4-hydroxynonenal induces apoptosis via caspase-3 activation and cytochrome c release.

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Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes

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Human glutathione transferase A4-4: an alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation

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Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily

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A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications

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Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture

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Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides

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7 January 2021

Crystal structure of a theta-class glutathione transferase.

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The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B

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Colorimetric and Fluorometric Assays of Glutathione Transferase Based on 7-Chloro-4-nitrobenzo-2-oxa-1,3-diazole

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Structure, catalytic mechanism, and evolution of the glutathione transferases

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The structure of a zeta class glutathione S-transferase from Arabidopsis thaliana: characterisation of a GST with novel active-site architecture and a putative role in tyrosine catabolism

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7 January 2021

Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface

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Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods

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X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function

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Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1

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A highly acidic tyrosine 9 and a normally titrating tyrosine 212 contribute to the catalytic mechanism of human glutathione transferase A4-4.

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7 January 2021

Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products

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Identification of an N-capping box that affects the alpha 6-helix propensity in glutathione S-transferase superfamily proteins: a role for an invariant aspartic residue.

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