Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus (Q45216896)

10 December 2017

Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus (English)

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10 December 2017

Onchocerca volvulus

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3

Christian Betzel

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10 December 2017

Markus Perbandt

1

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10 December 2017

Jana Höppner

series ordinal

2

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10 December 2017

Rolf D Walter

series ordinal

4

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10 December 2017

Eva Liebau

series ordinal

5

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10 December 2017

language of work or name

English

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publication date

7 January 2005

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Journal of Biological Chemistry

10 December 2017

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10 December 2017

280

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10 December 2017

13

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10 December 2017

12630-12636

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Mass drug treatment for lymphatic filariasis and onchocerciasis

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Glutathione S-transferase polymorphisms and their biological consequences

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Differential roles of tau class glutathione S-transferases in oxidative stress

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Glutathione S-transferase Pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site

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The role of glutathione-S-transferase in anti-cancer drug resistance

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Structural analysis and antibody response to the extracellular glutathione S-transferases from Onchocerca volvulus

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A dominant role for extracellular glutathione S-transferase from Onchocerca volvulus is the production of prostaglandin D2.

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Biochemical analysis, gene structure and localization of the 24 kDa glutathione S-transferase from Onchocerca volvulus

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Onchocerca volvulus: ultrastructural localization of two glutathione S-transferases

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Crystallization of the major cytosolic glutathione S-transferase from Onchocerca volvulus

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Processing of X-ray diffraction data collected in oscillation mode

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Solvent content of protein crystals

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AMoRe: an automated package for molecular replacement

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Efficient anisotropic refinement of macromolecular structures using FFT

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Assessment of phase accuracy by cross validation: the free R value. Methods and applications

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Automated protein model building combined with iterative structure refinement

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Structure, catalytic mechanism, and evolution of the glutathione transferases

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Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme

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Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST.

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Classical electrostatics in biology and chemistry

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21 January 2018

Identifiers

DOI

10.1074/JBC.M413551200

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10 December 2017

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