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

By D. Sheehan, G. Meade, V. Foley, C. Dowd. Biochemical Journal, 2001

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How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Redox Regulation of Cell Survival (2008, positive): “Furthermore, enzymes such as glutathione S-transferases (GSTs) are known to have Se-independent peroxidase activity (279).”
Large-Scale Determination of Sequence, Structure, and Function Relationships in Cytosolic Glutathione Transferases across the Biosphere (2014, background): “describe several other historical cases of misannotations/ re-classifications involving plant and mouse cytGSTs [58].”
A Hybrid Micro–Macroevolutionary Approach to Gene Tree Reconstruction (2005, positive): “The second tree, provided by Dr. Hugh Nicholas (Pittsburgh Supercomputing Center) is derived from the glutathione-s transferases (Sheehan et al. , 2001), a superfamily of detoxiﬁcation enzymes.”
Plant glutathione transferases — a decade falls short (2007, background): “Differences in the carboxy-terminal domain may be responsible for differences in the substrate specificity between different GST classes (Sheehan et al. 2001).”
Plant glutathione transferases (2002, background): “In cephalopods, however, sigma GSTs are lens S-crystallins [3], giving an indication of the functional diversity of these proteins.”
The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae (2012, background): “Glutathione transferases: Glutathione transferases (GSTs) are a major family of proteins, which are involved in the detoxification of many xenobiotic compounds (Sheehan et al. 2001).”