Automated Author ProfileMorel-Rouhier, Melanie
Morel-Rouhier, Melanie
Current S-Index
Sum of Dataset Indices for all datasets
Average Dataset Index per Dataset
Average Dataset Index per dataset
Total Datasets
Total datasets for this author
Average FAIR Score
Average FAIR Score per dataset
Total Citations
Total citations to the author's datasets
Total Mentions
Total mentions of the author's datasets
S-Index Interpretation
The S-Index (Sharing Index) is a comprehensive metric that represents the cumulative impact of all your datasets. It is calculated as the sum of Dataset Index scores across all your claimed datasets.
What it means:
- A higher S-index indicates greater overall impact of your datasets relative to typical datasets in their fields of research
- The S-Index grows as you add more datasets or as existing datasets gain more citations and mentions
- It provides a single number to track your research data impact over time
Current S-Index: 1.5 (sum of 3 datasets Dataset Index scores)
More information here.
S-Index Over Time
Cumulative Citations Over Time
Cumulative Mentions Over Time
Datasets
Glutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quinones, Omega GSTs are specialized in the reduction of glutathionyl-acetophenones. Here we present the study of TvGSTX1 and TvGSTX3 isoforms from the wood-degrading fungus Trametes versicolor. TvGSTX1 reduces GS-menadione as expected while TvGSTX3 reduces both Xi and Omega substrates. A structural analysis indicates a broader active site for TvGSTX3 due to specific differences in the nature of the residues situated in the C-terminal helix α9. This feature could explain the catalytic duality of TvGSTX3. Based on phylogenetic analysis we propose that this duality might exist in other fungi.
Authors
- Schwartz, Mathieu ;
- Perrot, Thomas ;
- Deroy, Aurélie ;
- Roret, Thomas ;
- Morel-Rouhier, Melanie ;
- Mulliert, Guillermo ;
- Gelhaye, Eric ;
- Favier, Frédérique ;
- Didierjean, Claude
Glutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quinones, Omega GSTs are specialized in the reduction of glutathionyl-acetophenones. Here we present the study of TvGSTX1 and TvGSTX3 isoforms from the wood-degrading fungus Trametes versicolor. TvGSTX1 reduces GS-menadione as expected while TvGSTX3 reduces both Xi and Omega substrates. A structural analysis indicates a broader active site for TvGSTX3 due to specific differences in the nature of the residues situated in the C-terminal helix α9. This feature could explain the catalytic duality of TvGSTX3. Based on phylogenetic analysis we propose that this duality might exist in other fungi.
Authors
- Schwartz, Mathieu ;
- Perrot, Thomas ;
- Deroy, Aurélie ;
- Roret, Thomas ;
- Morel-Rouhier, Melanie ;
- Mulliert, Guillermo ;
- Gelhaye, Eric ;
- Favier, Frédérique ;
- Didierjean, Claude