Multiple catalytically active thioredoxin folds: a winning strategy for many functions
By E. Pedone, D. Limauro, Katia D'Ambrosio, G. Simone, S. Bartolucci. 2010
40 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cell Biology
In Molecular Biology
- Lucy J. Colwell
- Sergey Ovchinnikov
- Dorothee Kern
- Hannah K. Wayment-Steele
- Anne-Florence Bitbol
- Jinbo Xu
- David Baker
- David T. Jones
Citations in the corpus
- Predicting multiple conformations via sequence clustering and AlphaFold2 (2023, neutral): “The thioredoxin superfamily containing Mpt53 is a ubiquitous set of enzymes known for their promiscuous catalytic activity, being able to reduce, oxidize and isomerize disulfide bonds 53 .”
- Prediction of multiple conformational states by combining sequence clustering with AlphaFold2 (2022, background): “The thioredoxin superfamily containing DsbE is a ubiquitous set of enzymes known for their promiscuous catalytic activity, being able to reduce, oxidize, and isomerize disulfide bonds 50 .”