Multiple catalytically active thioredoxin folds: a winning strategy for many functions(710 views) Pedone E, Limauro D, D'Ambrosio K, De Simone G, Bartolucci S
Cell Mol Life Sci Cellular And Molecular Life Sciences (ISSN: 1420-682x), 2010 Nov; 67(22): 3797-3814.
Keywords: Disulfide Bond, Hybrid Peroxiredoxin, Protein Disulfide Isomerase, Protein Disulfide Oxidoreductase, Redox Sites, Trx Fold, Hybrid Protein, Protein Erp57, Thioredoxin, Unclassified Drug, Alpha Helix, Beta Sheet, Catalysis, Dimerization, Enzyme Activity, Enzyme Analysis, Enzyme Structure, Molecular Evolution, Nonhuman, Nucleotide Sequence, Oxidation Reduction State, Protein Analysis, Protein Domain, Protein Folding, Protein Function, Protein Interaction, Protein Structure, Review, Thermophilic Bacterium, Amino Acid Sequence, Animals, Archaea, Archaeal Proteins, Bacterial Proteins, Catalytic Domain, Models, Molecular Sequence Data, Protein Disulfide-Isomerases, Sequence Alignment, Eukaryota,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, Naples 80134, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università Degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, Naples 80126, Italy
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Multiple catalytically active thioredoxin folds: a winning strategy for many functions