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Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue
The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox propertie...
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| Autori principali: | , , , , , , , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Biochemistry and Molecular Biology
2009
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2665069/ https://ncbi.nlm.nih.gov/pubmed/19181668 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M809509200 |
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