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Structure of human thioredoxin exhibits a large conformational change
Thioredoxin is an oxidoreductase, which is ubiquitously present across phyla from humans to plants and bacteria. Thioredoxin reduces a variety of substrates through active site Cys 32, which is subsequently oxidized to form the intramolecular disulphide with Cys 35. The thioredoxin fold is known to...
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| Hlavní autoři: | , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Wiley Subscription Services, Inc., A Wiley Company
2010
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2975144/ https://ncbi.nlm.nih.gov/pubmed/20661909 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.466 |
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