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Crystal structure of human thioredoxin revealing an unraveled helix and exposed S-nitrosation site
Thioredoxins reduce disulfide bonds and other thiol modifications in all cells using a CXXC motif. Human thioredoxin 1 is unusual in that it codes for an additional three cysteines in its 105 amino acid sequence, each of which have been implicated in other reductive activities. Cys 62 and Cys 69 are...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Wiley Subscription Services, Inc., A Wiley Company
2010
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2975143/ https://ncbi.nlm.nih.gov/pubmed/20662007 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.455 |
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