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Fluorotryptophan incorporation modulates the structure and stability of transthyretin in a site-specific manner
Abnormal deposition of aggregated wild-type (WT) human transthyretin (TTR) and its pathogenic variants is responsible for cardiomyopathy and neuropathy related to TTR amyloidosis. The tryptophan (Trp) fluorescence measurements typically used to study structural changes of TTR do not yield site-speci...
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| Publicat a: | Biochemistry |
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| Autors principals: | , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
2017
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5645263/ https://ncbi.nlm.nih.gov/pubmed/28920433 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.7b00815 |
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