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Prodomain–growth factor swapping in the structure of pro-TGF-β1
TGF-β is synthesized as a proprotein that dimerizes in the endoplasmic reticulum. After processing in the Golgi to cleave the N-terminal prodomain from the C-terminal growth factor (GF) domain in each monomer, pro-TGF-β is secreted and stored in latent complexes. It is unclear which prodomain and GF...
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| Опубликовано в: : | J Biol Chem |
|---|---|
| Главные авторы: | , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Biochemistry and Molecular Biology
2018
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5798290/ https://ncbi.nlm.nih.gov/pubmed/29109152 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M117.809657 |
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