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Calreticulin Is a Thermostable Protein with Distinct Structural Responses to Different Divalent Cation Environments
Calreticulin is a soluble calcium-binding chaperone of the endoplasmic reticulum (ER) that is also detected on the cell surface and in the cytosol. Calreticulin contains a single high affinity calcium-binding site within a globular domain and multiple low affinity sites within a C-terminal acidic re...
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| Главные авторы: | , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Biochemistry and Molecular Biology
2011
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3058961/ https://ncbi.nlm.nih.gov/pubmed/21177861 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.169193 |
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