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Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms
Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating function has been suggested for dynamins. Here we report the 2.3 Å crystal structure of the nucleoti...
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| Main Authors: | , , , , |
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| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
Oxford University Press
2001
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| Ábhair: | |
| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC125706/ https://ncbi.nlm.nih.gov/pubmed/11689422 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/20.21.5813 |
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