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Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane

Munc18-1 plays pleiotropic roles in neurosecretion by acting as 1) a molecular chaperone of syntaxin-1, 2) a mediator of dense-core vesicle docking, and 3) a priming factor for soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion. However, how these function...

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Hlavní autoři: Han, Gayoung A., Malintan, Nancy T., Saw, Ner Mu Nar, Li, Lijun, Han, Liping, Meunier, Frederic A., Collins, Brett M., Sugita, Shuzo
Médium: Artigo
Jazyk:Inglês
Vydáno: The American Society for Cell Biology 2011
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3204074/
https://ncbi.nlm.nih.gov/pubmed/21900502
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1091/mbc.E11-02-0135
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