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• W2056462826 abstract "In endothelial cells, the multifunctional blood glycoprotein von Willebrand Factor (VWF) is stored for rapid exocytic release in specialized secretory granules called Weibel-Palade bodies (WPBs). Electron cryomicroscopy at the thin periphery of whole, vitrified human umbilical vein endothelial cells (HUVECs) is used to directly image WPBs and their interaction with a 3D network of closely apposed membranous organelles, membrane tubules, and filaments. Fourier analysis of images and tomographic reconstruction show that VWF is packaged as a helix in WPBs. The helical signature of VWF tubules is used to identify VWF-containing organelles and characterize their paracrystalline order in low dose images. We build a 3D model of a WPB in which individual VWF helices can bend, but in which the paracrystalline packing of VWF tubules, closely wrapped by the WPB membrane, is associated with the rod-like morphology of the granules." @default.
• W2056462826 created "2016-06-24" @default.
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• W2056462826 date "2009-10-13" @default.
• W2056462826 modified "2023-09-27" @default.
• W2056462826 title "Structural organization of Weibel-Palade bodies revealed by cryo-EM of vitrified endothelial cells" @default.
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• W2056462826 doi "https://doi.org/10.1073/pnas.0902977106" @default.
• W2056462826 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2765093" @default.
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• W2056462826 hasPublicationYear "2009" @default.
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