Cell
ArticleA new type of coated vesicular carrier that appears not to contain clathrin: Its possible role in protein transport within the Golgi stack
References (28)
- et al.
Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine
Cell
(1984) - et al.
Sequential intermediates in the pathway of intercompartmental transport in a cell-free system
Cell
(1984) - et al.
The glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae
Cell
(1984) - et al.
Compartmental organization of the Golgi stack
Cell
(1985) - et al.
Attachment of terminal N-acetylglucosamine to asparagine-linked oligosaccharides occurs in the central cisternae of the Golgi stack
Cell
(1985) - et al.
A clathrin-coated, Golgi-related compartment of the insulin secreting cell accumulates proinsulin in the presence of monensin
Cell
(1984) - et al.
The synthesis of complex-type oligosaccharides
J. Biol. Chem.
(1978) - et al.
Specimen preparation for electron microscopy using low temperature embedding resins
J. Micros.
(1982) - et al.
The “coat” of kidney intercalated cell tubulovesicles does not contain clathrin
Am. J. Physiol.
(1986) - et al.
Early and late functions associated with the Golgi apparatus reside in distinct compartments
Progress in unraveling pathways of Golgi traffic
Ann. Rev. Cell Biol.
Transport of vesicular stomatitis virus glycoprotein in a cell-free extract
Coated pits, coated vesicles, and receptor-mediated endocytosis
Nature
Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane
J. Cell Biol.
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2017, Tissue and CellCitation Excerpt :Near the rims of the Golgi cisternae, there are many COPI-dependent vesicles with a diameter of 52 nm (Marsh et al., 2001; Mironov and Arvan, 2008; Fig. 2A: white arrows). COPI-dependent vesicles were first described by Orci et al. (1986), and these form from COPI-coated buds that are visible on the rims of the Golgi cisternae, the CMC and the ERES. The COPI coat on these buds is 10-nm thick, and it has an electron density similar to that of the external layer of the membranes (Marsh et al., 2001).
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