Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Christine M. Bentivoglio"'
Publikováno v:
Molecular Biology of the Cell
Yeast Coy1 and its human homologue CASP belong to the golgin family of extended coiled-coil proteins that underlie the structure and function of the Golgi complex. Here Coy1 is shown to operate in intra-Golgi retrograde transport through direct inter
Autor:
Christine M. Bentivoglio, Aaron D. Gitler, Charles Barlowe, Neil G. Margulis, Joshua D. Wilson, Nripesh Dhungel
Publikováno v:
Traffic. 17:191-210
Coat protein complex II (COPII) vesicle formation at the endoplasmic reticulum (ER) transports nascent secretory proteins forward to the Golgi complex. To further define the machinery that packages secretory cargo and targets vesicles to Golgi membra
Autor:
Neil G, Margulis, Joshua D, Wilson, Christine M, Bentivoglio, Nripesh, Dhungel, Aaron D, Gitler, Charles, Barlowe
Publikováno v:
Traffic (Copenhagen, Denmark). 17(3)
Coat protein complex II (COPII) vesicle formation at the endoplasmic reticulum (ER) transports nascent secretory proteins forward to the Golgi complex. To further define the machinery that packages secretory cargo and targets vesicles to Golgi membra
Publikováno v:
Molecular Biology of the Cell. 17:4780-4789
Secretory proteins are exported from the endoplasmic reticulum (ER) in transport vesicles formed by the coat protein complex II (COPII). We detected Erv26p as an integral membrane protein that was efficiently packaged into COPII vesicles and cycled b
Publikováno v:
Traffic. 7:1213-1223
The endoplasmic reticulum (ER) serves a critical role in the biogenesis of secretory proteins. Folding of nascent polypeptides occurs in the ER before anterograde transport through the secretory pathway, whereas terminally misfolded secretory protein