Results 11 to 20 of about 16,152 (159)
Cell, 1991 ADP-ribosylation factor (ARF) is an abundant and highly conserved low molecular weight GTP-binding protein that was originally identified as a key element required for the action of cholera toxin in mammalian cells, but whose physiological role is unknown.
T, Serafini +5 more
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COP‐coated vesicles in intracellular protein transport
FEBS Letters, 1995 COP‐coated vesicles have originally been implicated in vesicular transport between subcompartments of the Golgi complex in mammals in a cis to trans direction. More recently, a role for COP‐coated vesicles in transport between the endoplasmic reticulum (ER) and Golgi in mammalian cells has been proposed.
C. Harter
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Architecture of coatomer: Molecular characterization of delta-COP and protein interactions within the complex [PDF]
Journal of Cell Biology, 1996 Copyright © 2011 by The Rockefeller University Press.Coatomer is a cytosolic protein complex that forms the coat of COP I-coated transport vesicles.
Auerbach, S +9 more
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Structural basis for the binding of tryptophan-based motifs by δ-COP. [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2015 Coatomer consists of two subcomplexes: the membrane-targeting, ADP ribosylation factor 1 (Arf1):GTP-binding βγδζ-COP F-subcomplex, which is related to the adaptor protein (AP) clathrin adaptors, and the cargo-binding αβ'ε-COP B-subcomplex. We present the
Duden, Rainer +7 more
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GOLPH3-mTOR Crosstalk and Glycosylation: A Molecular Driver of Cancer Progression
CellsOriginally identified in proteomic-based studies of the Golgi, Golgi phosphoprotein 3 (GOLPH3) is a highly conserved protein from yeast to humans. GOLPH3 localizes to the Golgi through the interaction with phosphatidylinositol-4-phosphate and is required
Anna Frappaolo +2 more
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The presence of β'1-COP and β'2-COP is required for female and male gametophyte development. [PDF]
Plant Reprod, 2023 Coat protein I (COPI) and Coat protein II (COPII) coated vesicles mediate protein transport in the early secretory pathway. Although several components of COPII vesicles have been shown to have an essential role in Arabidopsis gametogenesis, the function
Sánchez-Simarro J +2 more
europepmc +2 more sources
Modulation of host cell pathways by <i>Coxiella burnetii</i> Dot/Icm effectors. [PDF]
mLifeAbstract Coxiella burnetii, the etiological agent of Q fever, is a significant intracellular bacterial pathogen. C. burnetii is a highly infectious pathogen that primarily targets pulmonary alveolar macrophages during natural infection. It can then disseminate to macrophages in other tissues and organs, leading to chronic infections. C.
Yuan J, Zhang Y, Song L, Luo ZQ.
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The structure of the COPI coat determined within the cell
eLife, 2017 COPI-coated vesicles mediate trafficking within the Golgi apparatus and from the Golgi to the endoplasmic reticulum. The structures of membrane protein coats, including COPI, have been extensively studied with in vitro reconstitution systems using ...
Yury S Bykov +7 more
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Retrograde transport pathways utilised by viruses and protein toxins [PDF]
, 2006 A model has been presented for retrograde transport of certain toxins and viruses from the cell surface to the ER that suggests an obligatory interaction with a glycolipid receptor at the cell surface. Here we review studies on the ER trafficking cholera
Easton, A. J. (Andrew J.) +4 more
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Silkworm coatomers and their role in tube expansion of posterior silkgland.
PLoS ONE, 2010 BackgroundCoat protein complex I (COPI) vesicles, coated by seven coatomer subunits, are mainly responsible for Golgi-to-ER transport. Silkworm posterior silkgland (PSG), a highly differentiated secretory tissue, secretes fibroin for silk production, but
Qiao Wang +9 more
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