Bulk Flow Revisited: Transport of a Soluble Protein in the Secretory Pathway

The C-terminal domain, Cp, of the Semliki Forest virus capsid protein, known for its rapid, efficient and chaperone-independent folding, was used to measure bulk fluid flow in the secretory pathway of Chinese hamster ovary cells. Being small, nonglycosylated, soluble and cytoplasmic in origin, Cp wa...

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Veröffentlicht in:	Traffic (Copenhagen, Denmark) Denmark), 2009-12, Vol.10 (12), p.1819-1830
Hauptverfasser:	Thor, Friederike, Gautschi, Matthias, Geiger, Roger, Helenius, Ari
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Capsid CHO Cells Cricetinae Cricetulus endoplasmic reticulum Models, Molecular Molecular Sequence Data Protein Folding Protein Transport quality control secretion Semliki Forest virus Semliki forest virus - metabolism Semliki Forest virus capsid protease soluble proteins Viral Proteins - chemistry Viral Proteins - metabolism
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