Showing results (1-10 of 43) with videos related to
Sort By:
Pageof 5
Trends in Cell Biology|April 8, 2000
Pathways for protein disulphide bond formationA R Frand, J W Cuozzo, C A KaiserMolecular Cell|November 5, 1999
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulumA R Frand, C A KaiserMolecular Biology of the Cell|September 12, 2000
Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumA R Frand, C A KaiserMolecular Cell|July 11, 1998
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulumA R Frand, C A KaiserNature Cell Biology|November 13, 1999
Competition between glutathione and protein thiols for disulphide-bond formationJ W Cuozzo, C A KaiserMolecular and Cellular Biology|November 20, 1998
A link between secretion and pre-mRNA processing defects in Saccharomyces cerevisiae and the identification of a novel splicing gene, RSE1E J Chen, A R Frand, E Chitouras, et al.Nature Cell Biology|October 5, 2001
A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formationC S Sevier, J W Cuozzo, A Vala, et al.The Journal of Biological Chemistry|May 20, 1994
Lysine is a common determinant for mannose phosphorylation of lysosomal proteinsJ W Cuozzo, G G SahagianThe Journal of Biological Chemistry|August 8, 1998
Lysine-based structure responsible for selective mannose phosphorylation of cathepsin D and cathepsin L defines a common structural motif for lysosomal enzyme targetingJ W Cuozzo, K Tao, M Cygler, et al.The Journal of Biological Chemistry|June 30, 1995
Lysine-based structure in the proregion of procathepsin L is the recognition site for mannose phosphorylationJ W Cuozzo, K Tao, Q L Wu, et al.Pageof 5