SEC53/YFL045C Literature Guide Help

Other names published for SEC53: ALG4, phosphomannomutase SEC53, YFL045C

SEC53 - Primary Literature (12)

ReferenceOther Genes Addressed
Lee KS, et al.  (2011) Improved galactose fermentation of Saccharomyces cerevisiae through inverse metabolic engineering. Biotechnol Bioeng 108(3):621-31
Mitra S, et al.  (2010) A deeply divergent phosphoglucomutase (PGM) of Giardia lamblia has both PGM and phosphomannomutase activities. Glycobiology 20(10):1233-40
Qian W, et al.  (2007) Molecular and functional analysis of phosphomannomutase (PMM) from higher plants and genetic evidence for the involvement of PMM in ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana. Plant J 49(3):399-413
Hogan GJ, et al.  (2006) Cell cycle-specified fluctuation of nucleosome occupancy at gene promoters. PLoS Genet 2(9):e158
Duttagupta R, et al.  (2005) Global analysis of Pub1p targets reveals a coordinate control of gene expression through modulation of binding and stability. Mol Cell Biol 25(13):5499-513
Dean N  (1995) Yeast glycosylation mutants are sensitive to aminoglycosides. Proc Natl Acad Sci U S A 92(5):1287-91
Kepes F and Schekman R  (1988) The yeast SEC53 gene encodes phosphomannomutase. J Biol Chem 263(19):9155-61
Feldman RI, et al.  (1987) Product of SEC53 is required for folding and glycosylation of secretory proteins in the lumen of the yeast endoplasmic reticulum. J Biol Chem 262(19):9332-9
Ruohola H and Ferro-Novick S  (1987) Sec53, a protein required for an early step in secretory protein processing and transport in yeast, interacts with the cytoplasmic surface of the endoplasmic reticulum. Proc Natl Acad Sci U S A 84(23):8468-72
Bernstein M, et al.  (1985) Characterization of a gene product (Sec53p) required for protein assembly in the yeast endoplasmic reticulum. J Cell Biol 101(6):2374-82
Ferro-Novick S, et al.  (1984) Genes required for completion of import of proteins into the endoplasmic reticulum in yeast. J Cell Biol 98(1):44-53
Huffaker TC and Robbins PW  (1983) Yeast mutants deficient in protein glycosylation. Proc Natl Acad Sci U S A 80(24):7466-70