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ERS1 encodes a functional homologue of the human lysosomal cystine transporter.
Gao XD, Wang J, Keppler-Ross S, Dean N. Gao XD, et al. Among authors: dean n. FEBS J. 2005 May;272(10):2497-511. doi: 10.1111/j.1742-4658.2005.04670.x. FEBS J. 2005. PMID: 15885099
Interaction between the C termini of Alg13 and Alg14 mediates formation of the active UDP-N-acetylglucosamine transferase complex.
Gao XD, Moriyama S, Miura N, Dean N, Nishimura S. Gao XD, et al. Among authors: dean n. J Biol Chem. 2008 Nov 21;283(47):32534-41. doi: 10.1074/jbc.M804060200. Epub 2008 Sep 22. J Biol Chem. 2008. PMID: 18809682 Free PMC article.
The second step of eukaryotic N-linked glycosylation in endoplasmic reticulum is catalyzed by an UDP-N-acetylglucosamine transferase that is comprised of two subunits, Alg13 and Alg14. ...In addition, deletion of the N-terminal beta-strand of Alg13 caused the …
The second step of eukaryotic N-linked glycosylation in endoplasmic reticulum is catalyzed by an UDP-N-acetylglucosamine trans …
Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation.
Gao XD, Tachikawa H, Sato T, Jigami Y, Dean N. Gao XD, et al. Among authors: dean n. J Biol Chem. 2005 Oct 28;280(43):36254-62. doi: 10.1074/jbc.M507569200. Epub 2005 Aug 12. J Biol Chem. 2005. PMID: 16100110
N-linked glycosylation requires the synthesis of an evolutionarily conserved lipid-linked oligosaccharide (LLO) precursor that is essential for glycoprotein folding and stability. ...
N-linked glycosylation requires the synthesis of an evolutionarily conserved lipid-linked oligosaccharide (LLO) precursor that is ess
Physical interactions between the Alg1, Alg2, and Alg11 mannosyltransferases of the endoplasmic reticulum.
Gao XD, Nishikawa A, Dean N. Gao XD, et al. Among authors: dean n. Glycobiology. 2004 Jun;14(6):559-70. doi: 10.1093/glycob/cwh072. Epub 2004 Mar 24. Glycobiology. 2004. PMID: 15044395
The early steps of N-linked glycosylation involve the synthesis of a lipid-linked oligosaccharide, Glc(3)Man(9)GlcNAc(2)-PP-dolichol, on the endoplasmic reticulum (ER) membrane. ...
The early steps of N-linked glycosylation involve the synthesis of a lipid-linked oligosaccharide, Glc(3)Man(9)GlcNAc(2)-PP-dolichol, …
Identification of a Candida glabrata homologue of the S. cerevisiae VRG4 gene, encoding the Golgi GDP-mannose transporter.
Nishikawa A, Mendez B, Jigami Y, Dean N. Nishikawa A, et al. Among authors: dean n. Yeast. 2002 Jun 15;19(8):691-8. doi: 10.1002/yea.854. Yeast. 2002. PMID: 12185838
Hetero-oligomeric interactions between early glycosyltransferases of the dolichol cycle.
Noffz C, Keppler-Ross S, Dean N. Noffz C, et al. Among authors: dean n. Glycobiology. 2009 May;19(5):472-8. doi: 10.1093/glycob/cwp001. Epub 2009 Jan 7. Glycobiology. 2009. PMID: 19129246 Free PMC article.
N-Linked glycosylation begins with the formation of a dolichol-linked oligosaccharide in the endoplasmic reticulum (ER). The first two steps of this pathway lead to the formation of GlcNAc(2)-PP-dolichol, whose synthesis is sequentially catalyzed by the Alg7p GlcNAc phosph
N-Linked glycosylation begins with the formation of a dolichol-linked oligosaccharide in the endoplasmic reticulum (ER). The first tw
Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation.
Averbeck N, Gao XD, Nishimura S, Dean N. Averbeck N, et al. Among authors: dean n. Mol Biol Cell. 2008 May;19(5):2169-78. doi: 10.1091/mbc.e07-10-1077. Epub 2008 Mar 12. Mol Biol Cell. 2008. PMID: 18337470 Free PMC article.
The second step of dolichol-linked oligosaccharide synthesis in the N-linked glycosylation pathway at the endoplasmic reticulum (ER) membrane is catalyzed by an unusual hetero-oligomeric UDP-N-acetylglucosamine transferase that in most eukaryotes is comprised of at …
The second step of dolichol-linked oligosaccharide synthesis in the N-linked glycosylation pathway at the endoplasmic reticulum (ER) …
Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit.
Averbeck N, Keppler-Ross S, Dean N. Averbeck N, et al. Among authors: dean n. J Biol Chem. 2007 Oct 5;282(40):29081-8. doi: 10.1074/jbc.M704410200. Epub 2007 Aug 8. J Biol Chem. 2007. PMID: 17686769
N-linked glycosylation begins in the endoplasmic reticulum with the synthesis of a highly conserved dolichol-linked oligosaccharide precursor. ...We provide evidence that Alg14 contains a C-terminal cytosolic tail and an N terminus that resides within the ER lumen.
N-linked glycosylation begins in the endoplasmic reticulum with the synthesis of a highly conserved dolichol-linked oligosaccharide p
The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the cytosolic side of the endoplasmic reticulum.
Cipollo JF, Trimble RB, Chi JH, Yan Q, Dean N. Cipollo JF, et al. Among authors: dean n. J Biol Chem. 2001 Jun 15;276(24):21828-40. doi: 10.1074/jbc.M010896200. Epub 2001 Feb 15. J Biol Chem. 2001. PMID: 11278778
The initial steps in N-linked glycosylation involve the synthesis of a lipid-linked core oligosaccharide followed by the transfer of the core glycan to nascent polypeptides in the endoplasmic reticulum (ER). ...
The initial steps in N-linked glycosylation involve the synthesis of a lipid-linked core oligosaccharide followed by the transfer of …
Distinct protein domains of the yeast Golgi GDP-mannose transporter mediate oligomer assembly and export from the endoplasmic reticulum.
Gao XD, Dean N. Gao XD, et al. Among authors: dean n. J Biol Chem. 2000 Jun 9;275(23):17718-27. doi: 10.1074/jbc.M909946199. J Biol Chem. 2000. PMID: 10748175
., and Yoda, K. (1999) FEBS Lett. 458, 309-312) and are unstable, while proteins lacking the N-terminal cytosolic tail are stable and multimerize efficiently, but are mislocalized to the endoplasmic reticulum (ER). Fusion of the N terminus of Vrg4p to related ER mem …
., and Yoda, K. (1999) FEBS Lett. 458, 309-312) and are unstable, while proteins lacking the N-terminal cytosolic tail are stable and …
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