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MGAT5B
Introduction
Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B is an enzyme that in humans is encoded by the MGAT5B gene.[1][2][3]
References
References
- ↑ Inamori K, Endo T, Gu J, Matsuo I, Ito Y, Fujii S, Iwasaki H, Narimatsu H, Miyoshi E, Honke K, Taniguchi N (Jan 2004). “N-Acetylglucosaminyltransferase IX acts on the GlcNAc beta 1,2-Man alpha 1-Ser/Thr moiety, forming a 2,6-branched structure in brain O-mannosyl glycan”. J Biol Chem. 279 (4): 2337–2340. doi:10.1074/jbc.C300480200. PMID 14617637.
- ↑ Kaneko M, Alvarez-Manilla G, Kamar M, Lee I, Lee JK, Troupe K, Zhang W, Osawa M, Pierce M (Nov 2003). “A novel beta(1,6)-N-acetylglucosaminyltransferase V (GnT-VB)(1)”. FEBS Lett. 554 (3): 515–519. doi:10.1016/S0014-5793(03)01234-1. PMID 14623122.
- ↑ “Entrez Gene: MGAT5B mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase, isozyme B”.
Further reading
Further reading
- Land A, Braakman I (2001). “Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum”. Biochimie. 83 (8): 783–790. doi:10.1016/S0300-9084(01)01314-1. PMID 11530211.
- Abbott KL, Troupe K, Lee I, Pierce M (2006). “Integrin-dependent neuroblastoma cell adhesion and migration on laminin is regulated by expression levels of two enzymes in the O-mannosyl-linked glycosylation pathway, PomGnT1 and GnT-Vb”. Exp. Cell Res. 312 (15): 2837–2850. doi:10.1016/j.yexcr.2006.05.022. PMID 16857188.
- Lee I, Guo HB, Kamar M, et al. (2006). “N-acetylglucosaminyltranferase VB expression enhances beta1 integrin- dependent PC12 neurite outgrowth on laminin and collagen”. J. Neurochem. 97 (4): 947–956. doi:10.1111/j.1471-4159.2006.03785.x. PMID 16606368.
- Inamori K, Mita S, Gu J, et al. (2006). “Demonstration of the expression and the enzymatic activity of N-acetylglucosaminyltransferase IX in the mouse brain”. Biochim. Biophys. Acta. 1760 (4): 678–684. doi:10.1016/j.bbagen.2005.11.019. PMID 16413118.
- Guo HB, Lee I, Kamar M, Pierce M (2004). “N-acetylglucosaminyltransferase V expression levels regulate cadherin-associated homotypic cell-cell adhesion and intracellular signaling pathways”. J. Biol. Chem. 278 (52): 52412–52424. doi:10.1074/jbc.M308837200. PMID 14561752.
- Inamori K, Endo T, Ide Y, et al. (2003). “Molecular cloning and characterization of human GnT-IX, a novel beta1,6-N-acetylglucosaminyltransferase that is specifically expressed in the brain”. J. Biol. Chem. 278 (44): 43102–43109. doi:10.1074/jbc.M308255200. PMID 12941944.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Papandreou MJ, Fenouillet E (1997). “Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation”. FEBS Lett. 406 (1–2): 191–195. doi:10.1016/S0014-5793(97)00273-1. PMID 9109416.
- Bolmstedt A, Sjölander S, Hansen JE, et al. (1996). “Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response”. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12 (3): 213–20. doi:10.1097/00042560-199607000-00001. PMID 8673525.
- Fenouillet E, Jones I, Powell B, et al. (1993). “Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain”. J. Virol. 67 (1): 150–60. PMC 237347. PMID 8093218.
- Montefiori DC, Robinson WE, Mitchell WM (1988). “Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1”. Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9248–9252. doi:10.1073/pnas.85.23.9248. PMC 282716. PMID 3264072.
- Blough HA, Pauwels R, De Clercq E, et al. (1987). “Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins”. Biochem. Biophys. Res. Commun. 141 (1): 33–38. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.
- Robinson WE, Montefiori DC, Mitchell WM (1988). “Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis”. AIDS Res. Hum. Retroviruses. 3 (3): 265–282. doi:10.1089/aid.1987.3.265. PMID 2829950.
- Kozarsky K, Penman M, Basiripour L, et al. (1989). “Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein”. J. Acquir. Immune Defic. Syndr. 2 (2): 163–9. PMID 2649653.
- Pal R, Hoke GM, Sarngadharan MG (1989). “Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1”. Proc. Natl. Acad. Sci. U.S.A. 86 (9): 3384–3388. doi:10.1073/pnas.86.9.3384. PMC 287137. PMID 2541446.
- Kalyanaraman VS, Rodriguez V, Veronese F, et al. (1990). “Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1”. AIDS Res. Hum. Retroviruses. 6 (3): 371–380. doi:10.1089/aid.1990.6.371. PMID 2187500.
- Dedera DA, Gu RL, Ratner L (1992). “Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function”. Virology. 187 (1): 377–382. doi:10.1016/0042-6822(92)90331-I. PMID 1736542.