| 释义 |
- References
- Further reading
- External links
{{Infobox_gene}}Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the MGAT2 gene.[1][2]{{PBB_Summary
| section_title =
| summary_text = The product of this gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in this gene may lead to carbohydrate-deficient glycoprotein syndrome, type II. The coding region of this gene is intronless. Transcript variants with a spliced 5' UTR may exist, but their biological validity has not been determined.[3]
}}References1. ^{{cite journal |vauthors=Tan J, D'Agostaro AF, Bendiak B, Reck F, Sarkar M, Squire JA, Leong P, Schachter H | title = The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein | journal = Eur J Biochem | volume = 231 | issue = 2 | pages = 317–28 |date=Sep 1995 | pmid = 7635144 | pmc = | doi =10.1111/j.1432-1033.1995.tb20703.x }}
2. ^{{cite web | title = Entrez Gene: MGAT2 mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4247| accessdate = }}
3. ^{{cite web | title = Entrez Gene: MGAT2 mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4247| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal |vauthors=Cormier-Daire V, Amiel J, Vuillaumier-Barrot S, etal |title=Congenital disorders of glycosylation IIa cause growth retardation, mental retardation, and facial dysmorphism |journal=J. Med. Genet. |volume=37 |issue= 11 |pages= 875–7 |year= 2000 |pmid= 11228641 |doi=10.1136/jmg.37.11.875 | pmc=1734478 }}
- {{cite journal |vauthors=Land A, Braakman I |title=Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum |journal=Biochimie |volume=83 |issue= 8 |pages= 783–90 |year= 2001 |pmid= 11530211 |doi=10.1016/S0300-9084(01)01314-1 }}
- {{cite journal |vauthors=Dedera DA, Gu RL, Ratner L |title=Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function |journal=Virology |volume=187 |issue= 1 |pages= 377–82 |year= 1992 |pmid= 1736542 |doi=10.1016/0042-6822(92)90331-I }}
- {{cite journal |vauthors=Kalyanaraman VS, Rodriguez V, Veronese F, etal |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1 |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371–80 |year= 1990 |pmid= 2187500 |doi=10.1089/aid.1990.6.371 }}
- {{cite journal |vauthors=Shimizu H, Tsuchie H, Honma H, etal |title=Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins |journal=Jpn. J. Med. Sci. Biol. |volume=43 |issue= 3 |pages= 75–87 |year= 1991 |pmid= 2283726 |doi= 10.7883/yoken1952.43.75}}
- {{cite journal |vauthors=Leonard CK, Spellman MW, Riddle L, etal |title=Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10373–82 |year= 1990 |pmid= 2355006 |doi= }}
- {{cite journal |vauthors=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384–8 |year= 1989 |pmid= 2541446 |doi=10.1073/pnas.86.9.3384 | pmc=287137 }}
- {{cite journal |vauthors=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452–6 |year= 1989 |pmid= 2542563 |doi= | pmc=250699 }}
- {{cite journal |vauthors=Kozarsky K, Penman M, Basiripour L, etal |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163–9 |year= 1989 |pmid= 2649653 |doi= }}
- {{cite journal |vauthors=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265–82 |year= 1988 |pmid= 2829950 |doi=10.1089/aid.1987.3.265 }}
- {{cite journal |vauthors=Blough HA, Pauwels R, De Clercq E, etal |title=Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins |journal=Biochem. Biophys. Res. Commun. |volume=141 |issue= 1 |pages= 33–8 |year= 1987 |pmid= 3099781 |doi=10.1016/S0006-291X(86)80330-8 }}
- {{cite journal |vauthors=Montefiori DC, Robinson WE, Mitchell WM |title=Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 9248–52 |year= 1988 |pmid= 3264072 |doi=10.1073/pnas.85.23.9248 | pmc=282716 }}
- {{cite journal |vauthors=D'Agostaro GA, Zingoni A, Moritz RL, etal |title=Molecular cloning and expression of cDNA encoding the rat UDP-N-acetylglucosamine:alpha-6-D-mannoside beta-1,2-N-acetylglucosaminyltransferase II |journal=J. Biol. Chem. |volume=270 |issue= 25 |pages= 15211–21 |year= 1995 |pmid= 7797505 |doi=10.1074/jbc.270.25.15211 }}
- {{cite journal |vauthors=Fenouillet E, Jones I, Powell B, etal |title=Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain |journal=J. Virol. |volume=67 |issue= 1 |pages= 150–60 |year= 1993 |pmid= 8093218 |doi= | pmc=237347 }}
- {{cite journal |vauthors=Yeh JC, Seals JR, Murphy CI, etal |title=Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system |journal=Biochemistry |volume=32 |issue= 41 |pages= 11087–99 |year= 1993 |pmid= 8218172 |doi=10.1021/bi00092a019 }}
- {{cite journal |vauthors=Bolmstedt A, Sjölander S, Hansen JE, etal |title=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 |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=12 |issue= 3 |pages= 213–20 |year= 1996 |pmid= 8673525 |doi= 10.1097/00042560-199607000-00001}}
- {{cite journal |vauthors=Tan J, Dunn J, Jaeken J, Schachter H |title=Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disease with defective brain development |journal=Am. J. Hum. Genet. |volume=59 |issue= 4 |pages= 810–7 |year= 1996 |pmid= 8808595 |doi= | pmc=1914797 }}
- {{cite journal |vauthors=Hu H, Shioda T, Moriya C, etal |title=Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface |journal=J. Virol. |volume=70 |issue= 11 |pages= 7462–70 |year= 1996 |pmid= 8892864 |doi= | pmc=190813 }}
- {{cite journal |vauthors=Papandreou MJ, Fenouillet E |title=Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation |journal=FEBS Lett. |volume=406 |issue= 1–2 |pages= 191–5 |year= 1997 |pmid= 9109416 |doi=10.1016/S0014-5793(97)00273-1 }}
{{refend}}External links- [https://www.ncbi.nlm.nih.gov/books/NBK1332/ GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview]
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