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词条 MGAT4B
释义

  1. References

  2. Further reading

{{Infobox_gene}}Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B is an enzyme that in humans is encoded by the MGAT4B gene.[1][2]{{PBB_Summary
| section_title =
| summary_text = This gene encodes a key glycosyltransferase that regulates the formation of tri- and multiantennary branching structures in the Golgi apparatus. The encoded protein, in addition to the related isoenzyme A, catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc in a beta-1,4 linkage to the Man-alpha-1,3-Man-beta-1,4-GlcNAc arm of R-Man-alpha-1,6(GlcNAc-beta-1,2-Man-alpha-1,3)Man-beta-1,4-GlcNAc-beta-1,4-GlcNAc-beta-1-Asn. Therefore the protein is essential for the production of tri- and tetra-antennary sugar chains. The encoded protein may play a role in regulating the availability of serum glycoproteins, oncogenesis, and differentiation.[3] Its affinities for donors of acceptors are lower than that of MGAT4A so it is suggested that it is not the main contributor in N-glycan biosynthesis.[4]
}}

References

1. ^{{cite journal |vauthors=Yoshida A, Minowa MT, Takamatsu S, Hara T, Ikenaga H, Takeuchi M | title = A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment | journal = Glycoconj J | volume = 15 | issue = 12 | pages = 1115–23 |date=Jul 1999 | pmid = 10372966 | pmc = | doi =10.1023/A:1006951519522 }}
2. ^{{cite web | title = Entrez Gene: MGAT4B mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme B| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11282| accessdate = }}
3. ^{{cite web | title = Entrez Gene: MGAT4B mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme B| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11282| accessdate = }}
4. ^{{UniProt|Q9UQ53|name="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B"}}

Further reading

{{refbegin | 2}}
  • {{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=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=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=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
  • {{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=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 }}
  • {{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
  • {{cite journal |vauthors=Clark HF, Gurney AL, Abaya E, etal |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 | pmc=403697 }}
  • {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
  • {{cite journal |vauthors=Brandenberger R, Wei H, Zhang S, etal |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
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