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词条 HS3ST2
释义

  1. References

  2. Further reading

{{Infobox_gene}}Heparan sulfate glucosamine 3-O-sulfotransferase 2 is an enzyme that in humans is encoded by the HS3ST2 gene.[1][2]{{PBB_Summary
| section_title =
| summary_text = Heparan sulfate biosynthetic enzymes are key components in generating a myriad of distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It is a type II integral membrane protein and possesses heparan sulfate glucosaminyl 3-O-sulfotransferase activity. This gene is expressed predominantly in brain and may play a role in the nervous system.[3]
}}

References

1. ^{{cite journal |vauthors=Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD | title = Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci | journal = J Biol Chem | volume = 274 | issue = 8 | pages = 5170–84 |date=Mar 1999 | pmid = 9988767 | pmc = | doi =10.1074/jbc.274.8.5170 }}
2. ^{{cite web | title = Entrez Gene: HS3ST2 heparan sulfate (glucosamine) 3-O-sulfotransferase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9956| accessdate = }}
3. ^{{cite web | title = Entrez Gene: HS3ST2 heparan sulfate (glucosamine) 3-O-sulfotransferase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9956| accessdate = }}

Further reading

{{refbegin | 2}}
  • {{cite journal |vauthors=Lawrence R, Yabe T, Hajmohammadi S, etal |title=The principal neuronal gD-type 3-O-sulfotransferases and their products in central and peripheral nervous system tissues. |journal=Matrix Biol. |volume=26 |issue= 6 |pages= 442–55 |year= 2007 |pmid= 17482450 |doi= 10.1016/j.matbio.2007.03.002 | pmc=1993827 }}
  • {{cite journal |vauthors=O'Donnell CD, Tiwari V, Oh MJ, Shukla D |title=A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread. |journal=Virology |volume=346 |issue= 2 |pages= 452–9 |year= 2006 |pmid= 16336986 |doi= 10.1016/j.virol.2005.11.003 }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{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=Miyamoto K, Asada K, Fukutomi T, etal |title=Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers. |journal=Oncogene |volume=22 |issue= 2 |pages= 274–80 |year= 2003 |pmid= 12527896 |doi= 10.1038/sj.onc.1206146 }}
  • {{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=Liu J, Shworak NW, Sinaÿ P, etal |title=Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. |journal=J. Biol. Chem. |volume=274 |issue= 8 |pages= 5185–92 |year= 1999 |pmid= 9988768 |doi=10.1074/jbc.274.8.5185 }}
  • {{cite journal |vauthors=Razi N, Lindahl U |title=Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides. |journal=J. Biol. Chem. |volume=270 |issue= 19 |pages= 11267–75 |year= 1995 |pmid= 7744762 |doi=10.1074/jbc.270.19.11267 }}
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