ST8SIA4: Difference between revisions

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{{Infobox_gene}}
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'''CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase''' is an [[enzyme]] that in humans is encoded by the ''ST8SIA4'' [[gene]].<ref name="pmid7624364">{{cite journal |vauthors=Nakayama J, Fukuda MN, Fredette B, Ranscht B, Fukuda M | title = Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain | journal = Proc Natl Acad Sci U S A | volume = 92 | issue = 15 | pages = 7031–5 |date=Aug 1995 | pmid = 7624364 | pmc = 41465 | doi =10.1073/pnas.92.15.7031 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ST8SIA4 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7903| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4
| HGNCid = 10871
| Symbol = ST8SIA4
| AltSymbols =; PST; MGC34450; MGC61459; PST1; SIAT8D; ST8SIA-IV
| OMIM = 602547
| ECnumber = 
| Homologene = 4147
| MGIid = 106018
| GeneAtlas_image1 = PBB_GE_ST8SIA4_206925_at_tn.png
| Function = {{GNF_GO|id=GO:0003828 |text = alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity}} {{GNF_GO|id=GO:0008373 |text = sialyltransferase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030173 |text = integral to Golgi membrane}}
  | Process = {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}} {{GNF_GO|id=GO:0006491 |text = N-glycan processing}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0009311 |text = oligosaccharide metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7903
    | Hs_Ensembl = ENSG00000113532
    | Hs_RefseqProtein = NP_005659
    | Hs_RefseqmRNA = NM_005668
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 100170803
    | Hs_GenLoc_end = 100266886
    | Hs_Uniprot = Q92187
    | Mm_EntrezGene = 20452
    | Mm_Ensembl = ENSMUSG00000040710
    | Mm_RefseqmRNA = NM_009183
    | Mm_RefseqProtein = NP_033209
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 97418090
    | Mm_GenLoc_end = 97497995
    | Mm_Uniprot = Q53WR7
  }}
}}
'''ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4''', also known as '''ST8SIA4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ST8SIA4 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7903| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member of glycosyltransferase family 29, is a type II membrane protein that may be present in the Golgi apparatus. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ST8SIA4 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7903| accessdate = }}</ref>
| summary_text = The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of [[polysialic acid]], a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member of [[glycosyltransferase]] family 29, is a type II membrane protein that may be present in the Golgi apparatus. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Cohn JA, Noone PG, Jowell PS |title=Idiopathic pancreatitis related to CFTR: complex inheritance and identification of a modifier gene. |journal=J. Investig. Med. |volume=50 |issue= 5 |pages= 247S-255S |year= 2002 |pmid= 12227654 |doi=  }}
*{{cite journal  |vauthors=Cohn JA, Noone PG, Jowell PS |title=Idiopathic pancreatitis related to CFTR: complex inheritance and identification of a modifier gene |journal=J. Investig. Med. |volume=50 |issue= 5 |pages= 247S–255S |year= 2002 |pmid= 12227654 |doi=  }}
*{{cite journal  | author=Nakayama J, Fukuda MN, Fredette B, ''et al.'' |title=Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 15 |pages= 7031-5 |year= 1995 |pmid= 7624364 |doi=  }}
*{{cite journal  | author=Eckhardt M |title=Molecular characterization of eukaryotic polysialyltransferase-1 |journal=Nature |volume=373 |issue= 6516 |pages= 715–8 |year= 1995 |pmid= 7854457 |doi= 10.1038/373715a0 |name-list-format=vanc| author2=Mühlenhoff M | author3=Bethe A | display-authors=3  | last4=Koopman  | first4=Jaap  | last5=Frosch  | first5=Matthias  | last6=Gerardy-Schahn  | first6=Rita }}
*{{cite journal  | author=Eckhardt M, Mühlenhoff M, Bethe A, ''et al.'' |title=Molecular characterization of eukaryotic polysialyltransferase-1. |journal=Nature |volume=373 |issue= 6516 |pages= 715-8 |year= 1995 |pmid= 7854457 |doi= 10.1038/373715a0 }}
*{{cite journal  | author=Angata K |title=Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 7182–90 |year= 1997 |pmid= 9054414 |doi=10.1074/jbc.272.11.7182 |name-list-format=vanc| author2=Nakayama J | author3=Fredette B  | display-authors=3  | last4=Chong  | first4=K | last5=Ranscht  | first5=B  | last6=Fukuda  | first6=M }}
*{{cite journal  | author=Angata K, Nakayama J, Fredette B, ''et al.'' |title=Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 7182-90 |year= 1997 |pmid= 9054414 |doi=  }}
*{{cite journal  |vauthors=Angata K, Suzuki M, Fukuda M |title=Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX |journal=J. Biol. Chem. |volume=273 |issue= 43 |pages= 28524–32 |year= 1998 |pmid= 9774483 |doi=10.1074/jbc.273.43.28524 }}
*{{cite journal | author=Angata K, Suzuki M, Fukuda M |title=Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX. |journal=J. Biol. Chem. |volume=273 |issue= 43 |pages= 28524-32 |year= 1998 |pmid= 9774483 |doi=  }}
*{{cite journal  |vauthors=Close BE, Colley KJ |title=In vivo autopolysialylation and localization of the polysialyltransferases PST and STX |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 34586–93 |year= 1999 |pmid= 9852130 |doi=10.1074/jbc.273.51.34586  }}
*{{cite journal  | author=Close BE, Colley KJ |title=In vivo autopolysialylation and localization of the polysialyltransferases PST and STX. |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 34586-93 |year= 1999 |pmid= 9852130 |doi=  }}
*{{cite journal  |vauthors=Close BE, Tao K, Colley KJ |title=Polysialyltransferase-1 autopolysialylation is not requisite for polysialylation of neural cell adhesion molecule |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4484–91 |year= 2000 |pmid= 10660622 |doi=10.1074/jbc.275.6.4484  }}
*{{cite journal  | author=Close BE, Tao K, Colley KJ |title=Polysialyltransferase-1 autopolysialylation is not requisite for polysialylation of neural cell adhesion molecule. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4484-91 |year= 2000 |pmid= 10660622 |doi= }}
*{{cite journal  | author=Angata K |title=Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18594–601 |year= 2000 |pmid= 10766765 |doi= 10.1074/jbc.M910204199 |name-list-format=vanc| author2=Suzuki M  | author3=McAuliffe J  | display-authors=3  | last4=Ding  | first4=Y  | last5=Hindsgaul  | first5=O  | last6=Fukuda  | first6=M }}
*{{cite journal  | author=Angata K, Suzuki M, McAuliffe J, ''et al.'' |title=Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18594-601 |year= 2000 |pmid= 10766765 |doi= 10.1074/jbc.M910204199 }}
*{{cite journal  | author=Angata K |title=Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15369–77 |year= 2001 |pmid= 11279095 |doi= 10.1074/jbc.M100576200 |name-list-format=vanc| author2=Yen TY  | author3=El-Battari A  | display-authors=3  | last4=Macher  | first4=BA  | last5=Fukuda  | first5=M }}
*{{cite journal  | author=Angata K, Yen TY, El-Battari A, ''et al.'' |title=Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15369-77 |year= 2001 |pmid= 11279095 |doi= 10.1074/jbc.M100576200 }}
*{{cite journal  | author=Close BE |title=The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule |journal=Glycobiology |volume=11 |issue= 11 |pages= 997–1008 |year= 2002 |pmid= 11744634 |doi=10.1093/glycob/11.11.997  |name-list-format=vanc| author2=Wilkinson JM  | author3=Bohrer TJ  | display-authors=3  | last4=Goodwin  | first4=CP  | last5=Broom  | first5=LJ  | last6=Colley  | first6=KJ  }}
*{{cite journal | author=Close BE, Wilkinson JM, Bohrer TJ, ''et al.'' |title=The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule. |journal=Glycobiology |volume=11 |issue= 11 |pages= 997-1008 |year= 2002 |pmid= 11744634 |doi=  }}
*{{cite journal  | author=Nałogowska-Głośnicka K |title=[Relationship between SA gene Pst1 polymorphism and predisposition to H-gestosis] |journal=Pol. Arch. Med. Wewn. |volume=107 |issue= 1 |pages= 7–11 |year= 2002 |pmid= 12046348 |doi=  |name-list-format=vanc| author2=Łacka B  | author3=Zychma M  | display-authors=3  | last4=Grzeszczak  | first4=W  | last5=Zukowska-Szczechowska  | first5=E  | last6=Michalski  | first6=B  | last7=Poreba  | first7=R | last8=Kniazewski  | first8=B  | last9=Rzempołuch  | first9=J  }}
*{{cite journal  | author=Nałogowska-Głośnicka K, Łacka B, Zychma M, ''et al.'' |title=[Relationship between SA gene Pst1 polymorphism and predisposition to H-gestosis] |journal=Pol. Arch. Med. Wewn. |volume=107 |issue= 1 |pages= 7-11 |year= 2002 |pmid= 12046348 |doi=  }}
*{{cite journal  |vauthors=Angata K, Suzuki M, Fukuda M |title=ST8Sia II and ST8Sia IV polysialyltransferases exhibit marked differences in utilizing various acceptors containing oligosialic acid and short polysialic acid. The basis for cooperative polysialylation by two enzymes |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 36808–17 |year= 2002 |pmid= 12138100 |doi= 10.1074/jbc.M204632200 }}
*{{cite journal  | author=Angata K, Suzuki M, Fukuda M |title=ST8Sia II and ST8Sia IV polysialyltransferases exhibit marked differences in utilizing various acceptors containing oligosialic acid and short polysialic acid. The basis for cooperative polysialylation by two enzymes. |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 36808-17 |year= 2002 |pmid= 12138100 |doi= 10.1074/jbc.M204632200 }}
*{{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal  | author=Gerhard DS |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  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{cite journal  | author=Beecken WD |title=Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells |journal=Int. Immunopharmacol. |volume=5 |issue= 4 |pages= 757–69 |year= 2005 |pmid= 15710344 |doi= 10.1016/j.intimp.2004.12.009  |name-list-format=vanc| author2=Engl T  | author3=Ogbomo H  | display-authors=3  | last4=Relja  | first4=B  | last5=Cinatl  | first5=J  | last6=Bereiterhahn  | first6=J  | last7=Oppermann  | first7=E  | last8=Jonas  | first8=D  | last9=Blaheta  | first9=R }}
*{{cite journal | author=Beecken WD, Engl T, Ogbomo H, ''et al.'' |title=Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells. |journal=Int. Immunopharmacol. |volume=5 |issue= 4 |pages= 757-69 |year= 2005 |pmid= 15710344 |doi= 10.1016/j.intimp.2004.12.009 }}
*{{cite journal  |vauthors=Mendiratta SS, Sekulic N, Lavie A, Colley KJ |title=Specific amino acids in the first fibronectin type III repeat of the neural cell adhesion molecule play a role in its recognition and polysialylation by the polysialyltransferase ST8Sia IV/PST |journal=J. Biol. Chem. |volume=280 |issue= 37 |pages= 32340–8 |year= 2005 |pmid= 16027151 |doi= 10.1074/jbc.M506217200 }}
*{{cite journal | author=Mendiratta SS, Sekulic N, Lavie A, Colley KJ |title=Specific amino acids in the first fibronectin type III repeat of the neural cell adhesion molecule play a role in its recognition and polysialylation by the polysialyltransferase ST8Sia IV/PST. |journal=J. Biol. Chem. |volume=280 |issue= 37 |pages= 32340-8 |year= 2005 |pmid= 16027151 |doi= 10.1074/jbc.M506217200 }}
*{{cite journal  |vauthors=Wang B, Hu H, Yu B |title=Molecular characterization of pig ST8Sia IV--a critical gene for the formation of neural cell adhesion molecule and its response to sialic acid supplement in piglets |journal=Nutritional neuroscience |volume=9 |issue= 3–4 |pages= 147–54 |year= 2007 |pmid= 17176637 |doi=10.1080/10284150600903594  }}
*{{cite journal  | author=Wang B, Hu H, Yu B |title=Molecular characterization of pig ST8Sia IV--a critical gene for the formation of neural cell adhesion molecule and its response to sialic acid supplement in piglets. |journal=Nutritional neuroscience |volume=9 |issue= 3-4 |pages= 147-54 |year= 2007 |pmid= 17176637 |doi= }}
*{{cite journal  |vauthors=Szabo R, Skropeta D, etal |title=Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities. |journal=Med. Res. Rev. |volume=37 |pages= 210-270 |year= 2017 |doi= 10.1002/med.21407 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Glycosyltransferases}}
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[[Category:EC 2.4.99]]
 
 
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Latest revision as of 07:08, 11 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

n/a

RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase is an enzyme that in humans is encoded by the ST8SIA4 gene.[1][2]

The protein encoded by this gene catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid, a modulator of the adhesive properties of neural cell adhesion molecule (NCAM1). The encoded protein, which is a member of glycosyltransferase family 29, is a type II membrane protein that may be present in the Golgi apparatus. Two transcript variants encoding different isoforms have been found for this gene.[2]

References

  1. ↑ Nakayama J, Fukuda MN, Fredette B, Ranscht B, Fukuda M (Aug 1995). "Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain". Proc Natl Acad Sci U S A. 92 (15): 7031–5. doi:10.1073/pnas.92.15.7031. PMC 41465. PMID 7624364.
  2. ↑ 2.0 2.1 "Entrez Gene: ST8SIA4 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4".

Further reading

  • Cohn JA, Noone PG, Jowell PS (2002). "Idiopathic pancreatitis related to CFTR: complex inheritance and identification of a modifier gene". J. Investig. Med. 50 (5): 247S–255S. PMID 12227654.
  • Eckhardt M, Mühlenhoff M, Bethe A, et al. (1995). "Molecular characterization of eukaryotic polysialyltransferase-1". Nature. 373 (6516): 715–8. doi:10.1038/373715a0. PMID 7854457.
  • Angata K, Nakayama J, Fredette B, et al. (1997). "Human STX polysialyltransferase forms the embryonic form of the neural cell adhesion molecule. Tissue-specific expression, neurite outgrowth, and chromosomal localization in comparison with another polysialyltransferase, PST". J. Biol. Chem. 272 (11): 7182–90. doi:10.1074/jbc.272.11.7182. PMID 9054414.
  • Angata K, Suzuki M, Fukuda M (1998). "Differential and cooperative polysialylation of the neural cell adhesion molecule by two polysialyltransferases, PST and STX". J. Biol. Chem. 273 (43): 28524–32. doi:10.1074/jbc.273.43.28524. PMID 9774483.
  • Close BE, Colley KJ (1999). "In vivo autopolysialylation and localization of the polysialyltransferases PST and STX". J. Biol. Chem. 273 (51): 34586–93. doi:10.1074/jbc.273.51.34586. PMID 9852130.
  • Close BE, Tao K, Colley KJ (2000). "Polysialyltransferase-1 autopolysialylation is not requisite for polysialylation of neural cell adhesion molecule". J. Biol. Chem. 275 (6): 4484–91. doi:10.1074/jbc.275.6.4484. PMID 10660622.
  • Angata K, Suzuki M, McAuliffe J, et al. (2000). "Differential biosynthesis of polysialic acid on neural cell adhesion molecule (NCAM) and oligosaccharide acceptors by three distinct alpha 2,8-sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III". J. Biol. Chem. 275 (24): 18594–601. doi:10.1074/jbc.M910204199. PMID 10766765.
  • Angata K, Yen TY, El-Battari A, et al. (2001). "Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity". J. Biol. Chem. 276 (18): 15369–77. doi:10.1074/jbc.M100576200. PMID 11279095.
  • Close BE, Wilkinson JM, Bohrer TJ, et al. (2002). "The polysialyltransferase ST8Sia II/STX: posttranslational processing and role of autopolysialylation in the polysialylation of neural cell adhesion molecule". Glycobiology. 11 (11): 997–1008. doi:10.1093/glycob/11.11.997. PMID 11744634.
  • Nałogowska-Głośnicka K, Łacka B, Zychma M, et al. (2002). "[Relationship between SA gene Pst1 polymorphism and predisposition to H-gestosis]". Pol. Arch. Med. Wewn. 107 (1): 7–11. PMID 12046348.
  • Angata K, Suzuki M, Fukuda M (2002). "ST8Sia II and ST8Sia IV polysialyltransferases exhibit marked differences in utilizing various acceptors containing oligosialic acid and short polysialic acid. The basis for cooperative polysialylation by two enzymes". J. Biol. Chem. 277 (39): 36808–17. doi:10.1074/jbc.M204632200. PMID 12138100.
  • 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): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Beecken WD, Engl T, Ogbomo H, et al. (2005). "Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells". Int. Immunopharmacol. 5 (4): 757–69. doi:10.1016/j.intimp.2004.12.009. PMID 15710344.
  • Mendiratta SS, Sekulic N, Lavie A, Colley KJ (2005). "Specific amino acids in the first fibronectin type III repeat of the neural cell adhesion molecule play a role in its recognition and polysialylation by the polysialyltransferase ST8Sia IV/PST". J. Biol. Chem. 280 (37): 32340–8. doi:10.1074/jbc.M506217200. PMID 16027151.
  • Wang B, Hu H, Yu B (2007). "Molecular characterization of pig ST8Sia IV--a critical gene for the formation of neural cell adhesion molecule and its response to sialic acid supplement in piglets". Nutritional neuroscience. 9 (3–4): 147–54. doi:10.1080/10284150600903594. PMID 17176637.
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