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Volumn 89, Issue 3, 2011, Pages 407-414

ST3GAL3 mutations impair the development of higher cognitive functions

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDE ALPHA2, 3 SIALYLTRANSFERASE III; ENZYME; UNCLASSIFIED DRUG;

EID: 80052722309     PISSN: 00029297     EISSN: 15376605     Source Type: Journal    
DOI: 10.1016/j.ajhg.2011.08.008     Document Type: Article
Times cited : (91)

References (49)
  • 1
    • 10644243538 scopus 로고    scopus 로고
    • X-linked mental retardation
    • DOI 10.1038/nrg1501
    • H.H. Ropers, and B.C. Hamel X-linked mental retardation Nat. Rev. Genet. 6 2005 46 57 (Pubitemid 39657897)
    • (2005) Nature Reviews Genetics , vol.6 , Issue.1 , pp. 46-57
    • Ropers, H.-H.1    Hamel, B.C.J.2
  • 2
    • 52949098733 scopus 로고    scopus 로고
    • Genetics of intellectual disability
    • H.H. Ropers Genetics of intellectual disability Curr. Opin. Genet. Dev. 18 2008 241 250
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 241-250
    • Ropers, H.H.1
  • 3
    • 77957968873 scopus 로고    scopus 로고
    • Genetics of early onset cognitive impairment
    • H.H. Ropers Genetics of early onset cognitive impairment Annu. Rev. Genomics Hum. Genet. 11 2010 161 187
    • (2010) Annu. Rev. Genomics Hum. Genet. , vol.11 , pp. 161-187
    • Ropers, H.H.1
  • 4
    • 0027201584 scopus 로고
    • Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase
    • H. Kitagawa, and J.C. Paulson Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase Biochem. Biophys. Res. Commun. 194 1993 375 382
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 375-382
    • Kitagawa, H.1    Paulson, J.C.2
  • 6
    • 3943056897 scopus 로고    scopus 로고
    • Role of glycosylation in development
    • DOI 10.1146/annurev.biochem.73.011303.074043
    • R.S. Haltiwanger, and J.B. Lowe Role of glycosylation in development Annu. Rev. Biochem. 73 2004 491 537 (Pubitemid 39050378)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 491-537
    • Haltiwanger, R.S.1    Lowe, J.B.2
  • 7
    • 1342310622 scopus 로고    scopus 로고
    • Glycans and neural cell interactions
    • R. Kleene, and M. Schachner Glycans and neural cell interactions Nat. Rev. Neurosci. 5 2004 195 208 (Pubitemid 38252476)
    • (2004) Nature Reviews Neuroscience , vol.5 , Issue.3 , pp. 195-208
    • Kleene, R.1    Schachner, M.2
  • 8
    • 0036840817 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: A review
    • DOI 10.1203/01.PDR.0000031921.02259.35
    • S. Grunewald, G. Matthijs, and J. Jaeken Congenital disorders of glycosylation: A review Pediatr. Res. 52 2002 618 624 (Pubitemid 35286026)
    • (2002) Pediatric Research , vol.52 , Issue.5 , pp. 618-624
    • Grunewald, S.1    Matthijs, G.2    Jaeken, J.3
  • 9
    • 0037605951 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: Review of their molecular bases, clinical presentations and specific therapies
    • T. Marquardt, and J. Denecke Congenital disorders of glycosylation: Review of their molecular bases, clinical presentations and specific therapies Eur. J. Pediatr. 162 2003 359 379 (Pubitemid 36693736)
    • (2003) European Journal of Pediatrics , vol.162 , Issue.6 , pp. 359-379
    • Marquardt, T.1    Denecke, J.2
  • 12
    • 77956041687 scopus 로고    scopus 로고
    • The sialome - Far more than the sum of its parts
    • M. Cohen, and A. Varki The sialome - far more than the sum of its parts OMICS 14 2010 455 464
    • (2010) OMICS , vol.14 , pp. 455-464
    • Cohen, M.1    Varki, A.2
  • 13
    • 70349878950 scopus 로고    scopus 로고
    • Sialic acids as regulators of molecular and cellular interactions
    • R. Schauer Sialic acids as regulators of molecular and cellular interactions Curr. Opin. Struct. Biol. 19 2009 507 514
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 507-514
    • Schauer, R.1
  • 15
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • DOI 10.1038/nri2056, PII NRI2056
    • P.R. Crocker, J.C. Paulson, and A. Varki Siglecs and their roles in the immune system Nat. Rev. Immunol. 7 2007 255 266 (Pubitemid 46480955)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.4 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 16
    • 79751521478 scopus 로고    scopus 로고
    • Biomedical differences between human and nonhuman hominids: Potential roles for uniquely human aspects of sialic acid biology
    • N.M. Varki, E. Strobert, E.J. Dick Jr., K. Benirschke, and A. Varki Biomedical differences between human and nonhuman hominids: Potential roles for uniquely human aspects of sialic acid biology Annu. Rev. Pathol. 6 2011 365 393
    • (2011) Annu. Rev. Pathol. , vol.6 , pp. 365-393
    • Varki, N.M.1    Strobert, E.2    Dick, Jr.E.J.3    Benirschke, K.4    Varki, A.5
  • 17
    • 77952369047 scopus 로고    scopus 로고
    • Colloquium paper: Uniquely human evolution of sialic acid genetics and biology
    • A. Varki Colloquium paper: Uniquely human evolution of sialic acid genetics and biology Proc. Natl. Acad. Sci. USA 107 Suppl 2 2010 8939 8946
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , Issue.SUPPL 2 , pp. 8939-8946
    • Varki, A.1
  • 18
    • 0020491419 scopus 로고
    • Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase and a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase from rat liver
    • J. Weinstein, U. de Souza-e-Silva, and J.C. Paulson Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase and a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase from rat liver J. Biol. Chem. 257 1982 13845 13853
    • (1982) J. Biol. Chem. , vol.257 , pp. 13845-13853
    • Weinstein, J.1    De Souza-E-Silva, U.2    Paulson, J.C.3
  • 19
    • 78951473016 scopus 로고    scopus 로고
    • Autosomal recessive mental retardation: Homozygosity mapping identifies 27 single linkage intervals, at least 14 novel loci and several mutation hotspots
    • A.W. Kuss, M. Garshasbi, K. Kahrizi, A. Tzschach, F. Behjati, H. Darvish, L. Abbasi-Moheb, L. Puettmann, A. Zecha, and R. Weissmann Autosomal recessive mental retardation: homozygosity mapping identifies 27 single linkage intervals, at least 14 novel loci and several mutation hotspots Hum. Genet. 129 2011 141 148
    • (2011) Hum. Genet. , vol.129 , pp. 141-148
    • Kuss, A.W.1    Garshasbi, M.2    Kahrizi, K.3    Tzschach, A.4    Behjati, F.5    Darvish, H.6    Abbasi-Moheb, L.7    Puettmann, L.8    Zecha, A.9    Weissmann, R.10
  • 22
    • 84975742565 scopus 로고    scopus 로고
    • A map of human genome variation from population-scale sequencing
    • 1000 Genomes Project Consortium
    • 1000 Genomes Project Consortium A map of human genome variation from population-scale sequencing Nature 467 2010 1061 1073
    • (2010) Nature , vol.467 , pp. 1061-1073
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 25144496606 scopus 로고    scopus 로고
    • PMUT: A web-based tool for the annotation of pathological mutations on proteins
    • DOI 10.1093/bioinformatics/bti486
    • C. Ferrer-Costa, J.L. Gelpí, L. Zamakola, I. Parraga, X. de la Cruz, and M. Orozco PMUT: A web-based tool for the annotation of pathological mutations on proteins Bioinformatics 21 2005 3176 3178 (Pubitemid 41418475)
    • (2005) Bioinformatics , vol.21 , Issue.14 , pp. 3176-3178
    • Ferrer-Costa, C.1    Gelpi, J.L.2    Zamakola, L.3    Parraga, I.4    De La Cruz, X.5    Orozco, M.6
  • 28
    • 68149165614 scopus 로고    scopus 로고
    • Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm
    • P. Kumar, S. Henikoff, and P.C. Ng Predicting the effects of coding non-synonymous variants on protein function using the SIFT algorithm Nat. Protoc. 4 2009 1073 1081
    • (2009) Nat. Protoc. , vol.4 , pp. 1073-1081
    • Kumar, P.1    Henikoff, S.2    Ng, P.C.3
  • 29
    • 77955151784 scopus 로고    scopus 로고
    • MutationTaster evaluates disease-causing potential of sequence alterations
    • J.M. Schwarz, C. Rödelsperger, M. Schuelke, and D. Seelow MutationTaster evaluates disease-causing potential of sequence alterations Nat. Methods 7 2010 575 576
    • (2010) Nat. Methods , vol.7 , pp. 575-576
    • Schwarz, J.M.1    Rödelsperger, C.2    Schuelke, M.3    Seelow, D.4
  • 30
    • 0020037889 scopus 로고
    • Immunocytochemical localization of galactosyltransferase in HeLa cells: Codistribution with thiamine pyrophosphatase in trans-Golgi cisternae
    • DOI 10.1083/jcb.93.1.223
    • J. Roth, and E.G. Berger Immunocytochemical localization of galactosyltransferase in HeLa cells: Codistribution with thiamine pyrophosphatase in trans-Golgi cisternae J. Cell Biol. 93 1982 223 229 (Pubitemid 12117060)
    • (1982) Journal of Cell Biology , vol.93 , Issue.1 , pp. 223-229
    • Roth, J.1    Berger, E.G.2
  • 31
    • 0031594236 scopus 로고    scopus 로고
    • Immunocytochemical localization of alpha2,3(N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: Evidence for golgi and post-golgi localization
    • P.C. Burger, M. Lötscher, M. Streiff, R. Kleene, B. Kaissling, and E.G. Berger Immunocytochemical localization of alpha2,3(N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: Evidence for golgi and post-golgi localization Glycobiology 8 1998 245 257
    • (1998) Glycobiology , vol.8 , pp. 245-257
    • Burger, P.C.1    Lötscher, M.2    Streiff, M.3    Kleene, R.4    Kaissling, B.5    Berger, E.G.6
  • 32
    • 0035805602 scopus 로고    scopus 로고
    • Conserved cysteines in the sialyltransferase sialylmotifs form an essential disulfide bond
    • A.K. Datta, R. Chammas, and J.C. Paulson Conserved cysteines in the sialyltransferase sialylmotifs form an essential disulfide bond J. Biol. Chem. 276 2001 15200 15207
    • (2001) J. Biol. Chem. , vol.276 , pp. 15200-15207
    • Datta, A.K.1    Chammas, R.2    Paulson, J.C.3
  • 33
    • 73749085462 scopus 로고    scopus 로고
    • Localization of Golgi-resident glycosyltransferases
    • L. Tu, and D.K. Banfield Localization of Golgi-resident glycosyltransferases Cell. Mol. Life Sci. 67 2010 29 41
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 29-41
    • Tu, L.1    Banfield, D.K.2
  • 34
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulum-associated degradation
    • J. Hoseki, R. Ushioda, and K. Nagata Mechanism and components of endoplasmic reticulum-associated degradation J. Biochem. 147 2010 19 25
    • (2010) J. Biochem. , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 35
    • 0037287977 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein degradation
    • DOI 10.1016/S0074-7696(05)23002-4
    • E. Jarosch, U. Lenk, and T. Sommer Endoplasmic reticulum-associated protein degradation Int. Rev. Cytol. 223 2003 39 81 (Pubitemid 36278511)
    • (2003) International Review of Cytology , vol.223 , pp. 39-81
    • Jarosch, E.1    Lenk, U.2    Sommer, T.3
  • 37
    • 68149131942 scopus 로고    scopus 로고
    • Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis
    • S.O. Reinke, G. Lehmer, S. Hinderlich, and W. Reutter Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis Biol. Chem. 390 2009 591 599
    • (2009) Biol. Chem. , vol.390 , pp. 591-599
    • Reinke, S.O.1    Lehmer, G.2    Hinderlich, S.3    Reutter, W.4
  • 38
    • 0030974649 scopus 로고    scopus 로고
    • Mouse β-galactoside α2,3-sialyltransferases: Comparison of in vitro substrate specificities and tissue specific expression
    • DOI 10.1093/glycob/7.4.469
    • M. Kono, Y. Ohyama, Y.C. Lee, T. Hamamoto, N. Kojima, and S. Tsuji Mouse beta-galactoside alpha 2,3-sialyltransferases: Comparison of in vitro substrate specificities and tissue specific expression Glycobiology 7 1997 469 479 (Pubitemid 27246720)
    • (1997) Glycobiology , vol.7 , Issue.4 , pp. 469-479
    • Kono, M.1    Ohyama, Y.2    Lee, Y.-C.3    Hamamoto, T.4    Kojima, N.5    Tsuji, S.6
  • 39
    • 72649085741 scopus 로고    scopus 로고
    • Anti-oligosaccharide antibodies as tools for studying sulfated sialoglycoconjugate ligands for siglecs and selectins
    • R. Kannagi, K. Ohmori, and N. Kimura Anti-oligosaccharide antibodies as tools for studying sulfated sialoglycoconjugate ligands for siglecs and selectins Glycoconj. J. 26 2009 923 928
    • (2009) Glycoconj. J. , vol.26 , pp. 923-928
    • Kannagi, R.1    Ohmori, K.2    Kimura, N.3
  • 40
    • 0038499694 scopus 로고    scopus 로고
    • Cloning and sequencing of nineteen transcript isoforms of the human α2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues
    • DOI 10.1023/A:1024253808424
    • A. Grahn, G.S. Barkhordar, and G. Larson Cloning and sequencing of nineteen transcript isoforms of the human alpha2,3-sialyltransferase gene, ST3Gal III; its genomic organisation and expression in human tissues Glycoconj. J. 19 2002 197 210 (Pubitemid 36851263)
    • (2002) Glycoconjugate Journal , vol.19 , Issue.3 , pp. 197-210
    • Grahn, A.1    Barkhordar, G.S.2    Larson, G.3
  • 42
    • 0025979045 scopus 로고
    • Localization of glycosylation sites in the Golgi apparatus using immunolabeling and cytochemistry
    • J. Roth Localization of glycosylation sites in the Golgi apparatus using immunolabeling and cytochemistry J. Electron Microsc. Tech. 17 1991 121 131
    • (1991) J. Electron Microsc. Tech. , vol.17 , pp. 121-131
    • Roth, J.1
  • 46
    • 79953001206 scopus 로고    scopus 로고
    • Sialic acids attached to O-glycans modulate voltage-gated potassium channel gating
    • T.A. Schwetz, S.A. Norring, A.R. Ednie, and E.S. Bennett Sialic acids attached to O-glycans modulate voltage-gated potassium channel gating J. Biol. Chem. 286 2011 4123 4132
    • (2011) J. Biol. Chem. , vol.286 , pp. 4123-4132
    • Schwetz, T.A.1    Norring, S.A.2    Ednie, A.R.3    Bennett, E.S.4
  • 49
    • 79960837291 scopus 로고    scopus 로고
    • Voltage-gated potassium channel antibody associated mood disorder without paraneoplastic disease
    • S. Kitten, N. Gupta, R.M. Bloch, and C.K. Dunham Voltage-gated potassium channel antibody associated mood disorder without paraneoplastic disease Biol. Psychiatry 70 2011 e15 e17
    • (2011) Biol. Psychiatry , vol.70
    • Kitten, S.1    Gupta, N.2    Bloch, R.M.3    Dunham, C.K.4


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