메뉴 건너뛰기




Volumn 22, Issue 6, 2012, Pages 768-777

Erratum: UDP-N-acetyl-a-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferases: Completion of the family tree(Glycobiology (2012) 22: 6 (768-777) DOI:10.1093/glycob/cwr183);UDP-N-acetyl α-d-galactosamine: Polypeptide N- acetylgalactosaminyltransferases: Completion of the family tree

Author keywords

Enzyme activity; Expression analysis; GaNAcT; Splice variants

Indexed keywords

CARBOHYDRATE; ENZYME VARIANT; GLYCAN; GLYCOPEPTIDE; ISOENZYME; MUCIN; MUCIN 1; MUCIN 2; MUCIN 5AC; N ACETYLGALACTOSAMINYLTRANSFERASE; POLYPEPTIDE; TRANSFERASE; URIDINE DIPHOSPHATE N ACETYLGALACTOSAMINE;

EID: 84860381244     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwv003     Document Type: Erratum
Times cited : (75)

References (35)
  • 1
    • 84860365843 scopus 로고    scopus 로고
    • Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family
    • Bennett EP, Mandel U, Clausen H, Gerken TA, Fritz TA, Tabak LA. 2012. Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family. Glycobiology. 22: 736-756.
    • (2012) Glycobiology. , vol.22 , pp. 736-756
    • Bennett, E.P.1    Mandel, U.2    Clausen, H.3    Gerken, T.A.4    Fritz, T.A.5    Tabak, L.A.6
  • 2
    • 0032701175 scopus 로고    scopus 로고
    • A novel human UDP-N-acetyl-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates
    • Bennett EP, Hassan H, Hollingsworth MA, Clausen H. 1999. A novel human UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates. FEBS Lett. 460: 226-230.
    • (1999) FEBS Lett , vol.460 , pp. 226-230
    • Bennett, E.P.1    Hassan, H.2    Hollingsworth, M.A.3    Clausen, H.4
  • 3
    • 33847328331 scopus 로고    scopus 로고
    • Contribution of membrane mucins to tumor progression through modulation of cellular growth signaling pathways
    • Carraway KL, 3rd, Funes M, Workman HC, Sweeney C. 2007. Contribution of membrane mucins to tumor progression through modulation of cellular growth signaling pathways. Curr Top Dev Biol. 78: 1-22.
    • (2007) Curr Top Dev Biol , vol.78 , pp. 1-22
    • Carraway III, K.L.1    Funes, M.2    Workman, H.C.3    Sweeney, C.4
  • 4
    • 34250021602 scopus 로고    scopus 로고
    • Signaling mucins: The new kids on the MAPK block
    • Cullen PJ. 2007. Signaling mucins: The new kids on the MAPK block. Crit Rev Eukaryot Gene Expr. 17: 241-257.
    • (2007) Crit Rev Eukaryot Gene Expr , vol.17 , pp. 241-257
    • Cullen, P.J.1
  • 5
    • 7444220526 scopus 로고    scopus 로고
    • The beginnings of mucin biosynthesis: The crystal structure of UDP-GalNAc: Polypeptide α-N-acetylgalactosaminyltransferase-T1
    • Fritz TA, Hurley JH, Trinh LB, Shiloach J, Tabak LA. 2004. The beginnings of mucin biosynthesis: The crystal structure of UDP-GalNAc: polypeptide α-N-acetylgalactosaminyltransferase-T1. Proc Natl Acad Sci USA. 101: 15307-15312.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15307-15312
    • Fritz, T.A.1    Hurley, J.H.2    Trinh, L.B.3    Shiloach, J.4    Tabak, L.A.5
  • 6
    • 33646828699 scopus 로고    scopus 로고
    • Dynamic association between the catalytic and lectin domains of human UDP-GalNAc: Polypeptide α-N-acetylgalactosaminyltransferase-2
    • Fritz TA, Raman J, Tabak LA. 2006. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc: polypeptide α-N-acetylgalactosaminyltransferase-2. J Biol Chem. 281: 8613-8619.
    • (2006) J Biol Chem , vol.281 , pp. 8613-8619
    • Fritz, T.A.1    Raman, J.2    Tabak, L.A.3
  • 7
    • 0032500663 scopus 로고    scopus 로고
    • Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat
    • Gerken TA, Owens CL, Pasumarthy M. 1998. Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. J Biol Chem. 273: 26580-26588.
    • (1998) J Biol Chem , vol.273 , pp. 26580-26588
    • Gerken, T.A.1    Owens, C.L.2    Pasumarthy, M.3
  • 8
    • 54549083447 scopus 로고    scopus 로고
    • Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs
    • Gerken TA, Ten Hagen KG, Jamison O. 2008. Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs. Glycobiology. 18: 861-870.
    • (2008) Glycobiology , vol.18 , pp. 861-870
    • Gerken, T.A.1    Ten Hagen, K.G.2    Jamison, O.3
  • 9
    • 0037426326 scopus 로고    scopus 로고
    • Interdependence of backbone flexibility, residue conservation, and enzyme function: A case study on β1,4-galactosyltransferase-I
    • Gunasekaran K, Ma B, Ramakrishnan B, Qasba PK, Nussinov R. 2003. Interdependence of backbone flexibility, residue conservation, and enzyme function: A case study on β1,4-galactosyltransferase-I. Biochemistry. 42: 3674-3687.
    • (2003) Biochemistry , vol.42 , pp. 3674-3687
    • Gunasekaran, K.1    Ma, B.2    Ramakrishnan, B.3    Qasba, P.K.4    Nussinov, R.5
  • 10
    • 0030922124 scopus 로고    scopus 로고
    • CDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase
    • Hagen FK, Ten Hagen KG, Beres TM, Balys MM, VanWuyckhuyse BC, Tabak LA. 1997. cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase. J Biol Chem. 272: 13843-13848.
    • (1997) J Biol Chem , vol.272 , pp. 13843-13848
    • Hagen, F.K.1    Ten Hagen, K.G.2    Beres, T.M.3    Balys, M.M.4    Vanwuyckhuyse, B.C.5    Tabak, L.A.6
  • 11
    • 49949092699 scopus 로고    scopus 로고
    • Regulation of TGF-β signalling by N-acetylgalactosaminyltransferase- like 1
    • Herr P, Korniychuk G, Yamamoto Y, Grubisic K, Oelgeschlager M. 2008. Regulation of TGF-β signalling by N-acetylgalactosaminyltransferase-like 1. Development. 135: 1813-1822.
    • (2008) Development , vol.135 , pp. 1813-1822
    • Herr, P.1    Korniychuk, G.2    Yamamoto, Y.3    Grubisic, K.4    Oelgeschlager, M.5
  • 12
    • 33646795021 scopus 로고    scopus 로고
    • Structural basis of carbohydrate transfer activity by human UDP-GalNAc: Polypeptide α-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)
    • Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H. 2006. Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide α-N-acetylgalactosaminyltransferase (pp-GalNAc-T10). J Mol Biol. 359: 708-727.
    • (2006) J Mol Biol , vol.359 , pp. 708-727
    • Kubota, T.1    Shiba, T.2    Sugioka, S.3    Furukawa, S.4    Sawaki, H.5    Kato, R.6    Wakatsuki, S.7    Narimatsu, H.8
  • 13
    • 84859012703 scopus 로고    scopus 로고
    • Characterization of ppGalNAc-T18, a member of the vertebrate-specific y subfamily of UDP-N-acetyl-α-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferases
    • Li X, Wang J, Li W, Xu Y, Shao D, Xie Y, Xie W, Kubota T, Narimatsu H, Zhang Y. 2011. Characterization of ppGalNAc-T18, a member of the vertebrate-specific Y subfamily of UDP-N-acetyl-α-D-galactosamine: polypeptide N-acetylgalactosaminyltransferases. Glycobiology. 22: 602-615.
    • (2011) Glycobiology. , vol.22 , pp. 602-615
    • Li, X.1    Wang, J.2    Li, W.3    Xu, Y.4    Shao, D.5    Xie, Y.6    Xie, W.7    Kubota, T.8    Narimatsu, H.9    Zhang, Y.10
  • 15
    • 34548814998 scopus 로고    scopus 로고
    • Substrate-induced conformational changes and dynamics of UDP-N-acetylgalactosamine: Polypeptide N-acetylgalactosaminyltransferase-2
    • Milac AL, Buchete NV, Fritz TA, Hummer G, Tabak LA. 2007. Substrate-induced conformational changes and dynamics of UDP-N- acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase-2. J Mol Biol. 373: 439-451.
    • (2007) J Mol Biol , vol.373 , pp. 439-451
    • Milac, A.L.1    Buchete, N.V.2    Fritz, T.A.3    Hummer, G.4    Tabak, L.A.5
  • 16
    • 21144452401 scopus 로고    scopus 로고
    • Cloning and expression of a brain-specific putative UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase gene
    • Nakamura N, Toba S, Hirai M, Morishita S, Mikami T, Konishi M, Itoh N, Kurosaka A. 2005. Cloning and expression of a brain-specific putative UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase gene. Biol Pharm Bull. 28: 429-433.
    • (2005) Biol Pharm Bull , vol.28 , pp. 429-433
    • Nakamura, N.1    Toba, S.2    Hirai, M.3    Morishita, S.4    Mikami, T.5    Konishi, M.6    Itoh, N.7    Kurosaka, A.8
  • 17
    • 0030945377 scopus 로고    scopus 로고
    • Biosynthesis of a low-molecular-mass rat submandibular gland mucin glycoprotein in COS7 cells
    • Nehrke K, Tabak LA. 1997. Biosynthesis of a low-molecular-mass rat submandibular gland mucin glycoprotein in COS7 cells. Biochem J. 323(Pt 2): 497-502.
    • (1997) Biochem J , vol.323 , Issue.PART 2 , pp. 497-502
    • Nehrke, K.1    Tabak, L.A.2
  • 19
    • 67749133871 scopus 로고    scopus 로고
    • Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2
    • Perrine CL, Ganguli A, Wu P, Bertozzi CR, Fritz TA, Raman J, Tabak LA, Gerken TA. 2009. Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2. J Biol Chem. 284: 20387-20397.
    • (2009) J Biol Chem , vol.284 , pp. 20387-20397
    • Perrine, C.L.1    Ganguli, A.2    Wu, P.3    Bertozzi, C.R.4    Fritz, T.A.5    Raman, J.6    Tabak, L.A.7    Gerken, T.A.8
  • 20
    • 3343023761 scopus 로고    scopus 로고
    • Deconvoluting the functions of polypeptide N-α- acetylgalactosaminyltransferase family members by glycopeptide substrate profiling
    • Pratt MR, Hang HC, Ten Hagen KG, Rarick J, Gerken TA, Tabak LA, Bertozzi CR. 2004. Deconvoluting the functions of polypeptide N-α- acetylgalactosaminyltransferase family members by glycopeptide substrate profiling. Chem Biol. 11: 1009-1016.
    • (2004) Chem Biol , vol.11 , pp. 1009-1016
    • Pratt, M.R.1    Hang, H.C.2    Ten Hagen, K.G.3    Rarick, J.4    Gerken, T.A.5    Tabak, L.A.6    Bertozzi, C.R.7
  • 21
    • 53149142512 scopus 로고    scopus 로고
    • The catalytic and lectin domains of UDP-GalNAc: Polypeptide α-N-acetylgalactosaminyltransferase function in concert to direct glycosylation site selection
    • Raman J, Fritz TA, Gerken TA, Jamison O, Live D, Liu M, Tabak LA. 2008. The catalytic and lectin domains of UDP-GalNAc: polypeptide α-N- acetylgalactosaminyltransferase function in concert to direct glycosylation site selection. J Biol Chem. 283: 22942-22951.
    • (2008) J Biol Chem , vol.283 , pp. 22942-22951
    • Raman, J.1    Fritz, T.A.2    Gerken, T.A.3    Jamison, O.4    Live, D.5    Liu, M.6    Tabak, L.A.7
  • 22
    • 0039992226 scopus 로고    scopus 로고
    • Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus
    • Rottger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T. 1998. Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 111(Pt 1): 45-60.
    • (1998) J Cell Sci , vol.111 , Issue.PART 1 , pp. 45-60
    • Rottger, S.1    White, J.2    Wandall, H.H.3    Olivo, J.C.4    Stark, A.5    Bennett, E.P.6    Whitehouse, C.7    Berger, E.G.8    Clausen, H.9    Nilsson, T.10
  • 23
    • 33847716294 scopus 로고    scopus 로고
    • Innate immunity and mucus structure and function
    • discussion 167-159 216-159
    • Sheehan JK, Kesimer M, Pickles R. 2006. Innate immunity and mucus structure and function. Novartis Found Symp. 279: 155-166; discussion 167-159, 216-159.
    • (2006) Novartis Found Symp , vol.279 , pp. 155-166
    • Sheehan, J.K.1    Kesimer, M.2    Pickles, R.3
  • 24
    • 33747883766 scopus 로고    scopus 로고
    • Cell surface-associated mucins in signal transduction
    • Singh PK, Hollingsworth MA. 2006. Cell surface-associated mucins in signal transduction. Trends Cell Biol. 16: 467-476.
    • (2006) Trends Cell Biol , vol.16 , pp. 467-476
    • Singh, P.K.1    Hollingsworth, M.A.2
  • 26
    • 0028942854 scopus 로고
    • In defense of the oral cavity: Structure, biosynthesis, and function of salivary mucins
    • Tabak LA. 1995. In defense of the oral cavity: Structure, biosynthesis, and function of salivary mucins. Annu Rev Physiol. 57: 547-564.
    • (1995) Annu Rev Physiol , vol.57 , pp. 547-564
    • Tabak, L.A.1
  • 27
  • 28
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc: Polypeptide N- acetylgalactosaminyltransferases
    • Ten Hagen KG, Fritz TA, Tabak LA. 2003. All in the family: The UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferases. Glycobiology. 13: 1R-16R.
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 29
    • 0033600864 scopus 로고    scopus 로고
    • Characterization of a UDP-GalNAc: Polypeptide N- acetylgalactosaminyltransferase that displays glycopeptide N- acetylgalactosaminyltransferase activity
    • Ten Hagen KG, Tetaert D, Hagen FK, Richet C, Beres TM, Gagnon J, Balys MM, VanWuyckhuyse B, Bedi GS, Degand P, et al. 1999. Characterization of a UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase that displays glycopeptide N-acetylgalactosaminyltransferase activity. J Biol Chem. 274: 27867-27874.
    • (1999) J Biol Chem , vol.274 , pp. 27867-27874
    • Ten Hagen, K.G.1    Tetaert, D.2    Hagen, F.K.3    Richet, C.4    Beres, T.M.5    Gagnon, J.6    Balys, M.M.7    Vanwuyckhuyse, B.8    Bedi, G.S.9    Degand, P.10
  • 30
    • 0036049652 scopus 로고    scopus 로고
    • Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)
    • Tenno M, Toba S, Kezdy FJ, Elhammer AP, Kurosaka A. 2002. Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1). Eur J Biochem. 269: 4308-4316.
    • (2002) Eur J Biochem , vol.269 , pp. 4308-4316
    • Tenno, M.1    Toba, S.2    Kezdy, F.J.3    Elhammer, A.P.4    Kurosaka, A.5
  • 31
    • 0035395790 scopus 로고    scopus 로고
    • Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides
    • Tetaert D, Ten Hagen KG, Richet C, Boersma A, Gagnon J, Degand P. 2001. Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides. Biochem J. 357: 313-320.
    • (2001) Biochem J , vol.357 , pp. 313-320
    • Tetaert, D.1    Ten Hagen, K.G.2    Richet, C.3    Boersma, A.4    Gagnon, J.5    Degand, P.6
  • 32
    • 0034618602 scopus 로고    scopus 로고
    • Brain-specific expression of a novel human UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9)
    • Toba S, Tenno M, Konishi M, Mikami T, Itoh N, Kurosaka A. 2000. Brain-specific expression of a novel human UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9). Biochim Biophys Acta. 1493: 264-268.
    • (2000) Biochim Biophys Acta , vol.1493 , pp. 264-268
    • Toba, S.1    Tenno, M.2    Konishi, M.3    Mikami, T.4    Itoh, N.5    Kurosaka, A.6
  • 33
    • 0034603745 scopus 로고    scopus 로고
    • Molecular cloning of a novel human UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T8, and analysis as a candidate autosomal dominant hypophosphatemic rickets (ADHR) gene
    • White KE, Lorenz B, Evans WE, Meitinger T, Strom TM, Econs MJ. 2000. Molecular cloning of a novel human UDP-GalNAc: polypeptide N- acetylgalactosaminyltransferase, GalNAc-T8, and analysis as a candidate autosomal dominant hypophosphatemic rickets (ADHR) gene. Gene. 246: 347-356.
    • (2000) Gene , vol.246 , pp. 347-356
    • White, K.E.1    Lorenz, B.2    Evans, W.E.3    Meitinger, T.4    Strom, T.M.5    Econs, M.J.6
  • 34
    • 0038157153 scopus 로고    scopus 로고
    • Expression of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: A new view of a large family
    • Young WW, Jr, Holcomb DR, Ten Hagen KG, Tabak LA. 2003. Expression of UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: A new view of a large family. Glycobiology. 13: 549-557.
    • (2003) Glycobiology , vol.13 , pp. 549-557
    • Young Jr., W.W.1    Holcomb, D.R.2    Ten Hagen, K.G.3    Tabak, L.A.4
  • 35
    • 0037414798 scopus 로고    scopus 로고
    • Cloning and characterization of a new human UDP-N-acetyl-alpha-D- galactosamine: Polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen
    • Zhang Y, Iwasaki H, Wang H, Kudo T, Kalka TB, Hennet T, Kubota T, Cheng L, Inaba N, Gotoh M, et al. 2003. Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine: polypeptide N- acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen. J Biol Chem. 278: 573-584.
    • (2003) J Biol Chem , vol.278 , pp. 573-584
    • Zhang, Y.1    Iwasaki, H.2    Wang, H.3    Kudo, T.4    Kalka, T.B.5    Hennet, T.6    Kubota, T.7    Cheng, L.8    Inaba, N.9    Gotoh, M.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.