메뉴 건너뛰기




Volumn 22, Issue 5, 2012, Pages 602-615

Characterization of ppGalNAc-T18, a member of the vertebrate-specific y subfamily of UDP-N-acetyl-d-galactosamine:polypeptide N- acetylgalactosaminyltransferases

Author keywords

ER localization; glycosyltransferase; O glycan; O glycosylation; ppGalNAc T

Indexed keywords

CHAPERONE; N ACETYLGALACTOSAMINYLTRANSFERASE; URIDINE DIPHOSPHATE N ACETYLGALACTOSAMINE;

EID: 84859012703     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwr179     Document Type: Article
Times cited : (39)

References (40)
  • 1
    • 77449111350 scopus 로고    scopus 로고
    • The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase
    • Aryal RP, Ju T, Cummings RD. 2010. The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase. J Biol Chem. 285:2456-2462
    • (2010) J Biol Chem. , vol.285 , pp. 2456-2462
    • Aryal, R.P.1    Ju, T.2    Cummings, R.D.3
  • 2
    • 0030035111 scopus 로고    scopus 로고
    • CDNA cloning and expression of a novel human UDP-N-acetyl-α-D- galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3
    • Bennett EP, Hassan H, Clausen H. 1996. cDNA cloning and expression of a novel human UDP-N-acetyl-α-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3. J Biol Chem. 271:17006-17012
    • (1996) J Biol Chem. , vol.271 , pp. 17006-17012
    • Bennett, E.P.1    Hassan, H.2    Clausen, H.3
  • 3
    • 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
  • 4
    • 15444344929 scopus 로고    scopus 로고
    • Cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat
    • Bennett EP, Hassan H, Mandel U, Mirgorodskaya E, Roepstorff P, Burchell J, Taylor-Papadimitriou J, Hollingsworth MA, Merkx G, van Kessel AG, et al. 1998. Cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat. J Biol Chem. 273:30472-30481
    • (1998) J Biol Chem. , vol.273 , pp. 30472-30481
    • Bennett, E.P.1    Hassan, H.2    Mandel, U.3    Mirgorodskaya, E.4    Roepstorff, P.5    Burchell, J.6    Taylor-Papadimitriou, J.7    Hollingsworth, M.A.8    Merkx, G.9    Van Kessel, A.G.10
  • 5
    • 33744799438 scopus 로고    scopus 로고
    • Mucin-type O-glycans in human colon and breast cancer: Glycodynamics and functions
    • Brockhausen I. 2006. Mucin-type O-glycans in human colon and breast cancer: Glycodynamics and functions. EMBO Rep. 7:599-604
    • (2006) EMBO Rep. , vol.7 , pp. 599-604
    • Brockhausen, I.1
  • 6
    • 0001811291 scopus 로고    scopus 로고
    • Glycosyltransferases involved in N- and O-glycan biosynthesis
    • Gabius H, Gabius S, editors. Weinheim (DE): Chapman and Hall
    • Brockhausen I, Schachter H. 1997. Glycosyltransferases involved in N- and O-glycan biosynthesis. In Gabius H, Gabius S, editors. Glycosciences: Status and Perspectives. Weinheim (DE): Chapman and Hall. p. 79-114
    • (1997) Glycosciences: Status and Perspectives. , pp. 79-114
    • Brockhausen, I.1    Schachter, H.2
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0346037269 scopus 로고    scopus 로고
    • Mucin core O-glycosylation is modulated by neighboring residue glycosylation status. Kinetic modeling of the site-specific glycosylation of the apo-porcine submaxillary mucin tandem repeat by UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases T1 and T2
    • Gerken TA, Zhang J, Levine J, Elhammer A. 2002. Mucin core O-glycosylation is modulated by neighboring residue glycosylation status. Kinetic modeling of the site-specific glycosylation of the apo-porcine submaxillary mucin tandem repeat by UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferases T1 and T2. J Biol Chem. 277:49850-49862
    • (2002) J Biol Chem. , vol.277 , pp. 49850-49862
    • Gerken, T.A.1    Zhang, J.2    Levine, J.3    Elhammer, A.4
  • 10
    • 77953161781 scopus 로고    scopus 로고
    • Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes
    • Gill DJ, Chia J, Senewiratne J, Bard F. 2010. Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. J Cell Biol. 189:843-858
    • (2010) J Cell Biol. , vol.189 , pp. 843-858
    • Gill, D.J.1    Chia, J.2    Senewiratne, J.3    Bard, F.4
  • 11
    • 79952106660 scopus 로고    scopus 로고
    • Location, location, location: New insights into O-GalNAc protein glycosylation
    • Gill DJ, Clausen H, Bard F. 2011. Location, location, location: New insights into O-GalNAc protein glycosylation. Trends Cell Biol. 21:149-158
    • (2011) Trends Cell Biol. , vol.21 , pp. 149-158
    • Gill, D.J.1    Clausen, H.2    Bard, F.3
  • 12
    • 0344628712 scopus 로고    scopus 로고
    • Structure-function analysis of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold
    • Hagen FK, Hazes B, Raffo R, deSa D, Tabak LA. 1999. Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N- acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold. J Biol Chem. 274:6797-6803
    • (1999) J Biol Chem. , vol.274 , pp. 6797-6803
    • Hagen, F.K.1    Hazes, B.2    Raffo, R.3    De Sa, D.4    Tabak, L.A.5
  • 13
    • 0032478833 scopus 로고    scopus 로고
    • CDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans
    • Hagen FK, Nehrke K. 1998. cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans. J Biol Chem. 273:8268-8277
    • (1998) J Biol Chem. , vol.273 , pp. 8268-8277
    • Hagen, F.K.1    Nehrke, K.2
  • 14
    • 0030035805 scopus 로고    scopus 로고
    • The (QxW)3 domain: A flexible lectin scaffold
    • Hazes B. 1996. The (QxW)3 domain: A flexible lectin scaffold. Protein Sci. 5:1490-1501
    • (1996) Protein Sci. , vol.5 , pp. 1490-1501
    • Hazes, B.1
  • 15
    • 0037066753 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc- peptide β1,3-N-acetylglucosaminyltransferase (β3Gn-T6), an enzyme synthesizing the core 3 structure of O-glycans
    • Iwai T, Inaba N, Naundorf A, Zhang Y, Gotoh M, Iwasaki H, Kudo T, Togayachi A, Ishizuka Y, Nakanishi H, et al. 2002. Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-peptide β1,3-N- acetylglucosaminyltransferase (β3Gn-T6), an enzyme synthesizing the core 3 structure of O-glycans. J Biol Chem. 277:12802-12809
    • (2002) J Biol Chem. , vol.277 , pp. 12802-12809
    • Iwai, T.1    Inaba, N.2    Naundorf, A.3    Zhang, Y.4    Gotoh, M.5    Iwasaki, H.6    Kudo, T.7    Togayachi, A.8    Ishizuka, Y.9    Nakanishi, H.10
  • 16
    • 49749151409 scopus 로고    scopus 로고
    • Regulation of protein O-glycosylation by the endoplasmic reticulum-localized molecular chaperone Cosmc
    • Ju T, Aryal RP, Stowell CJ, Cummings RD. 2008. Regulation of protein O-glycosylation by the endoplasmic reticulum-localized molecular chaperone Cosmc. J Cell Biol. 182:531-542
    • (2008) J Cell Biol. , vol.182 , pp. 531-542
    • Ju, T.1    Aryal, R.P.2    Stowell, C.J.3    Cummings, R.D.4
  • 17
    • 0037168608 scopus 로고    scopus 로고
    • A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase
    • Ju T, Cummings RD. 2002. A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase. Proc Natl Acad Sci USA. 99:16613-16618
    • (2002) Proc Natl Acad Sci USA. , vol.99 , pp. 16613-16618
    • Ju, T.1    Cummings, R.D.2
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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
  • 22
    • 79955611128 scopus 로고    scopus 로고
    • Co-translational function of Cosmc, core 1 synthase specific molecular chaperone, revealed by a cell-free translation system
    • Narimatsu Y, Kubota T, Furukawa S, Shimojima M, Iwasaki H, Tozawa Y, Tachibana K, Narimatsu H. 2011. Co-translational function of Cosmc, core 1 synthase specific molecular chaperone, revealed by a cell-free translation system. FEBS Lett. 585:1276-1280
    • (2011) FEBS Lett. , vol.585 , pp. 1276-1280
    • Narimatsu, Y.1    Kubota, T.2    Furukawa, S.3    Shimojima, M.4    Iwasaki, H.5    Tozawa, Y.6    Tachibana, K.7    Narimatsu, H.8
  • 23
    • 79953708277 scopus 로고    scopus 로고
    • Polypeptide N-acetylgalactosaminyltransferase 6 disrupts mammary acinar morphogenesis through O-glycosylation of fibronectin
    • Park JH, Katagiri T, Chung S, Kijima K, Nakamura Y. 2011. Polypeptide N-acetylgalactosaminyltransferase 6 disrupts mammary acinar morphogenesis through O-glycosylation of fibronectin. Neoplasia. 13:320-326
    • (2011) Neoplasia. , vol.13 , pp. 320-326
    • Park, J.H.1    Katagiri, T.2    Chung, S.3    Kijima, K.4    Nakamura, Y.5
  • 24
    • 77950792706 scopus 로고    scopus 로고
    • Critical roles of mucin 1 glycosylation by transactivated polypeptide N-acetylgalactosaminyltransferase 6 in mammary carcinogenesis
    • Park JH, Nishidate T, Kijima K, Ohashi T, Takegawa K, Fujikane T, Hirata K, Nakamura Y, Katagiri T. 2010. Critical roles of mucin 1 glycosylation by transactivated polypeptide N-acetylgalactosaminyltransferase 6 in mammary carcinogenesis. Cancer Res. 70:2759-2769
    • (2010) Cancer Res. , vol.70 , pp. 2759-2769
    • Park, J.H.1    Nishidate, T.2    Kijima, K.3    Ohashi, T.4    Takegawa, K.5    Fujikane, T.6    Hirata, K.7    Nakamura, Y.8    Katagiri, T.9
  • 26
    • 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
  • 27
    • 0028587240 scopus 로고
    • Subcellular localization of the UDP-N-acetyl-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase- mediated O-glycosylation reaction in the submaxillary gland
    • Roth J, Wang Y, Eckhardt AE, Hill RL. 1994. Subcellular localization of the UDP-N-acetyl-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase- mediated O-glycosylation reaction in the submaxillary gland. Proc Natl Acad Sci USA. 91:8935-8939
    • (1994) Proc Natl Acad Sci USA. , vol.91 , pp. 8935-8939
    • Roth, J.1    Wang, Y.2    Eckhardt, A.E.3    Hill, R.L.4
  • 28
    • 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
  • 29
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M. 1987. The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol Biol Evol. 4:406-425
    • (1987) Mol Biol Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 30
    • 0037151059 scopus 로고    scopus 로고
    • Functional conservation of subfamilies of putative UDP-N- acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila
    • Schwientek T, Bennett EP, Flores C, Thacker J, Hollmann M, Reis CA, Behrens J, Mandel U, Keck B, Schafer MA, et al. 2002. Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila. J Biol Chem. 277:22623-22638
    • (2002) J Biol Chem. , vol.277 , pp. 22623-22638
    • Schwientek, T.1    Bennett, E.P.2    Flores, C.3    Thacker, J.4    Hollmann, M.5    Reis, C.A.6    Behrens, J.7    Mandel, U.8    Keck, B.9    Schafer, M.A.10
  • 33
    • 36248985010 scopus 로고    scopus 로고
    • Function of conserved aromatic residues in the Gal/GalNAc- glycosyltransferase motif of UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferase 1
    • Tenno M, Saeki A, Elhammer AP, Kurosaka A. 2007. Function of conserved aromatic residues in the Gal/GalNAc-glycosyltransferase motif of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1. FEBS J. 274:6037-6045
    • (2007) FEBS J. , vol.274 , pp. 6037-6045
    • Tenno, M.1    Saeki, A.2    Elhammer, A.P.3    Kurosaka, A.4
  • 34
    • 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
  • 35
    • 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
  • 37
    • 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
  • 38
    • 0037414798 scopus 로고    scopus 로고
    • Cloning and characterization of a new human UDP-N-acetyl-α-D- galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc α-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-α-D-galactosamine:polypeptide N- acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc α-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
  • 39
    • 78049381483 scopus 로고    scopus 로고
    • Dissecting the biological role of mucin-type O-glycosylation using RNA interference in Drosophila cell culture
    • Zhang L, Ten Hagen KG. 2010. Dissecting the biological role of mucin-type O-glycosylation using RNA interference in Drosophila cell culture. J Biol Chem. 285:34477-34484
    • (2010) J Biol Chem. , vol.285 , pp. 34477-34484
    • Zhang, L.1    Ten Hagen, K.G.2
  • 40
    • 77953512867 scopus 로고    scopus 로고
    • An O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand
    • Zhang L, Tran DT, Ten Hagen KG. 2010. An O-glycosyltransferase promotes cell adhesion during development by influencing secretion of an extracellular matrix integrin ligand. J Biol Chem. 285:19491-19501.
    • (2010) J Biol Chem. , vol.285 , pp. 19491-19501
    • Zhang, L.1    Tran, D.T.2    Ten Hagen, K.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.