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Volumn 289, Issue 17, 2014, Pages 11630-11641

Identification of a novel protein binding motif within the t-synthase for the molecular chaperone cosmc

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Indexed keywords

BIOCHEMISTRY;

EID: 84899460156     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.555870     Document Type: Article
Times cited : (21)

References (67)
  • 1
    • 62449106207 scopus 로고    scopus 로고
    • Recent insights into the biological roles of mucin-type O-glycosylation
    • Tian, E., and Ten Hagen, K. G. (2009) Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconj. J. 26, 325-334
    • (2009) Glycoconj. J. , vol.26 , pp. 325-334
    • Tian, E.1    Ten Hagen, K.G.2
  • 3
    • 22844433667 scopus 로고    scopus 로고
    • The chemistry and biology of mucin-type O-linked glycosylation
    • Hang, H. C., and Bertozzi, C. R. (2005) The chemistry and biology of mucin-type O-linked glycosylation. Bioorg. Med. Chem. 13, 5021-5034
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 5021-5034
    • Hang, H.C.1    Bertozzi, C.R.2
  • 5
    • 1942542931 scopus 로고    scopus 로고
    • Ligands for L-selectin: Homing, inflammation, and beyond
    • Rosen, S. D. (2004) Ligands for L-selectin: homing, inflammation, and beyond. Annu. Rev. Immunol. 22, 129-156
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 129-156
    • Rosen, S.D.1
  • 6
    • 0030854107 scopus 로고    scopus 로고
    • Perspectives series: Cell adhesion in vascular biology: Role of PSGL-1 binding to selectins in leukocyte recruitment
    • McEver, R. P., and Cummings, R. D. (1997) Perspectives series: cell adhesion in vascular biology: role of PSGL-1 binding to selectins in leukocyte recruitment. J. Clin. Invest. 100, 485-491
    • (1997) J. Clin. Invest. , vol.100 , pp. 485-491
    • McEver, R.P.1    Cummings, R.D.2
  • 7
    • 0031472384 scopus 로고    scopus 로고
    • Role of PSGL-1 binding to selectins in leukocyte recruitment
    • McEver, R. P., and Cummings, R. D. (1997) Role of PSGL-1 binding to selectins in leukocyte recruitment. J. Clin. Invest. 100, S97-S103
    • (1997) J. Clin. Invest. , vol.100
    • McEver, R.P.1    Cummings, R.D.2
  • 10
    • 79952748335 scopus 로고    scopus 로고
    • The two mucus layers of colon are organized by the MUC2 mucin, whereas the outer layer is a legislator of host-microbial interactions
    • Johansson, M. E., Larsson, J. M., and Hansson, G. C. (2011) The two mucus layers of colon are organized by the MUC2 mucin, whereas the outer layer is a legislator of host-microbial interactions. Proc. Natl. Acad. Sci. U.S.A. 108, 4659-4665
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 4659-4665
    • Johansson, M.E.1    Larsson, J.M.2    Hansson, G.C.3
  • 11
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferases
    • Ten Hagen, K. G., Fritz, T. A., and Tabak, L. A. (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
  • 12
    • 0037016720 scopus 로고    scopus 로고
    • Cloning and expression of human core 1 β1,3-galactosyltransferase
    • Ju, T., Brewer, K., D'Souza, A., Cummings, R. D., and Canfield, W. M. (2002) Cloning and expression of human core 1 β1,3-galactosyltransferase. J. Biol. Chem. 277, 178-186
    • (2002) J. Biol. Chem. , vol.277 , pp. 178-186
    • Ju, T.1    Brewer, K.2    D'souza, A.3    Cummings, R.D.4    Canfield, W.M.5
  • 13
    • 0037016738 scopus 로고    scopus 로고
    • Purification, characterization, and subunit structure of rat core 1 β1,3-galactosyltransferase
    • Ju, T., Cummings, R. D., and Canfield, W. M. (2002) Purification, characterization, and subunit structure of rat core 1 β1,3- galactosyltransferase. J. Biol. Chem. 277, 169-177
    • (2002) J. Biol. Chem. , vol.277 , pp. 169-177
    • Ju, T.1    Cummings, R.D.2    Canfield, W.M.3
  • 14
    • 0021813383 scopus 로고
    • Mucin synthesis: UDP-GlcNAc:GalNAc-R β3-N- acetylglucosaminyltransferase and UDP-GlcNAc:GlcNAc β1-3GalNAc-R (GlcNAc to GalNAc) β6-Nacetylglucosaminyltransferase from pig and rat colon mucosa
    • Brockhausen, I., Matta, K. L., Orr, J., and Schachter, H. (1985) Mucin synthesis: UDP-GlcNAc:GalNAc-R β3-N-acetylglucosaminyltransferase and UDP-GlcNAc:GlcNAc β1-3GalNAc-R (GlcNAc to GalNAc) β6- Nacetylglucosaminyltransferase from pig and rat colon mucosa. Biochemistry 24, 1866-1874
    • (1985) Biochemistry , vol.24 , pp. 1866-1874
    • Brockhausen, I.1    Matta, K.L.2    Orr, J.3    Schachter, H.4
  • 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., and Narimatsu, H. (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    Narimatsu, H.11
  • 16
    • 77449111350 scopus 로고    scopus 로고
    • The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase
    • Aryal, R. P., Ju, T., and Cummings, R. D. (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
  • 17
    • 49749151409 scopus 로고    scopus 로고
    • Regulation of protein O-glycosylation by the endoplasmic reticulum-localized molecular chaperone Cosmc
    • Ju, T., Aryal, R. P., Stowell, C. J., and Cummings, R. D. (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
  • 18
    • 0037168608 scopus 로고    scopus 로고
    • A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase
    • Ju, T., and Cummings, R. D. (2002) A unique molecular chaperone Cosmc required for activity of the mammalian core 1 β3-galactosyltransferase. Proc. Natl. Acad. Sci. U.S.A. 99, 16613-16618
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16613-16618
    • Ju, T.1    Cummings, R.D.2
  • 19
    • 84860868131 scopus 로고    scopus 로고
    • Tight complex formation between Cosmc chaperone and its specific client non-native T-synthase leads to enzyme activity and client-driven dissociation
    • Aryal, R. P., Ju, T., and Cummings, R. D. (2012) Tight complex formation between Cosmc chaperone and its specific client non-native T-synthase leads to enzyme activity and client-driven dissociation. J. Biol. Chem. 287, 15317-15329
    • (2012) J. Biol. Chem. , vol.287 , pp. 15317-15329
    • Aryal, R.P.1    Ju, T.2    Cummings, R.D.3
  • 20
    • 27644442375 scopus 로고    scopus 로고
    • Protein glycosylation: Chaperone mutation in Tn syndrome
    • Ju, T., and Cummings, R. D. (2005) Protein glycosylation: chaperone mutation in Tn syndrome. Nature 437, 1252
    • (2005) Nature , vol.437 , pp. 1252
    • Ju, T.1    Cummings, R.D.2
  • 23
    • 79951801155 scopus 로고    scopus 로고
    • The Tn antigen-structural simplicity and biological complexity
    • Ju, T., Otto, V. I., and Cummings, R. D. (2011) The Tn antigen-structural simplicity and biological complexity. Angew. Chem. Int. Ed. Engl. 50, 1770-1791
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 1770-1791
    • Ju, T.1    Otto, V.I.2    Cummings, R.D.3
  • 24
    • 0021141716 scopus 로고
    • T and Tn, general carcinoma autoantigens
    • Springer, G. F. (1984) T and Tn, general carcinoma autoantigens. Science 224, 1198-1206
    • (1984) Science , vol.224 , pp. 1198-1206
    • Springer, G.F.1
  • 26
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 27
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink, A. L. (1999) Chaperone-mediated protein folding. Physiol. Rev. 79, 425-449
    • (1999) Physiol. Rev. , vol.79 , pp. 425-449
    • Fink, A.L.1
  • 28
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. (1996) Molecular chaperones in cellular protein folding. Nature 381, 571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 30
    • 0037144495 scopus 로고    scopus 로고
    • Molecular cloning and enzymatic characterization of a UDP-GalNAc:GlcNAc(β)-R β1,4-Nacetylgalactosaminyltransferase from Caenorhabditis elegans
    • Kawar, Z. S., Van Die, I., and Cummings, R. D. (2002) Molecular cloning and enzymatic characterization of a UDP-GalNAc:GlcNAc(β)-R β1,4-Nacetylgalactosaminyltransferase from Caenorhabditis elegans. J. Biol. Chem. 277, 34924-34932
    • (2002) J. Biol. Chem. , vol.277 , pp. 34924-34932
    • Kawar, Z.S.1    Van Die, I.2    Cummings, R.D.3
  • 31
    • 0033005637 scopus 로고    scopus 로고
    • The acceptor substrate specificity of human β4-galactosyltransferase v indicates its potential function in O-glycosylation
    • van Die, I., van Tetering, A., Schiphorst, W. E., Sato, T., Furukawa, K., and van den Eijnden, D. H. (1999) The acceptor substrate specificity of human β4-galactosyltransferase V indicates its potential function in O-glycosylation. FEBS Lett. 450, 52-56
    • (1999) FEBS Lett. , vol.450 , pp. 52-56
    • Van Die, I.1    Van Tetering, A.2    Schiphorst, W.E.3    Sato, T.4    Furukawa, K.5    Van Den Eijnden, D.H.6
  • 32
    • 42949090427 scopus 로고    scopus 로고
    • Structure and function of β-1,4-galactosyltransferase
    • Qasba, P. K., Ramakrishnan, B., and Boeggeman, E. (2008) Structure and function of β-1,4-galactosyltransferase. Curr Drug Targets 9, 292-309
    • (2008) Curr Drug Targets , vol.9 , pp. 292-309
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 33
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. (1973) Principles that govern the folding of protein chains. Science 181, 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 35
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi, S., Cwirla, S. E., Dower, W. J., Lipshutz, R. J., Sprang, S. R., Sambrook, J. F., and Gething, M. J. (1993) Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717-728
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.F.6    Gething, M.J.7
  • 36
    • 77954502545 scopus 로고    scopus 로고
    • A more precise characterization of chaperonin substrates
    • Raineri, E., Ribeca, P., Serrano, L., and Maier, T. (2010) A more precise characterization of chaperonin substrates. Bioinformatics 26, 1685-1689
    • (2010) Bioinformatics , vol.26 , pp. 1685-1689
    • Raineri, E.1    Ribeca, P.2    Serrano, L.3    Maier, T.4
  • 38
    • 0035966068 scopus 로고    scopus 로고
    • The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis
    • Dafforn, T. R., Della, M., and Miller, A. D. (2001) The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis. J. Biol. Chem. 276, 49310-49319
    • (2001) J. Biol. Chem. , vol.276 , pp. 49310-49319
    • Dafforn, T.R.1    Della, M.2    Miller, A.D.3
  • 39
    • 0037155282 scopus 로고    scopus 로고
    • Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47
    • Koide, T., Takahara, Y., Asada, S., and Nagata, K. (2002) Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47. J. Biol. Chem. 277, 6178-6182
    • (2002) J. Biol. Chem. , vol.277 , pp. 6178-6182
    • Koide, T.1    Takahara, Y.2    Asada, S.3    Nagata, K.4
  • 40
    • 33645639418 scopus 로고    scopus 로고
    • Specific recognition of the collagen triple helix by chaperone HSP47: Minimal structural requirement and spatial molecular orientation
    • Koide, T., Asada, S., Takahara, Y., Nishikawa, Y., Nagata, K., and Kitagawa, K. (2006) Specific recognition of the collagen triple helix by chaperone HSP47: Minimal structural requirement and spatial molecular orientation. J. Biol. Chem. 281, 3432-3438
    • (2006) J. Biol. Chem. , vol.281 , pp. 3432-3438
    • Koide, T.1    Asada, S.2    Takahara, Y.3    Nishikawa, Y.4    Nagata, K.5    Kitagawa, K.6
  • 42
    • 0034795208 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
    • Randow, F., and Seed, B. (2001) Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nat. Cell Biol. 3, 891-896
    • (2001) Nat. Cell Biol. , vol.3 , pp. 891-896
    • Randow, F.1    Seed, B.2
  • 43
    • 33847260278 scopus 로고    scopus 로고
    • Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages
    • Yang, Y., Liu, B., Dai, J., Srivastava, P. K., Zammit, D. J., Lefrançois, L., and Li, Z. (2007) Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages. Immunity 26, 215-226
    • (2007) Immunity , vol.26 , pp. 215-226
    • Yang, Y.1    Liu, B.2    Dai, J.3    Srivastava, P.K.4    Zammit, D.J.5    Lefrançois, L.6    Li, Z.7
  • 44
    • 84863115806 scopus 로고    scopus 로고
    • The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain
    • Wu, S., Hong, F., Gewirth, D., Guo, B., Liu, B., and Li, Z. (2012) The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain. J. Biol. Chem. 287, 6735-6742
    • (2012) J. Biol. Chem. , vol.287 , pp. 6735-6742
    • Wu, S.1    Hong, F.2    Gewirth, D.3    Guo, B.4    Liu, B.5    Li, Z.6
  • 45
    • 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., and 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
  • 46
    • 79953192555 scopus 로고    scopus 로고
    • The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum
    • Sun, Q., Ju, T., and Cummings, R. D. (2011) The transmembrane domain of the molecular chaperone Cosmc directs its localization to the endoplasmic reticulum. J. Biol. Chem. 286, 11529-11542
    • (2011) J. Biol. Chem. , vol.286 , pp. 11529-11542
    • Sun, Q.1    Ju, T.2    Cummings, R.D.3
  • 47
    • 84878986182 scopus 로고    scopus 로고
    • Specificity and regulation of the endoplasmic reticulum-associated degradation machinery
    • Merulla, J., Fasana, E., Soldà, T., and Molinari, M. (2013) Specificity and regulation of the endoplasmic reticulum-associated degradation machinery. Traffic 14, 767-777
    • (2013) Traffic , vol.14 , pp. 767-777
    • Merulla, J.1    Fasana, E.2    Soldà, T.3    Molinari, M.4
  • 48
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • Frydman, J., and Hartl, F. U. (1996) Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science 272, 1497-1502
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F.U.2
  • 49
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • Siegers, K., Waldmann, T., Leroux, M. R., Grein, K., Shevchenko, A., Schiebel, E., and Hartl, F. U. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18, 75-84
    • (1999) EMBO J. , vol.18 , pp. 75-84
    • Siegers, K.1    Waldmann, T.2    Leroux, M.R.3    Grein, K.4    Shevchenko, A.5    Schiebel, E.6    Hartl, F.U.7
  • 50
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • Thulasiraman, V., Yang, C. F., and Frydman, J. (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J. 18, 85-95
    • (1999) EMBO J. , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 55
    • 84873703055 scopus 로고    scopus 로고
    • COSMC is overexpressed in proliferating infantile hemangioma and enhances endothelial cell growth via VEGFR2
    • Lee, J., Jr., Chen, C. H., Chen, Y. H., Huang, M. J., Huang, J., Hung, J. S., Chen, M. T., and Huang, M. C. (2013) COSMC is overexpressed in proliferating infantile hemangioma and enhances endothelial cell growth via VEGFR2. PLoS One 8, e56211
    • (2013) PLoS One , vol.8
    • Lee, Jr.J.1    Chen, C.H.2    Chen, Y.H.3    Huang, M.J.4    Huang, J.5    Hung, J.S.6    Chen, M.T.7    Huang, M.C.8
  • 57
    • 84880962090 scopus 로고    scopus 로고
    • Mucin-type O-glycans and their roles in intestinal homeostasis
    • Bergstrom, K. S., and Xia, L. (2013) Mucin-type O-glycans and their roles in intestinal homeostasis. Glycobiology 23, 1026-1037
    • (2013) Glycobiology , vol.23 , pp. 1026-1037
    • Bergstrom, K.S.1    Xia, L.2
  • 59
    • 0031040995 scopus 로고    scopus 로고
    • Golgi localization of glycosyltransferases: More questions than answers
    • Colley, K. J. (1997) Golgi localization of glycosyltransferases: More questions than answers. Glycobiology 7, 1-13
    • (1997) Glycobiology , vol.7 , pp. 1-13
    • Colley, K.J.1
  • 61
    • 0033431697 scopus 로고    scopus 로고
    • The relationship between ST6Gal i Golgi retention and its cleavage- secretion
    • Kitazume-Kawaguchi, S., Dohmae, N., Takio, K., Tsuji, S., and Colley, K. J. (1999) The relationship between ST6Gal I Golgi retention and its cleavage- secretion. Glycobiology 9, 1397-1406
    • (1999) Glycobiology , vol.9 , pp. 1397-1406
    • Kitazume-Kawaguchi, S.1    Dohmae, N.2    Takio, K.3    Tsuji, S.4    Colley, K.J.5
  • 63
    • 0031584217 scopus 로고    scopus 로고
    • A soluble form of α1,3-galactosyltransferase functions within cells to galactosylate glycoproteins
    • Cho, S. K., and Cummings, R. D. (1997) A soluble form of α1,3-galactosyltransferase functions within cells to galactosylate glycoproteins. J. Biol. Chem. 272, 13622-13628
    • (1997) J. Biol. Chem. , vol.272 , pp. 13622-13628
    • Cho, S.K.1    Cummings, R.D.2
  • 64
    • 0043071534 scopus 로고    scopus 로고
    • The N-terminal stem region of bovine and human β1,4- galactosyltransferase i increases the in vitro folding efficiency of their catalytic domain from inclusion bodies
    • Boeggeman, E. E., Ramakrishnan, B., and Qasba, P. K. (2003) The N-terminal stem region of bovine and human β1,4-galactosyltransferase I increases the in vitro folding efficiency of their catalytic domain from inclusion bodies. Protein Expr. Purif. 30, 219-229
    • (2003) Protein Expr. Purif. , vol.30 , pp. 219-229
    • Boeggeman, E.E.1    Ramakrishnan, B.2    Qasba, P.K.3
  • 65
    • 82255191912 scopus 로고    scopus 로고
    • "Add-on" domains of Drosophila β1,4-N- acetylgalactosaminyltransferase B in the stem region and its pilot protein
    • Kraft, B., Johswich, A., Kauczor, G., Scharenberg, M., Gerardy-Schahn, R., and Bakker, H. (2011) "Add-on" domains of Drosophila β1,4-N-acetylgalactosaminyltransferase B in the stem region and its pilot protein. Cell Mol. Life Sci. 68, 4091-4100
    • (2011) Cell Mol. Life Sci. , vol.68 , pp. 4091-4100
    • Kraft, B.1    Johswich, A.2    Kauczor, G.3    Scharenberg, M.4    Gerardy-Schahn, R.5    Bakker, H.6
  • 66
    • 59849114984 scopus 로고    scopus 로고
    • Golgi targeting of Drosophila melanogaster β4GalNAcTB requires a DHHC protein family-related protein as a pilot
    • Johswich, A., Kraft, B., Wuhrer, M., Berger, M., Deelder, A. M., Hokke, C. H., Gerardy-Schahn, R., and Bakker, H. (2009) Golgi targeting of Drosophila melanogaster β4GalNAcTB requires a DHHC protein family-related protein as a pilot. J. Cell Biol. 184, 173-183
    • (2009) J. Cell Biol. , vol.184 , pp. 173-183
    • Johswich, A.1    Kraft, B.2    Wuhrer, M.3    Berger, M.4    Deelder, A.M.5    Hokke, C.H.6    Gerardy-Schahn, R.7    Bakker, H.8
  • 67
    • 33748702275 scopus 로고    scopus 로고
    • Identification of core 1 O-glycan T-synthase from Caenorhabditis elegans
    • Ju, T., Zheng, Q., and Cummings, R. D. (2006) Identification of core 1 O-glycan T-synthase from Caenorhabditis elegans. Glycobiology 16, 947-958
    • (2006) Glycobiology , vol.16 , pp. 947-958
    • Ju, T.1    Zheng, Q.2    Cummings, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.