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Volumn 287, Issue 17, 2012, Pages 14040-14051

Crystal structure of N-glycosylated human glypican-1 core protein: Structure of two loops evolutionarily conserved in vertebrate glypican-1

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL DEVELOPMENT; BONE MORPHOGENETIC PROTEINS; BRAIN DEVELOPMENT; CD SPECTRA; CELL SURFACES; CHONDROITIN SULFATES; CORE PROTEINS; CYS RESIDUES; DISULFIDE BONDS; FIBROBLAST GROWTH FACTOR; GLYCOSAMINOGLYCANS; HELICAL DOMAINS; HEPARAN SULFATES; PROTEIN SPECIES; PROTEOGLYCANS; RANDOM COIL CONFORMATION; STRUCTURAL KNOWLEDGE;

EID: 84859986516     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.322487     Document Type: Article
Times cited : (52)

References (55)
  • 1
    • 33751187897 scopus 로고    scopus 로고
    • The molecular diversity of glycosaminoglycans shapes animal development
    • Bülow, H. E., and Hobert, O. (2006) The molecular diversity of glycosaminoglycans shapes animal development. Annu. Rev. Cell Dev. Biol. 22, 375-407
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 375-407
    • Bülow, H.E.1    Hobert, O.2
  • 2
    • 21744450786 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans: The sweet side of development
    • DOI 10.1038/nrm1681
    • Häcker, U., Nybakken, K., and Perrimon, N. (2005) Heparan sulfate proteoglycans. The sweet side of development. Nat. Rev. Mol. Cell Biol. 6, 530-541 (Pubitemid 40943044)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.7 , pp. 530-541
    • Hacker, U.1    Nybakken, K.2    Perrimon, N.3
  • 6
    • 70349410388 scopus 로고    scopus 로고
    • Glypican-1 controls brain size through regulation of fibroblast growth factor signaling in early neurogenesis
    • Jen, Y. H., Musacchio, M., and Lander, A. (2009) Glypican-1 controls brain size through regulation of fibroblast growth factor signaling in early neurogenesis. Neural Dev. 4, 33
    • (2009) Neural Dev. , vol.4 , pp. 33
    • Jen, Y.H.1    Musacchio, M.2    Lander, A.3
  • 7
    • 0028122383 scopus 로고
    • Amino acid determinants that drive heparan sulfate assembly in a proteoglycan
    • Zhang, L., and Esko, J. D. (1994) Amino acid determinants that drive heparan sulfate assembly in a proteoglycan. J. Biol. Chem. 269, 19295-19299 (Pubitemid 24233447)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.30 , pp. 19295-19299
    • Zhang, L.1    Esko, J.D.2
  • 8
    • 0028892362 scopus 로고
    • Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans
    • Zhang, L., David, G., and Esko, J. D. (1995) Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans. J. Biol. Chem. 270, 27127-27135
    • (1995) J. Biol. Chem. , vol.270 , pp. 27127-27135
    • Zhang, L.1    David, G.2    Esko, J.D.3
  • 9
    • 0035831531 scopus 로고    scopus 로고
    • Mechanisms underlying preferential assembly of heparan sulfate on glypican-1
    • Chen, R. L., and Lander, A. D. (2001) Mechanisms underlying preferential assembly of heparan sulfate on glypican-1. J. Biol. Chem. 276, 7507-7517
    • (2001) J. Biol. Chem. , vol.276 , pp. 7507-7517
    • Chen, R.L.1    Lander, A.D.2
  • 10
    • 77950538817 scopus 로고    scopus 로고
    • Dally-like core protein and its mammalian homologs mediate stimulatory and inhibitory effects on Hedgehog signal response
    • Williams, E. H., Pappano, W. N., Saunders, A. M., Kim, M. S., Leahy, D. J., and Beachy, P. A. (2010) Dally-like core protein and its mammalian homologs mediate stimulatory and inhibitory effects on Hedgehog signal response. Proc. Natl. Acad. Sci. U.S.A. 107, 5869-5874
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5869-5874
    • Williams, E.H.1    Pappano, W.N.2    Saunders, A.M.3    Kim, M.S.4    Leahy, D.J.5    Beachy, P.A.6
  • 11
    • 77953080875 scopus 로고    scopus 로고
    • The cell-surface proteins Dally-like and Ihog differentially regulate Hedgehog signaling strength and range during development
    • Yan, D., Wu, Y., Yang, Y., Belenkaya, T. Y., Tang, X., and Lin, X. (2010) The cell-surface proteins Dally-like and Ihog differentially regulate Hedgehog signaling strength and range during development. Development 137, 2033-2044
    • (2010) Development , vol.137 , pp. 2033-2044
    • Yan, D.1    Wu, Y.2    Yang, Y.3    Belenkaya, T.Y.4    Tang, X.5    Lin, X.6
  • 12
    • 43049097898 scopus 로고    scopus 로고
    • Glypican-3 Inhibits Hedgehog Signaling during Development by Competing with Patched for Hedgehog Binding
    • DOI 10.1016/j.devcel.2008.03.006, PII S1534580708001147
    • Capurro, M. I., Xu, P., Shi, W., Li, F., Jia, A., and Filmus, J. (2008) Glypican-3 inhibits Hedgehog signaling during development by competing with patched for Hedgehog binding. Dev. Cell 14, 700-711 (Pubitemid 351622615)
    • (2008) Developmental Cell , vol.14 , Issue.5 , pp. 700-711
    • Capurro, M.I.1    Xu, P.2    Shi, W.3    Li, F.4    Jia, A.5    Filmus, J.6
  • 13
    • 33845503275 scopus 로고    scopus 로고
    • The function of a Drosophila glypican does not depend entirely on heparan sulfate modification
    • DOI 10.1016/j.ydbio.2006.09.011, PII S0012160606012103
    • Kirkpatrick, C. A., Knox, S. M., Staatz, W. D., Fox, B., Lercher, D. M., and Selleck, S. B. (2006) The function of a Drosophila glypican does not depend entirely on heparan sulfate modification. Dev. Biol. 300, 570-582 (Pubitemid 44914138)
    • (2006) Developmental Biology , vol.300 , Issue.2 , pp. 570-582
    • Kirkpatrick, C.A.1    Knox, S.M.2    Staatz, W.D.3    Fox, B.4    Lercher, D.M.5    Selleck, S.B.6
  • 14
    • 22244480967 scopus 로고    scopus 로고
    • Glypican-3 promotes the growth of hepatocellular carcinoma by stimulating canonical Wnt signaling
    • DOI 10.1158/0008-5472.CAN-04-4244
    • Capurro, M. I., Xiang, Y. Y., Lobe, C., and Filmus, J. (2005) Glypican-3 promotes the growth of hepatocellular carcinoma by stimulating canonical Wnt signaling. Cancer Res. 65, 6245-6254 (Pubitemid 40994410)
    • (2005) Cancer Research , vol.65 , Issue.14 , pp. 6245-6254
    • Capurro, M.I.1    Xiang, Y.-Y.2    Lobe, C.3    Filmus, J.4
  • 15
    • 0038750629 scopus 로고    scopus 로고
    • Role of glypican 4 in the regulation of convergent extension movements during gastrulation in Xenopus laevis
    • DOI 10.1242/dev.00435
    • Ohkawara, B., Yamamoto, T. S., Tada, M., and Ueno, N. (2003) Role of glypican 4 in the regulation of convergent extension movements during gastrulation in Xenopus laevis. Development 130, 2129-2138 (Pubitemid 36656709)
    • (2003) Development , vol.130 , Issue.10 , pp. 2129-2138
    • Ohkawara, B.1    Yamamoto, T.S.2    Tada, M.3    Ueno, N.4
  • 16
    • 49349103711 scopus 로고    scopus 로고
    • Glypican-3-mediated oncogenesis involves the insulin-like growth factor-signaling pathway
    • Cheng, W., Tseng, C. J., Lin, T. T., Cheng, I., Pan, H. W., Hsu, H. C., and Lee, Y. M. (2008) Glypican-3-mediated oncogenesis involves the insulin-like growth factor-signaling pathway. Carcinogenesis 29, 1319-1326
    • (2008) Carcinogenesis , vol.29 , pp. 1319-1326
    • Cheng, W.1    Tseng, C.J.2    Lin, T.T.3    Cheng, I.4    Pan, H.W.5    Hsu, H.C.6    Lee, Y.M.7
  • 17
    • 70350218956 scopus 로고    scopus 로고
    • Chemical and thermal unfolding of glypican-1. Protective effect of heparan sulfate against heat-induced irreversible aggregation
    • Svensson, G., Linse, S., and Mani, K. (2009) Chemical and thermal unfolding of glypican-1. Protective effect of heparan sulfate against heat-induced irreversible aggregation. Biochemistry 48, 9994-10004
    • (2009) Biochemistry , vol.48 , pp. 9994-10004
    • Svensson, G.1    Linse, S.2    Mani, K.3
  • 18
    • 80051991015 scopus 로고    scopus 로고
    • Structure of the protein core of the glypican Dally-like and localization of a region important for hedgehog signaling
    • Kim, M. S., Saunders, A. M., Hamaoka, B. Y., Beachy, P. A., and Leahy, D. J. (2011) Structure of the protein core of the glypican Dally-like and localization of a region important for hedgehog signaling. Proc. Natl. Acad. Sci. U.S.A. 108, 13112-13117
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 13112-13117
    • Kim, M.S.1    Saunders, A.M.2    Hamaoka, B.Y.3    Beachy, P.A.4    Leahy, D.J.5
  • 19
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • Wu, H., Lustbader, J. W., Liu, Y., Canfield, R. E., and Hendrickson, W. A. (1994) Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein. Structure 2, 545-558
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 20
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment, and post-refinement
    • Kabsch, W. (2010) Integration, scaling, space-group assignment, and post-refinement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computational Project No. 4
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite. Programs for protein crystallography. Acta Crystallogr D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 24
    • 23844492576 scopus 로고    scopus 로고
    • Auto-Rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment
    • DOI 10.1107/S0907444905001307
    • Panjikar, S., Parthasarathy, V., Lamzin, V. S., Weiss, M. S., and Tucker, P. A. (2005) Auto-rickshaw. An automated crystal structure determination platform as an efficient tool for the validation of an x-ray diffraction experiment. Acta Crystallogr. D Biol. Crystallogr. 61, 449-457 (Pubitemid 43934605)
    • (2005) Acta Crystallographica Section D: Biological Crystallography , vol.61 , Issue.4 , pp. 449-457
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 25
    • 70349602499 scopus 로고    scopus 로고
    • On the combination of molecular replacement and single-wavelength anomalous diffraction phasing for automated structure determination
    • Panjikar, S., Parthasarathy, V., Lamzin, V. S., Weiss, M. S., and Tucker, P. A. (2009) On the combination of molecular replacement and single-wavelength anomalous diffraction phasing for automated structure determination. Acta Crystallogr. D Biol. Crystallogr. 65, 1089-1097
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 1089-1097
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 26
    • 0026817874 scopus 로고
    • Identification of heavy atom derivatives by normal probability methods
    • Howell, P. L., and Smith, G. D. (1992) Identification of heavy atom derivatives by normal probability methods. J. Appl. Crystallogr. 25, 81-86
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 81-86
    • Howell, P.L.1    Smith, G.D.2
  • 28
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • DOI 10.1016/S0076-6879(97)76073-7
    • de La Fortelle, E., Bricogne, G., and Carter, C. W., Jr. (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (Pubitemid 27085618)
    • (1997) Methods in Enzymology , vol.276 , pp. 472-494
    • De La, F.E.1    Bricogne, G.2
  • 29
    • 0033198415 scopus 로고    scopus 로고
    • Error estimation and bias correction in phase-improvement calculations
    • Cowtan, K. (1999) Error estimation and bias correction in phase-improvement calculations. Acta Crystallogr. D Biol. Crystallogr. 55, 1555-1567
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1555-1567
    • Cowtan, K.1
  • 32
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 33
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger, A. T. (2007) Version 1.2 of the Crystallography and NMR system. Nat. Protoc. 2, 2728-2733
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 37
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) Clustal W. Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties, and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 77954257799 scopus 로고    scopus 로고
    • Con-Surf 2010. Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) Con-Surf 2010. Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 39
    • 80055018082 scopus 로고    scopus 로고
    • The structural role of N-linked glycans on human glypican-1
    • Svensson, G., Hyrenius Wittsten, A., Linse, S., and Mani, K. (2011) The structural role of N-linked glycans on human glypican-1. Biochemistry 50, 9377-9387
    • (2011) Biochemistry , vol.50 , pp. 9377-9387
    • Svensson, G.1    Hyrenius Wittsten, A.2    Linse, S.3    Mani, K.4
  • 40
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R., and Lipman, D. J. (1988) Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. U.S.A. 85, 2444-2448
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 41
    • 0242593885 scopus 로고    scopus 로고
    • Processing by proprotein convertases is required for glypican-3 modulation of cell survival, Wnt signaling, and gastrulation movements
    • DOI 10.1083/jcb.200302152
    • De Cat, B., Muyldermans, S. Y., Coomans, C., Degeest, G., Vanderschueren, B., Creemers, J., Biemar, F., Peers, B., and David, G. (2003) Processing by proprotein convertases is required for glypican-3 modulation of cell survival, Wnt signaling, and gastrulation movements. J. Cell Biol. 163, 625-635 (Pubitemid 37429874)
    • (2003) Journal of Cell Biology , vol.163 , Issue.3 , pp. 625-635
    • De Cat, B.1    Muyldermans, S.-Y.2    Coomans, C.3    Degeest, G.4    Vanderschueren, B.5    Creemers, J.6    Biemar, F.7    Peers, B.8    David, G.9
  • 42
    • 29244465513 scopus 로고    scopus 로고
    • Processing by convertases is not required for glypican-3-induced stimulation of hepatocellular carcinoma growth
    • DOI 10.1074/jbc.M507004200
    • Capurro, M. I., Shi, W., Sandal, S., and Filmus, J. (2005) Processing by convertases is not required for glypican-3-induced stimulation of hepatocellular carcinoma growth. J. Biol. Chem. 280, 41201-41206 (Pubitemid 41832174)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41201-41206
    • Capurro, M.I.1    Shi, W.2    Sandal, S.3    Filmus, J.4
  • 43
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • DOI 10.1146/annurev.biochem.73.011303.073752
    • Helenius, A., and Aebi, M. (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73, 1019-1049 (Pubitemid 39050393)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 47
    • 79960113013 scopus 로고    scopus 로고
    • The solution structure of heparan sulfate differs from that of heparin: Implications for function
    • Khan, S., Rodriguez, E., Patel, R., Gor, J., Mulloy, B., and Perkins, S. J. (2011) The solution structure of heparan sulfate differs from that of heparin: implications for function. J. Biol. Chem. 286, 24842-24854
    • (2011) J. Biol. Chem. , vol.286 , pp. 24842-24854
    • Khan, S.1    Rodriguez, E.2    Patel, R.3    Gor, J.4    Mulloy, B.5    Perkins, S.J.6
  • 48
    • 33845927937 scopus 로고    scopus 로고
    • A conserved NXIP motif is required for cell adhesion properties of the syndecan-4 ectodomain
    • DOI 10.1074/jbc.M605553200
    • Whiteford, J. R., and Couchman, J. R. (2006) A conserved NXIP motif is required for cell adhesion properties of the syndecan-4 ectodomain. J. Biol. Chem. 281, 32156-32163 (Pubitemid 46036770)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.43 , pp. 32156-32163
    • Whiteford, J.R.1    Couchman, J.R.2
  • 49
    • 5444242206 scopus 로고    scopus 로고
    • 3 integrin activily in human mammary carcinoma cells
    • DOI 10.1083/jcb.200404171
    • Beauvais, D. M., Burbach, B. J., and Rapraeger, A. C. (2004) The syndecan-1 ectodomain regulates αvβ3 integrin activity in human mammary carcinoma cells. J. Cell Biol. 167, 171-181 (Pubitemid 39363424)
    • (2004) Journal of Cell Biology , vol.167 , Issue.1 , pp. 171-181
    • Beauvais, D.M.1    Burbach, B.J.2    Rapraeger, A.C.3
  • 50
    • 34247357022 scopus 로고    scopus 로고
    • Netrin-1/DCC signaling in commissural axon guidance requires cell-autonomous expression of heparan sulfate
    • DOI 10.1523/JNEUROSCI.0700-07.2007
    • Matsumoto, Y., Irie, F., Inatani, M., Tessier-Lavigne, M., and Yamaguchi, Y. (2007) Netrin-1/DCC signaling in commissural axon guidance requires cell-autonomous expression of heparan sulfate. J. Neurosci. 27, 4342-4350 (Pubitemid 46640711)
    • (2007) Journal of Neuroscience , vol.27 , Issue.16 , pp. 4342-4350
    • Matsumoto, Y.1    Irie, F.2    Inatani, M.3    Tessier-Lavigne, M.4    Yamaguchi, Y.5
  • 52
    • 0032500662 scopus 로고    scopus 로고
    • The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate
    • DOI 10.1074/jbc.273.41.26265
    • Lind, T., Tufaro, F., McCormick, C., Lindahl, U., and Lidholt, K. (1998) The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273, 26265-26268 (Pubitemid 28471622)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26265-26268
    • Lind, T.1    Tufaro, F.2    McCormick, C.3    Lindahl, U.4    Lidholt, K.5
  • 53
    • 0033553525 scopus 로고    scopus 로고
    • The tumor suppressor EXT-like gene EXTL2 encodes an α1,4-N- acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate
    • Kitagawa, H., Shimakawa, H., and Sugahara, K. (1999) The tumor suppressor EXT-like gene EXTL2 encodes an α1,4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. J. Biol. Chem. 274, 13933-13937
    • (1999) J. Biol. Chem. , vol.274 , pp. 13933-13937
    • Kitagawa, H.1    Shimakawa, H.2    Sugahara, K.3
  • 54
    • 0037088673 scopus 로고    scopus 로고
    • Molecular cloning and expression of human chondroitin N-acetylgalactosaminyltransferase. The key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate
    • DOI 10.1074/jbc.M111434200
    • Uyama, T., Kitagawa, H., Tamura, Ji. J., and Sugahara, K. (2002) Molecular cloning and expression of human chondroitin N- acetylgalactosaminyltransferase. The key enzyme for chain initiation and elongation of chondroitin/dermatan sulfate on the protein linkage region tetrasaccharide shared by heparin/heparan sulfate. J. Biol. Chem. 277, 8841-8846 (Pubitemid 34952951)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 8841-8846
    • Uyama, T.1    Kitagawa, H.2    Tamura, J.-I.3    Sugahara, K.4


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