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Volumn 56, Issue 7-8, 1999, Pages 670-682

Hyaluronan synthases: Fascinating glycosyltransferases from vertebrates, bacterial pathogens, and algal viruses

Author keywords

Enzymology; Glycosyltransferase; Hyaluronan; Hyaluronan synthase; Hyaluronate; Hyaluronic acid; Membrane proteins; Polysaccharide

Indexed keywords

BACTERIAL ENZYME; GLYCOSYLTRANSFERASE; HYALURONIC ACID; MEMBRANE ENZYME; SYNTHETASE; VIRUS ENZYME;

EID: 0032754629     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050461     Document Type: Review
Times cited : (172)

References (71)
  • 1
    • 0001413280 scopus 로고
    • The polysaccharide of the vitreous humor
    • 1 Meyer K. and Palmer J. W. (1934) The polysaccharide of the vitreous humor. J. Biol. Chem. 107: 629-634
    • (1934) J. Biol. Chem. , vol.107 , pp. 629-634
    • Meyer, K.1    Palmer, J.W.2
  • 3
  • 4
    • 0027504082 scopus 로고
    • Hyaluronan-binding proteins in development, tissue homeostasis, and disease
    • 4 Knudson C. B. and Knudson W. (1993) Hyaluronan-binding proteins in development, tissue homeostasis, and disease. FASEB J. 7: 1233-1241
    • (1993) FASEB J. , vol.7 , pp. 1233-1241
    • Knudson, C.B.1    Knudson, W.2
  • 5
    • 0002915419 scopus 로고
    • Proteoglycans and hyaluronan in morphogenesis and differentiation
    • Hay E. D. (ed.), Plenum, New York
    • 5 Toole B. P. (1991) Proteoglycans and hyaluronan in morphogenesis and differentiation. In: Cell Biology of the Extracellular Matrix, pp. 305-341, Hay E. D. (ed.), Plenum, New York
    • (1991) Cell Biology of the Extracellular Matrix , pp. 305-341
    • Toole B, P.1
  • 6
    • 0028297463 scopus 로고
    • Hyaluronic acid: A review of its pharmacology and use as a surgical aid in ophthamology and its therapeutic potential in joint disease and wound healing
    • 6 Goa K. L. and Benfield P. (1994) Hyaluronic acid: a review of its pharmacology and use as a surgical aid in ophthamology and its therapeutic potential in joint disease and wound healing. Drugs 47: 536-566
    • (1994) Drugs , vol.47 , pp. 536-566
    • Goa, K.L.1    Benfield, P.2
  • 7
    • 33746385042 scopus 로고
    • The role of the mucoid polysaccharide (hyaluronic acid) in the virulence of group a streptococci
    • 7 Kass E. H. and Seastone C. V. (1944) The role of the mucoid polysaccharide (hyaluronic acid) in the virulence of group A streptococci. J. Exp. Med. 79: 319-330
    • (1944) J. Exp. Med. , vol.79 , pp. 319-330
    • Kass, E.H.1    Seastone, C.V.2
  • 8
    • 0001339476 scopus 로고
    • Isolation of capsular polysaccharides from colonial variants of Pasteurella multocida
    • 8 Carter G. R. and Annau E. (1953) Isolation of capsular polysaccharides from colonial variants of Pasteurella multocida. Am. J. Vet. Res. 14: 475-478
    • (1953) Am. J. Vet. Res. , vol.14 , pp. 475-478
    • Carter, G.R.1    Annau, E.2
  • 10
    • 0019429611 scopus 로고
    • HA capsule prevents attachment of group A streptococci to mouse peritoneal macrophages
    • 10 Whitnack E., Bisno A. L. and Beachey E. H. (1981) HA capsule prevents attachment of group A streptococci to mouse peritoneal macrophages. Infect. Immun. 31: 985-991
    • (1981) Infect. Immun. , vol.31 , pp. 985-991
    • Whitnack, E.1    Bisno, A.L.2    Beachey, E.H.3
  • 11
    • 0026228030 scopus 로고
    • Resistance of Pasteurella multocida A:3,4 to phagocytosis by turkey macrophages and heterophils
    • 11 Harmon B. G., Glisson J. R., Latimer K. S., Steffens W. L. and Nunnally J. C. (1991) Resistance of Pasteurella multocida A:3,4 to phagocytosis by turkey macrophages and heterophils. Am. J. Vet. Res. 52: 1507-1511
    • (1991) Am. J. Vet. Res. , vol.52 , pp. 1507-1511
    • Harmon, B.G.1    Glisson, J.R.2    Latimer, K.S.3    Steffens, W.L.4    Nunnally, J.C.5
  • 12
  • 13
    • 0033046715 scopus 로고    scopus 로고
    • Enhanced adhesion of Pasteurella multocida to cultured turkey peripheral blood monocytes
    • 13 Pruimboom I. M., Rimler R. B. and Ackermann M. R. (1999) Enhanced adhesion of Pasteurella multocida to cultured turkey peripheral blood monocytes. Infect. Immun. 67: 1292-1296
    • (1999) Infect. Immun. , vol.67 , pp. 1292-1296
    • Pruimboom, I.M.1    Rimler, R.B.2    Ackermann, M.R.3
  • 14
    • 0030909888 scopus 로고    scopus 로고
    • Role of putative virulence factors of Streptococcus pyogenes in mouse models of long-term throat colonization and pneumonia
    • 14 Husmann L. K., Yung D. L., Hollingshead S. K. and Scott J. R. (1997) Role of putative virulence factors of Streptococcus pyogenes in mouse models of long-term throat colonization and pneumonia. Infect. Immun. 65: 1422-1430
    • (1997) Infect. Immun. , vol.65 , pp. 1422-1430
    • Husmann, L.K.1    Yung, D.L.2    Hollingshead, S.K.3    Scott, J.R.4
  • 17
    • 0021998673 scopus 로고
    • Mechanisms of chain initiation in the biosynthesis of connective tissue polysaccharides
    • 17 Roden L., Koerner T., Olson C. and Schwartz N. B. (1985) Mechanisms of chain initiation in the biosynthesis of connective tissue polysaccharides. Fed. Proc. 44: 373-380
    • (1985) Fed. Proc. , vol.44 , pp. 373-380
    • Roden, L.1    Koerner, T.2    Olson, C.3    Schwartz N, B.4
  • 18
    • 0000736863 scopus 로고
    • The enzymatic synthesis in vitro of hyaluronic acid chains
    • 18 Glaser L. and Brown D. H. (1955) The enzymatic synthesis in vitro of hyaluronic acid chains. Proc. Natl. Acad. Sci. USA 41: 253-260
    • (1955) Proc. Natl. Acad. Sci. USA , vol.41 , pp. 253-260
    • Glaser, L.1    Brown, D.H.2
  • 19
    • 0009521481 scopus 로고
    • The biosynthesis of HA by cell-free extracts of group A Streptococcus
    • 19 Markovitz A., Cifonelli J. A. and Dorfman A. (1958) The biosynthesis of HA by cell-free extracts of group A Streptococcus. Biochim. Biophys. Acta. 28: 453-455
    • (1958) Biochim. Biophys. Acta. , vol.28 , pp. 453-455
    • Markovitz, A.1    Cifonelli, J.A.2    Dorfman, A.3
  • 20
    • 70449272440 scopus 로고
    • The biosynthesis of HA by group A Streptococcus. VI. Biosynthesis from uridine nucleotides in cell-free extracts
    • 20 Markovitz A., Cifonelli J. A. and Dorfman A. (1959) The biosynthesis of HA by group A Streptococcus. VI. Biosynthesis from uridine nucleotides in cell-free extracts. J. Biol. Chem. 234: 2343-2350
    • (1959) J. Biol. Chem. , vol.234 , pp. 2343-2350
    • Markovitz, A.1    Cifonelli, J.A.2    Dorfman, A.3
  • 21
    • 0014689848 scopus 로고
    • The biosynthesis of hyaluronic acid by Streptococcus
    • 21 Stoolmiller A. C. and Dorfman A. (1969) The biosynthesis of hyaluronic acid by Streptococcus J. Biol. Chem. 244: 236-246
    • (1969) J. Biol. Chem. , vol.244 , pp. 236-246
    • Stoolmiller, A.C.1    Dorfman, A.2
  • 22
    • 0018609266 scopus 로고
    • Biosynthesis of hyaluronic acid by Streptococcus
    • 22 Sugahara K., Schwartz N. B. and Dorfman A. (1979) Biosynthesis of hyaluronic acid by Streptococcus. J. Biol. Chem. 254: 6252-6261
    • (1979) J. Biol. Chem. , vol.254 , pp. 6252-6261
    • Sugahara, K.1    Schwartz, N.B.2    Dorfman, A.3
  • 23
    • 0018611540 scopus 로고
    • Cell-free synthesis of hyaluronic acid in Marfan syndrome
    • 23 Appel A., Horwitz A. L. and Dorfman A. (1979) Cell-free synthesis of hyaluronic acid in Marfan syndrome. J. Biol. Chem. 254: 12199-12203
    • (1979) J. Biol. Chem. , vol.254 , pp. 12199-12203
    • Appel, A.1    Horwitz, A.L.2    Dorfman, A.3
  • 24
    • 0022313228 scopus 로고
    • Effect of hyaluronidase treatment of intact cells on hyaluronate synthetase activity
    • 24 Philipson L. H., Westley J. and Schwartz N. B. (1985) Effect of hyaluronidase treatment of intact cells on hyaluronate synthetase activity. Biochemistry 24: 899-906
    • (1985) Biochemistry , vol.24 , pp. 899-906
    • Philipson, L.H.1    Westley, J.2    Schwartz, N.B.3
  • 25
    • 0020966422 scopus 로고
    • Synthesis of hyaluronate in differentiated teratocarcinoma cells: Characterization of the synthase
    • 25 Prehm P. (1983) Synthesis of hyaluronate in differentiated teratocarcinoma cells: characterization of the synthase. Biochem J. 211: 181-189
    • (1983) Biochem J. , vol.211 , pp. 181-189
    • Prehm, P.1
  • 26
    • 0021325058 scopus 로고
    • Subcellular localization of hyaluronate synthetase in oligodendroglioma cells
    • 26 Philipson L. H. and Schwartz N. B. (1984) Subcellular localization of hyaluronate synthetase in oligodendroglioma cells. J. Biol. Chem. 259: 5017-5023
    • (1984) J. Biol. Chem. , vol.259 , pp. 5017-5023
    • Philipson, L.H.1    Schwartz, N.B.2
  • 27
    • 0032566738 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes
    • 27 Spicer A. P., Kaback L. A., Smith T. J. and Seldin M. F. (1998) Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes. J. Biol. Chem. 273: 25117-25124
    • (1998) J. Biol. Chem. , vol.273 , pp. 25117-25124
    • Spicer, A.P.1    Kaback, L.A.2    Smith, T.J.3    Seldin, M.F.4
  • 28
    • 0029774397 scopus 로고    scopus 로고
    • Enzymological characterization of the Pasteurella multocida hyaluronic acid synthase
    • 28 DeAngelis P. L. (1996) Enzymological characterization of the Pasteurella multocida hyaluronic acid synthase. Biochemistry 35: 9768-9771
    • (1996) Biochemistry , vol.35 , pp. 9768-9771
    • DeAngelis, P.L.1
  • 29
    • 0028059074 scopus 로고
    • Immunochemical confirmation of the primary structure of streptococcal hyaluronan synthase and synthesis of high molecular weight product by recombinant enzyme
    • 29 DeAngelis P. L. and Weigel P. H. (1994) Immunochemical confirmation of the primary structure of streptococcal hyaluronan synthase and synthesis of high molecular weight product by recombinant enzyme. Biochemistry 33: 9033-9039
    • (1994) Biochemistry , vol.33 , pp. 9033-9039
    • DeAngelis, P.L.1    Weigel, P.H.2
  • 30
    • 0032570558 scopus 로고    scopus 로고
    • Enzymological characterization of recombinant Xenopus DG42, a vertebrate hyaluronan synthase
    • 30 Pummill P. E., Achyuthan A. M. and DeAngelis P. L. (1998) Enzymological characterization of recombinant Xenopus DG42, a vertebrate hyaluronan synthase. J. Biol. Chem. 273: 4976-4981
    • (1998) J. Biol. Chem. , vol.273 , pp. 4976-4981
    • Pummill, P.E.1    Achyuthan, A.M.2    DeAngelis, P.L.3
  • 31
    • 0022527301 scopus 로고
    • Isolation of streptococcal HA synthase
    • 31 Prehm P. and Mausolf A. (1986) Isolation of streptococcal HA synthase. Biochem. J. 235: 887-889
    • (1986) Biochem. J. , vol.235 , pp. 887-889
    • Prehm, P.1    Mausolf, A.2
  • 32
    • 0027414284 scopus 로고
    • The hyaluronate synthase from a eukaryotic cell line
    • 32 Klewes L., Turley E. A. and Prehm P. (1993) The hyaluronate synthase from a eukaryotic cell line. Biochem. J. 290: 791-795
    • (1993) Biochem. J. , vol.290 , pp. 791-795
    • Klewes, L.1    Turley, E.A.2    Prehm, P.3
  • 33
    • 0026448218 scopus 로고
    • Analysis of the streptococcal HA synthase complex using the photoaffinity probe 5-azido-UDP-GlcA
    • 33 Rijn I. van de and Drake R. R. (1992) Analysis of the streptococcal HA synthase complex using the photoaffinity probe 5-azido-UDP-GlcA. J. Biol. Chem. 267: 24302-24306
    • (1992) J. Biol. Chem. , vol.267 , pp. 24302-24306
    • Van De Rijn, I.1    Drake, R.R.2
  • 34
    • 0022558911 scopus 로고
    • Characterization of a high-Mr plasma-membrane-bound protein and assessment of its role as a constituent of hyaluronate synthase complex
    • 34 Mian N. (1986) Characterization of a high-Mr plasma-membrane-bound protein and assessment of its role as a constituent of hyaluronate synthase complex. Biochem. J. 237: 343-357
    • (1986) Biochem. J. , vol.237 , pp. 343-357
    • Mian, N.1
  • 36
    • 0027320534 scopus 로고
    • Isolation of a Streptococcus pyogenes gene locus that directs hyaluronan biosynthesis in acapsular mutants and in heterologous bacteria
    • 36 DeAngelis P. L., Papaconstantinou J. and Weigel P. H. (1993) Isolation of a Streptococcus pyogenes gene locus that directs hyaluronan biosynthesis in acapsular mutants and in heterologous bacteria. J. Biol. Chem. 268: 14568-14571
    • (1993) J. Biol. Chem. , vol.268 , pp. 14568-14571
    • DeAngelis, P.L.1    Papaconstantinou, J.2    Weigel, P.H.3
  • 37
    • 0027184101 scopus 로고
    • Molecular cloning, identification, and sequence of the hyaluronan synthase gene from group A Streptococcus pyogenes
    • 37 DeAngelis P. L., Papaconstantinou J. and Weigel P. H. (1993) Molecular cloning, identification, and sequence of the hyaluronan synthase gene from group A Streptococcus pyogenes. J. Biol. Chem. 268: 19181-19184
    • (1993) J. Biol. Chem. , vol.268 , pp. 19181-19184
    • DeAngelis, P.L.1    Papaconstantinou, J.2    Weigel, P.H.3
  • 38
    • 0028032079 scopus 로고
    • Molecular characterization of hasA from an operon required for hyaluronic acid synthesis in group A streptococci
    • 38 Dougherty B. A. and Rijn I. van de (1994) Molecular characterization of hasA from an operon required for hyaluronic acid synthesis in group A streptococci. J. Biol. Chem. 269: 169-175
    • (1994) J. Biol. Chem. , vol.269 , pp. 169-175
    • Dougherty, B.A.1    Van De Rijn, I.2
  • 39
    • 0032478626 scopus 로고    scopus 로고
    • Identification and molecular cloning of a unique hyaluronan synthase from Pasteurella multocida
    • 39 DeAngelis P. L., Jing W., Drake R. R. and Achyuthan A. M. (1998) Identification and molecular cloning of a unique hyaluronan synthase from Pasteurella multocida. J. Biol. Chem. 273: 8454-8458
    • (1998) J. Biol. Chem. , vol.273 , pp. 8454-8458
    • DeAngelis, P.L.1    Jing, W.2    Drake, R.R.3    Achyuthan, A.M.4
  • 40
    • 0028362752 scopus 로고
    • The Streptococcus pyogenes hyaluronan synthase: Sequence comparison and conservation among various group A strains
    • 40 DeAngelis P. L., Yang N. and Weigel P. H. (1994) The Streptococcus pyogenes hyaluronan synthase: sequence comparison and conservation among various group A strains. Biochem. Biophys. Res. Commun. 199: 1-10
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 1-10
    • DeAngelis, P.L.1    Yang, N.2    Weigel, P.H.3
  • 41
    • 0023792770 scopus 로고
    • Accumulation and decay of DG42 gene products follow a gradient pattern during Xenopus embryogenesis
    • 41 Rosa F., Sargent T. D., Rebbert M. L., Michaels G. S., Jamrich M., Grunz H. et al. (1988) Accumulation and decay of DG42 gene products follow a gradient pattern during Xenopus embryogenesis. Dev. Biol. 129: 114-123
    • (1988) Dev. Biol. , vol.129 , pp. 114-123
    • Rosa, F.1    Sargent T, D.2    Rebbert, M.L.3    Michaels, G.S.4    Jamrich, M.5    Grunz, H.6
  • 42
    • 0029955223 scopus 로고    scopus 로고
    • Cells expressing the DG42 gene from early Xenopus embryos synthesize hyaluronan
    • 42 Meyer M. F. and Kreil G. (1996) Cells expressing the DG42 gene from early Xenopus embryos synthesize hyaluronan. Proc. Natl. Acad. Sci. USA 93: 4543-4547
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4543-4547
    • Meyer, M.F.1    Kreil, G.2
  • 43
    • 0029796367 scopus 로고    scopus 로고
    • Yeast-derived recombinant DG42 protein of Xenopux can synthesize hyaluronan in vitro
    • 43 DeAngelis P. L. and Achyuthan A. M. (1996) Yeast-derived recombinant DG42 protein of Xenopux can synthesize hyaluronan in vitro. J. Biol. Chem. 271: 23657-23660
    • (1996) J. Biol. Chem. , vol.271 , pp. 23657-23660
    • DeAngelis, P.L.1    Achyuthan, A.M.2
  • 44
    • 0030001849 scopus 로고    scopus 로고
    • Expression cloning and molecular characterization of HAS protein, a cukaryotic hyaluronan synthase
    • 44 Itano N. and Kimata K. (1996) Expression cloning and molecular characterization of HAS protein, a cukaryotic hyaluronan synthase. J. Biol. Chem. 271: 9875-9878
    • (1996) J. Biol. Chem. , vol.271 , pp. 9875-9878
    • Itano, N.1    Kimata, K.2
  • 46
    • 0029809885 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a putative mouse hyaluronan synthase
    • 46 Spicer A. P., Augustine M. L. and McDonald J. A. (1996) Molecular cloning and characterization of a putative mouse hyaluronan synthase. J. Biol. Chem. 271: 23400-23406
    • (1996) J. Biol. Chem. , vol.271 , pp. 23400-23406
    • Spicer, A.P.1    Augustine, M.L.2    McDonald, J.A.3
  • 47
    • 0029836238 scopus 로고    scopus 로고
    • Molecular identification of a putative human hyaluronan synthase
    • 47 Watanabe K. and Yamaguchi Y. (1996) Molecular identification of a putative human hyaluronan synthase. J. Biol. Chem. 271: 22945-22948
    • (1996) J. Biol. Chem. , vol.271 , pp. 22945-22948
    • Watanabe, K.1    Yamaguchi, Y.2
  • 48
    • 0030938092 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding the third putative mammalian hyaluronan synthase
    • 48 Spicer A. P., Olson J. S. and McDonald J. A. (1997) Molecular cloning and characterization of a cDNA encoding the third putative mammalian hyaluronan synthase. J. Biol. Chem. 272: 8957-8961
    • (1997) J. Biol. Chem. , vol.272 , pp. 8957-8961
    • Spicer, A.P.1    Olson, J.S.2    McDonald, J.A.3
  • 49
    • 0031453134 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of the authentic hyaluronan synthase from group C Streptococcus equisimilis
    • 49 Kumari K. and Weigel P. H. (1997) Molecular cloning, expression, and characterization of the authentic hyaluronan synthase from group C Streptococcus equisimilis. J. Biol. Chem. 272: 32539-32546
    • (1997) J. Biol. Chem. , vol.272 , pp. 32539-32546
    • Kumari, K.1    Weigel, P.H.2
  • 51
    • 0026510117 scopus 로고
    • Immunohistochemical localization of HA synthase in cornea and conjunctiva of cynomolgus monkey
    • 51 Rittig M., Lutjendrecoll E. and Prehm P. (1992) Immunohistochemical localization of HA synthase in cornea and conjunctiva of cynomolgus monkey. Exp. Eye Res. 54: 455-460
    • (1992) Exp. Eye Res. , vol.54 , pp. 455-460
    • Rittig, M.1    Lutjendrecoll, E.2    Prehm, P.3
  • 52
  • 53
    • 0028071427 scopus 로고
    • Intracellular signal transduction for serum activation of the hyaluronan synthase in eukaryotic cell lines
    • 53 Klewes L. and Prehm P. (1994) Intracellular signal transduction for serum activation of the hyaluronan synthase in eukaryotic cell lines. J. Cell. Physiol. 160: 539-544
    • (1994) J. Cell. Physiol. , vol.160 , pp. 539-544
    • Klewes, L.1    Prehm, P.2
  • 54
    • 0032566906 scopus 로고    scopus 로고
    • Chlorella virus PBCV-I encodes functional glutamine:Fructose-6-phosphate amidotransferase and UDP-glucose dehydrogenase enzymes
    • 54 Landstein D., Graves M. V., Burbank D. E., DeAngelis P. and Van Etten J. L. (1998) Chlorella virus PBCV-I encodes functional glutamine:fructose-6-phosphate amidotransferase and UDP-glucose dehydrogenase enzymes. Virology 250: 388-396
    • (1998) Virology , vol.250 , pp. 388-396
    • Landstein, D.1    Graves, M.V.2    Burbank, D.E.3    DeAngelis, P.4    Van Etten, J.L.5
  • 55
    • 0033543684 scopus 로고    scopus 로고
    • Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase
    • 55 DeAngelis P. L. (1999) Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase. J. Biol. Chem. 274: 26557-26562
    • (1999) J. Biol. Chem. , vol.274 , pp. 26557-26562
    • DeAngelis, P.L.1
  • 56
    • 0009488982 scopus 로고    scopus 로고
    • Topological and functional studies of the streptococcal hyaluronan synthase
    • 56 Heldermon C., Tlapak-Simmons V. L., DeAngelis P. L. and Weigel P. H. (1996) Topological and functional studies of the streptococcal hyaluronan synthase. Glycobiology 6: 741
    • (1996) Glycobiology , vol.6 , pp. 741
    • Heldermon, C.1    Tlapak-Simmons, V.L.2    DeAngelis, P.L.3    Weigel, P.H.4
  • 57
    • 0024338028 scopus 로고
    • Radiation inactivation of membrane components and molecular weight determination by target analysis
    • 57 Kempner E. S. and Fleischer S. (1989) Radiation inactivation of membrane components and molecular weight determination by target analysis. Methods Enzymol. 172: 410-439
    • (1989) Methods Enzymol. , vol.172 , pp. 410-439
    • Kempner, E.S.1    Fleischer, S.2
  • 58
    • 0032476034 scopus 로고    scopus 로고
    • The active streptococcal hyaluronan synthases (HASs) contain a single HAS monomer and multiple cardiolipin molecules
    • 58 Tlapak-Simmons V. L., Kempner E. S., Baggenstoss B. A. and Weigel P. H. (1998) The active streptococcal hyaluronan synthases (HASs) contain a single HAS monomer and multiple cardiolipin molecules. J. Biol. Chem. 273: 26100-26109
    • (1998) J. Biol. Chem. , vol.273 , pp. 26100-26109
    • Tlapak-Simmons, V.L.1    Kempner, E.S.2    Baggenstoss, B.A.3    Weigel, P.H.4
  • 60
    • 0020966423 scopus 로고
    • Synthesis of hyaluronate in differentiated teratocarcinoma cells: Mechanism of chain growth
    • 60 Prehm P. (1983) Synthesis of hyaluronate in differentiated teratocarcinoma cells: mechanism of chain growth. Biochem. J. 211: 191-198
    • (1983) Biochem. J. , vol.211 , pp. 191-198
    • Prehm, P.1
  • 61
    • 0028985614 scopus 로고
    • Synthesis of 'Nod'-like chitin oligosaccharides by the Xenopus developmental protein DG42
    • 61 Semino C. E. and Robbins P. W. (1995) Synthesis of 'Nod'-like chitin oligosaccharides by the Xenopus developmental protein DG42. Proc. Natl. Acad. Sci. USA 92: 3498-3501
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3498-3501
    • Semino, C.E.1    Robbins, P.W.2
  • 62
    • 0029900197 scopus 로고    scopus 로고
    • Homologs of the Xenopus developmental gene DG42 are present in zebralish and mouse and are involved in the synthesis of Nod-like chitin oligosaccharides during early embryogenesis
    • 62 Semino C. E., Specht C. A., Raimondi A. and Robbins P. W. (1996) Homologs of the Xenopus developmental gene DG42 are present in zebralish and mouse and are involved in the synthesis of Nod-like chitin oligosaccharides during early embryogenesis. Proc. Natl. Acad. Sci. USA 93: 4548-4553
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4548-4553
    • Semino, C.E.1    Specht, C.A.2    Raimondi, A.3    Robbins, P.W.4
  • 63
    • 0030750573 scopus 로고    scopus 로고
    • Parallel-up structure evidences the molecular directionality during biosynthesis of bacterial cellulose
    • 63 Koyama M., Helbert W., Imai T., Sugiyama J. and Henrissat B. (1997) Parallel-up structure evidences the molecular directionality during biosynthesis of bacterial cellulose. Proc. Natl. Acad. Sci. USA 94: 9091-9095
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9091-9095
    • Koyama, M.1    Helbert, W.2    Imai, T.3    Sugiyama, J.4    Henrissat, B.5
  • 64
    • 0028986927 scopus 로고
    • Multidomain architecture of beta-glcosyl transferases: Implications for mechanism of action
    • 64 Saxena I. M., Brown R. M. Jr, Fevre M., Geremia R. A. and Henrissat B. (1995) Multidomain architecture of beta-glcosyl transferases: implications for mechanism of action. J. Bacteriol. 177: 1419-1424
    • (1995) J. Bacteriol. , vol.177 , pp. 1419-1424
    • Saxena, I.M.1    Brown R.M., Jr.2    Fevre, M.3    Geremia, R.A.4    Henrissat, B.5
  • 65
    • 0000216230 scopus 로고
    • Structure and metabolism of connective tissue proteoglycans
    • Lennarz W. J. (ed.), Plenum, New York
    • 65 Roden L. (1980) Structure and metabolism of connective tissue proteoglycans. In: The Biochemistry of Glycoproteins and Proteoglycans, pp. 267-371. Lennarz W. J. (ed.), Plenum, New York
    • (1980) The Biochemistry of Glycoproteins and Proteoglycans , pp. 267-371
    • Roden, L.1
  • 66
    • 0033548093 scopus 로고    scopus 로고
    • Kinetic characterization of the recombinant hyaluronan synthases from Streptococcus pyogenes and Streptococcus equisimilis
    • 66 Tlapak-Simmons V. L., Baggenstoss B. A., Kumari K., Heldermon C. and Weigel P. H. (1999) Kinetic characterization of the recombinant hyaluronan synthases from Streptococcus pyogenes and Streptococcus equisimilis. J. Biol. Chem. 274: 4246-4253
    • (1999) J. Biol. Chem. , vol.274 , pp. 4246-4253
    • Tlapak-Simmons, V.L.1    Baggenstoss, B.A.2    Kumari, K.3    Heldermon, C.4    Weigel, P.H.5
  • 67
    • 0031939945 scopus 로고    scopus 로고
    • Characterization and molecular evolution of a vertebrate hyaluronan synthase gene family
    • 67 Spicer A. P. and McDonald J. A. (1998) Characterization and molecular evolution of a vertebrate hyaluronan synthase gene family. J. Biol. Chem. 273: 1923-1932
    • (1998) J. Biol. Chem. , vol.273 , pp. 1923-1932
    • Spicer, A.P.1    McDonald, J.A.2
  • 68
    • 0023033143 scopus 로고
    • Solubilization of hyaluronic acid synthetic activity from streptococci and its activation with phospholipids
    • 68 Triscott M. X. and Rijn I. van de (1986) Solubilization of hyaluronic acid synthetic activity from streptococci and its activation with phospholipids. J. Biol. Chem. 261: 6004-6009
    • (1986) J. Biol. Chem. , vol.261 , pp. 6004-6009
    • Triscott, M.X.1    Van De Rijn, I.2
  • 69
    • 0033548172 scopus 로고    scopus 로고
    • Purification and lipid dependence of the recombinant hyaluronan synthases from Streptococcus pyogenes and Streptococcus equisimilis
    • 69 Tlapak-Simmons V. L., Baggenstoss B. A., Clyne T. and Weigel P. H. (1999) Purification and lipid dependence of the recombinant hyaluronan synthases from Streptococcus pyogenes and Streptococcus equisimilis. J. Biol. Chem. 274: 4239-4245
    • (1999) J. Biol. Chem. , vol.274 , pp. 4239-4245
    • Tlapak-Simmons, V.L.1    Baggenstoss, B.A.2    Clyne, T.3    Weigel, P.H.4
  • 70
    • 0031148588 scopus 로고    scopus 로고
    • Chromosomal localization of the human and mouse hyaluronan synthase genes
    • 70 Spicer A. P., Seldin M. F., Olsen A. S., Brown N., Wells D. E., Doggett N. A. et al. (1997) Chromosomal localization of the human and mouse hyaluronan synthase genes. Genomics 41: 493-497
    • (1997) Genomics , vol.41 , pp. 493-497
    • Spicer, A.P.1    Seldin, M.F.2    Olsen, A.S.3    Brown, N.4    Wells, D.E.5    Doggett, N.A.6
  • 71
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • 71 Corpet F. (1988) Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16: 10881-10890
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1


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