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Volumn 86, Issue 5, 1996, Pages 767-775

Solution structure of the link module: A hyaluronan-binding domain involved in extracellular matrix stability and cell migration

Author keywords

[No Author keywords available]

Indexed keywords

AGGRECAN; HYALURONIC ACID;

EID: 0030572693     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80151-8     Document Type: Article
Times cited : (273)

References (66)
  • 1
    • 0006393051 scopus 로고
    • Two-dimensional spectroscopy: Application to nuclear magnetic resonance
    • Aue, W.P., Partholdi, E., and Ernst, R.R. (1976). Two-dimensional spectroscopy: application to nuclear magnetic resonance. J. Chem. Phys. 64, 2229-2246.
    • (1976) J. Chem. Phys. , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Partholdi, E.2    Ernst, R.R.3
  • 2
    • 0028173780 scopus 로고
    • Rules for α-helix termination by glycine
    • Aurora, R., Srinivasan, R., and Rose, G.D. (1994). Rules for α-helix termination by glycine. Science 264, 1126-1130.
    • (1994) Science , vol.264 , pp. 1126-1130
    • Aurora, R.1    Srinivasan, R.2    Rose, G.D.3
  • 3
    • 0023518540 scopus 로고
    • A strategy for the rapid multiple alignment of protein structures: Confidence levels from tertiary structure comparisons
    • Barton, G.J., and Sternberg, M.J.E. (1987). A strategy for the rapid multiple alignment of protein structures: confidence levels from tertiary structure comparisons. J. Mol. Biol. 198, 327-337.
    • (1987) J. Mol. Biol. , vol.198 , pp. 327-337
    • Barton, G.J.1    Sternberg, M.J.E.2
  • 4
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., and Davis, D.G. (1985). MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 5
    • 0028338551 scopus 로고
    • Link protein is ubiquitously expressed in non-cartilaginous tissues where it enhances and stabilises the interaction of proteoglycans with hyaluronic acid
    • Binette, F., Cravers, J., Kahoussie, B., Haudenschild, D., and Goetinck, P.F. (1994). Link protein is ubiquitously expressed in non-cartilaginous tissues where it enhances and stabilises the interaction of proteoglycans with hyaluronic acid. J. Biol. Chem. 269, 19116-19122.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19116-19122
    • Binette, F.1    Cravers, J.2    Kahoussie, B.3    Haudenschild, D.4    Goetinck, P.F.5
  • 7
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to protein correlation spectroscopy
    • Braunschweiler, L., and Ernst, R.R. (1983). Coherence transfer by isotropic mixing: application to protein correlation spectroscopy. J. Magn. Reson. 53, 531-538.
    • (1983) J. Magn. Reson. , vol.53 , pp. 531-538
    • Braunschweiler, L.1    Ernst, R.R.2
  • 10
    • 0017698774 scopus 로고
    • Interaction of cartilage proteoglycans with hyaluronic acid: The role of the hyaluronic acid carboxyl groups
    • Christner, J., Brown, M., and Dziewiatkowski, D.D. (1977). Interaction of cartilage proteoglycans with hyaluronic acid: the role of the hyaluronic acid carboxyl groups. Biochem. J. 167, 711-716.
    • (1977) Biochem. J. , vol.167 , pp. 711-716
    • Christner, J.1    Brown, M.2    Dziewiatkowski, D.D.3
  • 11
    • 0030221293 scopus 로고    scopus 로고
    • Overexpression, purification and refolding of Link module from human TSG-6 in Escherichia coli: Effect of temperature, media and mutagenesis on lysine misincorporation at arginine AGA codons
    • Day, A.J., Aplin, R.T., and Willis, A.C. (1996). Overexpression, purification and refolding of Link module from human TSG-6 in Escherichia coli: effect of temperature, media and mutagenesis on lysine misincorporation at arginine AGA codons. Protein Expr. Purif. 8, 1-16.
    • (1996) Protein Expr. Purif. , vol.8 , pp. 1-16
    • Day, A.J.1    Aplin, R.T.2    Willis, A.C.3
  • 12
    • 0029966274 scopus 로고    scopus 로고
    • CD44 and its ligand hyaluronate mediate rolling under physiologic flow: A novel lymphocyte-endothelial cell primary adhesion pathway
    • DeGrendele, H.C., Estess, P., Picker, L.J., and Siegelman, M.H. (1996). CD44 and its ligand hyaluronate mediate rolling under physiologic flow: a novel lymphocyte-endothelial cell primary adhesion pathway. J. Exp. Med. 183, 1119-1130.
    • (1996) J. Exp. Med. , vol.183 , pp. 1119-1130
    • DeGrendele, H.C.1    Estess, P.2    Picker, L.J.3    Siegelman, M.H.4
  • 13
    • 0023632550 scopus 로고
    • Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones
    • Doege, K., Sasaki, M., Horigan, E., Hassel, J.R., and Yamada, Y. (1987). Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones. J. Biol. Chem. 262, 17757-17767.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17757-17767
    • Doege, K.1    Sasaki, M.2    Horigan, E.3    Hassel, J.R.4    Yamada, Y.5
  • 14
    • 0025013424 scopus 로고
    • An Elisa plate based assay for hyaluronan using biotinylated proteoglycan G1 domain (HA-binding region)
    • Fosang, A.J., Hey, N.J., Carney, S.L., and Hardingham, T.E. (1990). An Elisa plate based assay for hyaluronan using biotinylated proteoglycan G1 domain (HA-binding region). Matrix 10, 306-313.
    • (1990) Matrix , vol.10 , pp. 306-313
    • Fosang, A.J.1    Hey, N.J.2    Carney, S.L.3    Hardingham, T.E.4
  • 15
    • 0023609134 scopus 로고
    • Thetandemly repeated sequences of cartilage link protein contain sitesfor interaction with hyaluronic acid
    • Goetinck, P.F., Stirpe, N.S., Tsonis, P.A., and Carlone, D. (1987). Thetandemly repeated sequences of cartilage link protein contain sitesfor interaction with hyaluronic acid. J. Cell Biol. 105, 2403-2408.
    • (1987) J. Cell Biol. , vol.105 , pp. 2403-2408
    • Goetinck, P.F.1    Stirpe, N.S.2    Tsonis, P.A.3    Carlone, D.4
  • 16
    • 0024517268 scopus 로고
    • A human lymphocyte homing receptor, the hermes antigen, is related to cartilage proteoglycan core and link proteins
    • Goldstein, L.A., Zhou, D.F.H., Picker, L.J., Minty, C.N., Bargatze, R.F., Ding, J.F., and Butcher, E.C. (1989). A human lymphocyte homing receptor, the hermes antigen, is related to cartilage proteoglycan core and link proteins. Cell 56, 1063-1072.
    • (1989) Cell , vol.56 , pp. 1063-1072
    • Goldstein, L.A.1    Zhou, D.F.H.2    Picker, L.J.3    Minty, C.N.4    Bargatze, R.F.5    Ding, J.F.6    Butcher, E.C.7
  • 18
    • 0028239180 scopus 로고
    • The expression of functional Link protein in a baculovirus system: Analysis of mutants lacking the A, B and B′ domains
    • Grover, J., and Roughley, P.J. (1994). The expression of functional Link protein in a baculovirus system: analysis of mutants lacking the A, B and B′ domains. Biochem. J. 300, 317-324.
    • (1994) Biochem. J. , vol.300 , pp. 317-324
    • Grover, J.1    Roughley, P.J.2
  • 19
    • 0026507880 scopus 로고
    • Proteoglycans: Many forms and functions
    • Hardingham, T.E., and Fosang, A.J. (1992). Proteoglycans: many forms and functions. FASEB J. 6, 861-870.
    • (1992) FASEB J. , vol.6 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 20
    • 0015719668 scopus 로고
    • Binding of oligosaccharides of hyaluronic acid to proteoglycans
    • Hardingham, T.E., and Muir, H. (1973). Binding of oligosaccharides of hyaluronic acid to proteoglycans. Biochem. J. 135, 905-908.
    • (1973) Biochem. J. , vol.135 , pp. 905-908
    • Hardingham, T.E.1    Muir, H.2
  • 21
    • 0017163510 scopus 로고
    • Cartilage proteoglycans: Structure and heterogeneity of the core protein and the effects of specific protein modification on the binding to hyaluronate
    • Hardingham, T.E., Ewins, R.J.F., and Muir, H. (1976). Cartilage proteoglycans: structure and heterogeneity of the core protein and the effects of specific protein modification on the binding to hyaluronate. Biochem. J. 157, 127-143.
    • (1976) Biochem. J. , vol.157 , pp. 127-143
    • Hardingham, T.E.1    Ewins, R.J.F.2    Muir, H.3
  • 22
    • 0027204024 scopus 로고
    • Helix stop signals in proteins and peptides: The capping box
    • Harper, E.T., and Rose, G.D. (1993). Helix stop signals in proteins and peptides: the capping box. Biochemistry 32, 7605-7609.
    • (1993) Biochemistry , vol.32 , pp. 7605-7609
    • Harper, E.T.1    Rose, G.D.2
  • 23
    • 0016221606 scopus 로고
    • Aggregation of cartilage proteoglycans: Oligosaccharide competitors of the proteoglycan-hyaluronic acid interaction
    • Hascall, V.C., and Heinegård, D. (1974). Aggregation of cartilage proteoglycans: oligosaccharide competitors of the proteoglycan-hyaluronic acid interaction. J. Biol. Chem. 249, 4242-4249.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4242-4249
    • Hascall, V.C.1    Heinegård, D.2
  • 24
    • 0028332247 scopus 로고
    • Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance
    • Hatanaka, H., Oka, M., Kohda, D., Tate, S., Suda, A., Tamiya, N., and Inagaki, F. (1994). Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance. J. Mol. Biol. 240, 155-166.
    • (1994) J. Mol. Biol. , vol.240 , pp. 155-166
    • Hatanaka, H.1    Oka, M.2    Kohda, D.3    Tate, S.4    Suda, A.5    Tamiya, N.6    Inagaki, F.7
  • 25
    • 0024435017 scopus 로고
    • CD44: A molecule involved in leukocyte adherence and T-cell activation
    • Haynes, B.F., Telen, M.J., Hale, L.P., and Denning, S.M. (1989). CD44: a molecule involved in leukocyte adherence and T-cell activation. Immunol. Today 10, 423-428.
    • (1989) Immunol. Today , vol.10 , pp. 423-428
    • Haynes, B.F.1    Telen, M.J.2    Hale, L.P.3    Denning, S.M.4
  • 26
    • 0025983894 scopus 로고
    • Measurement of an adhesion molecule as an indicator of inflammatory disease activity: Up regulation of the receptor for hyaluronate (CD44) in rheumatoid arthritis
    • Haynes, B.F., Hale, L.P., Patton, K.L., Martin, M.E., and McCallum, R.M. (1991). Measurement of an adhesion molecule as an indicator of inflammatory disease activity: up regulation of the receptor for hyaluronate (CD44) in rheumatoid arthritis. Arthritis Rheum. 34, 1434-1443.
    • (1991) Arthritis Rheum. , vol.34 , pp. 1434-1443
    • Haynes, B.F.1    Hale, L.P.2    Patton, K.L.3    Martin, M.E.4    McCallum, R.M.5
  • 27
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm, L., and Sander, C. (1994). The FSSP database of structurally aligned protein fold families. Nucl. Acids Res. 22, 3600-3609.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 28
    • 0027057526 scopus 로고
    • A database of protein structure families with common folding motifs
    • Holm, L., Ouzounis, C., Sander, C., Tuparev, G., and Vriend, G. (1992). A database of protein structure families with common folding motifs. Protein Sci. 1, 1691-1698.
    • (1992) Protein Sci. , vol.1 , pp. 1691-1698
    • Holm, L.1    Ouzounis, C.2    Sander, C.3    Tuparev, G.4    Vriend, G.5
  • 29
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Backmann, P., and Ernst, R.R. (1979). Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Backmann, P.3    Ernst, R.R.4
  • 31
    • 45149137348 scopus 로고
    • New methods for the measurement of NH-C-α-H coupling constants in N-15 labelled proteins
    • Kay, L.A., and Bax, A. (1990). New methods for the measurement of NH-C-α-H coupling constants in N-15 labelled proteins. J. Magn. Reson. 86, 110-126.
    • (1990) J. Magn. Reson. , vol.86 , pp. 110-126
    • Kay, L.A.1    Bax, A.2
  • 32
    • 0027504082 scopus 로고
    • Hyaluronan-binding proteins in development, tissue homeostasis and disease
    • 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
  • 33
    • 0029011123 scopus 로고
    • A single amino acid residue can determine the ligand specificity of E-selectin
    • Kogan, T.P., Revelle, B.M., Tapp, S., Scott, D., and Beck, P.J. (1995). A single amino acid residue can determine the ligand specificity of E-selectin. J. Biol. Chem. 270, 14047-14055.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14047-14055
    • Kogan, T.P.1    Revelle, B.M.2    Tapp, S.3    Scott, D.4    Beck, P.J.5
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0025854524 scopus 로고
    • Leukocytes roll on a selectin at physiologic flow rates: Distinction from and prerequisite for adhesion through integrins
    • Lawrence, M.B., and Springer, T.A. (1991). Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins. Cell 65, 859-873.
    • (1991) Cell , vol.65 , pp. 859-873
    • Lawrence, M.B.1    Springer, T.A.2
  • 36
    • 0026597436 scopus 로고
    • A novel secretory tumour necrosis factor-inducible protein (TSG-6) is a member of the family of hyaluronate binding proteins, closely related to the adhesion receptor CD44
    • Lee, T., Wisniewski, H.-G., and Vilcek, J. (1992). A novel secretory tumour necrosis factor-inducible protein (TSG-6) is a member of the family of hyaluronate binding proteins, closely related to the adhesion receptor CD44. J. Cell Biol. 116, 545-557.
    • (1992) J. Cell Biol. , vol.116 , pp. 545-557
    • Lee, T.1    Wisniewski, H.-G.2    Vilcek, J.3
  • 37
    • 0022525094 scopus 로고
    • Specific chemical modifications of link protein and their effect on binding to hyaluronate and cartilage proteoglycan
    • Lyon, M. (1986). Specific chemical modifications of link protein and their effect on binding to hyaluronate and cartilage proteoglycan. Biochim. Biophys. Acta 881, 22-29.
    • (1986) Biochim. Biophys. Acta , vol.881 , pp. 22-29
    • Lyon, M.1
  • 38
    • 49049150378 scopus 로고
    • Two-dimensional chemical-exchange and cross-relaxation spectroscopy of coupled nuclear spins
    • Macura, S., Huang, Y., Sueter, D., and Ernst, R.R. (1981). Two-dimensional chemical-exchange and cross-relaxation spectroscopy of coupled nuclear spins. J. Magn. Reson. 43, 259-281.
    • (1981) J. Magn. Reson. , vol.43 , pp. 259-281
    • Macura, S.1    Huang, Y.2    Sueter, D.3    Ernst, R.R.4
  • 39
    • 0029936595 scopus 로고    scopus 로고
    • TSG-6 expression in human articular chondrocytes: Possible implications in joint inflammation and cartilage degradation
    • Maier, R., Wisniewski, H.-G., Vilcek, J., and Lotz, M. (1996). TSG-6 expression in human articular chondrocytes: possible implications in joint inflammation and cartilage degradation. Arthritis Rheum. 39, 552-559.
    • (1996) Arthritis Rheum. , vol.39 , pp. 552-559
    • Maier, R.1    Wisniewski, H.-G.2    Vilcek, J.3    Lotz, M.4
  • 40
    • 0029002861 scopus 로고
    • Anti-CD44 treatment abrogates tissue oedema and leukocyte infiltration in murine arthritis
    • Mikecz, K., Brennan, F.R., Kim, J.H., and Glant, T.T. (1995). Anti-CD44 treatment abrogates tissue oedema and leukocyte infiltration in murine arthritis. Nature Med. 1, 558-563.
    • (1995) Nature Med. , vol.1 , pp. 558-563
    • Mikecz, K.1    Brennan, F.R.2    Kim, J.H.3    Glant, T.T.4
  • 41
    • 0023802130 scopus 로고
    • Cartilage proteoglycans: Assembly with hyaluronate and link protein as studied by electron microscopy
    • Morgelin, M., Paulsson, M., Hardingham, T.E., Heinegård, D., and Engel, J. (1988). Cartilage proteoglycans: assembly with hyaluronate and link protein as studied by electron microscopy. Biochem. J. 253, 175-185.
    • (1988) Biochem. J. , vol.253 , pp. 175-185
    • Morgelin, M.1    Paulsson, M.2    Hardingham, T.E.3    Heinegård, D.4    Engel, J.5
  • 42
    • 0028933622 scopus 로고
    • Evidence of a defined spatial arrangement of hyaluronate in the central filament of cartilage proteoglycan aggregates
    • Morgelin, M., Paulsson, M., Heinegård, D., Aebi, U., and Engel, J. (1995). Evidence of a defined spatial arrangement of hyaluronate in the central filament of cartilage proteoglycan aggregates. Biochem. J. 307, 595-601.
    • (1995) Biochem. J. , vol.307 , pp. 595-601
    • Morgelin, M.1    Paulsson, M.2    Heinegård, D.3    Aebi, U.4    Engel, J.5
  • 43
    • 0027284796 scopus 로고
    • The link proteins
    • Neame, P.J., and Barry, F.P. (1993). The link proteins. Experientia 49, 393-402.
    • (1993) Experientia , vol.49 , pp. 393-402
    • Neame, P.J.1    Barry, F.P.2
  • 44
    • 0023013611 scopus 로고
    • The primary structure of Link protein from rat chondrosarcoma proteoglycan aggregate
    • Neame, P.J., Christner, J.E., and Baker, J.R. (1986). The primary structure of Link protein from rat chondrosarcoma proteoglycan aggregate. J. Biol. Chem. 267, 3519-3535.
    • (1986) J. Biol. Chem. , vol.267 , pp. 3519-3535
    • Neame, P.J.1    Christner, J.E.2    Baker, J.R.3
  • 45
    • 0027269982 scopus 로고
    • Identification of hyaluronic acid binding sites in the extracellular domain of CD44
    • Peach, R.J., Hollenbaugh, D., Stamenkovic, I., and Aruffo, A. (1993). Identification of hyaluronic acid binding sites in the extracellular domain of CD44. J. Cell Biol. 722, 257-264.
    • (1993) J. Cell Biol. , vol.722 , pp. 257-264
    • Peach, R.J.1    Hollenbaugh, D.2    Stamenkovic, I.3    Aruffo, A.4
  • 46
    • 0024409824 scopus 로고
    • Immunoglobulin fold and tandem repeat structures in proteoglycan N-terminal domains and Link protein
    • Perkins, S.J., Nealis, A.S., Dudhia, J., and Hardingham, T.E. (1989). Immunoglobulin fold and tandem repeat structures in proteoglycan N-terminal domains and Link protein. J. Mol. Biol. 206, 737-753.
    • (1989) J. Mol. Biol. , vol.206 , pp. 737-753
    • Perkins, S.J.1    Nealis, A.S.2    Dudhia, J.3    Hardingham, T.E.4
  • 47
    • 0028470923 scopus 로고
    • Biotinylated hyaluronic acid: A new tool for probing hyaluronate-receptor interactions
    • Pouyani, T., and Prestwich, G.D. (1994). Biotinylated hyaluronic acid: a new tool for probing hyaluronate-receptor interactions. Bioconjug. Chem. 5, 370-372.
    • (1994) Bioconjug. Chem. , vol.5 , pp. 370-372
    • Pouyani, T.1    Prestwich, G.D.2
  • 48
    • 0026758360 scopus 로고
    • Cloning and primary structure of neurocan, a developmentally regulated, aggregating chondroitin sulfate proteoglycan of brain
    • Rauch, U., Karthikeyan, L., Maurel, P., Margolis, R.U., and Margolis, R.K. (1992). Cloning and primary structure of neurocan, a developmentally regulated, aggregating chondroitin sulfate proteoglycan of brain. J. Biol. Chem. 267, 19536-19547.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19536-19547
    • Rauch, U.1    Karthikeyan, L.2    Maurel, P.3    Margolis, R.U.4    Margolis, R.K.5
  • 49
    • 0027158038 scopus 로고
    • Lectin-carbohydrate complexes of plants and animal: An atomic view
    • Sharon, N. (1993). Lectin-carbohydrate complexes of plants and animal: an atomic view. Trends Biochem. Sci. 78, 221-226.
    • (1993) Trends Biochem. Sci. , vol.78 , pp. 221-226
    • Sharon, N.1
  • 50
    • 0028533911 scopus 로고
    • Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil
    • Sheriff, S., Chang, C.-Y.Y., and Ezekowitz, R.A.B. (1994). Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil. Struct. Biol. 1, 789-794.
    • (1994) Struct. Biol. , vol.1 , pp. 789-794
    • Sheriff, S.1    Chang, C.-Y.Y.2    Ezekowitz, R.A.B.3
  • 51
    • 0027956397 scopus 로고
    • Hyaluronate receptors: Key players in growth, differentiation, migration and tumour progression
    • Sherman, L., Sleeman, J., Herrlich, P., and Ponta, H. (1994). Hyaluronate receptors: key players in growth, differentiation, migration and tumour progression. Curr. Opin. Cell Biol. 6, 726-733.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 726-733
    • Sherman, L.1    Sleeman, J.2    Herrlich, P.3    Ponta, H.4
  • 53
    • 0000838671 scopus 로고
    • Estimation of interatomic distances in proteins from NOE spectra at longer mixing times using an empirical two-spin equation
    • Suri, A.K., and Levy, R.M. (1993). Estimation of interatomic distances in proteins from NOE spectra at longer mixing times using an empirical two-spin equation. J. Magn. Reson. B101, 320-324.
    • (1993) J. Magn. Reson. , vol.B101 , pp. 320-324
    • Suri, A.K.1    Levy, R.M.2
  • 54
    • 0020957871 scopus 로고
    • Effects of detergent solubilization on the hyaluronate-binding protein from membranes of simian virus 40-transformed 3T3 cells
    • Underhill, C.B., Chi-Rosso, G., and Toole, B.P. (1983). Effects of detergent solubilization on the hyaluronate-binding protein from membranes of simian virus 40-transformed 3T3 cells. J. Biol. Chem. 258, 8086-8091.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8086-8091
    • Underhill, C.B.1    Chi-Rosso, G.2    Toole, B.P.3
  • 55
    • 0029091616 scopus 로고
    • Expression and characterisation of a single recombinant proteoglycan tandem repeat domain of link protein that binds zinc and hyaluronate
    • Varelas, J.B., Kollar, J., Huynh, T.D., and Hering, T.M. (1995). Expression and characterisation of a single recombinant proteoglycan tandem repeat domain of link protein that binds zinc and hyaluronate. Arch. Biochem. Biophys. 321, 21-30.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 21-30
    • Varelas, J.B.1    Kollar, J.2    Huynh, T.D.3    Hering, T.M.4
  • 56
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas, N.K. (1991). Atomic features of protein-carbohydrate interactions. Curr. Opin. Struct. Biol. 1, 732-740.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 732-740
    • Vyas, N.K.1
  • 57
    • 0026342025 scopus 로고
    • Structure of the calcium-dependent lectin domain from a ratmannose-binding protein determined by MAD phasing
    • Weis, W.I., Kahn, R., Fourme, R., Drickamer, K., and Hendrickson, W.A. (1991). Structure of the calcium-dependent lectin domain from a ratmannose-binding protein determined by MAD phasing. Science 254, 1608-1615.
    • (1991) Science , vol.254 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3    Drickamer, K.4    Hendrickson, W.A.5
  • 58
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis, W.I., Drickamer, K., and Hendrickson, W.A. (1992). Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360, 127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 59
    • 0024279235 scopus 로고
    • Analysis and prediction of different types of β-turns in proteins
    • Wilmot, C.M., and Thornton, J.M. (1988). Analysis and prediction of different types of β-turns in proteins. J. Mol. Biol. 203, 221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 60
    • 0027486712 scopus 로고
    • TSG-6: A TNF-, IL-1-, and LPS-inducible secreted glycoprotein associated with arthritis
    • Wisniewski, H.-G., Maier, R., Lotz, M., Lee, S., Lee, T.H., and Vilcek, J. (1993). TSG-6: a TNF-, IL-1-, and LPS-inducible secreted glycoprotein associated with arthritis. J. Immunol. 151, 6593-6601.
    • (1993) J. Immunol. , vol.151 , pp. 6593-6601
    • Wisniewski, H.-G.1    Maier, R.2    Lotz, M.3    Lee, S.4    Lee, T.H.5    Vilcek, J.6
  • 61
    • 0030056876 scopus 로고    scopus 로고
    • TNF/IL-1-inducible protein TSG-6 potentiates plasmin inhibition by inter-α-inhibitor and exerts a strong anti-inflammatory effect in vivo
    • Wisniewski, H.-G., Hua, J.-C., Poppers, D.M., Naime, D., Vilcek, J., and Cronstein, B.N. (1996). TNF/IL-1-inducible protein TSG-6 potentiates plasmin inhibition by inter-α-inhibitor and exerts a strong anti-inflammatory effect in vivo. J. Immunol. 156, 1609-1615.
    • (1996) J. Immunol. , vol.156 , pp. 1609-1615
    • Wisniewski, H.-G.1    Hua, J.-C.2    Poppers, D.M.3    Naime, D.4    Vilcek, J.5    Cronstein, B.N.6
  • 62
    • 0028233391 scopus 로고
    • Molecular cloning of brevican, a novel brain proteoglycan of the aggrecan/versican family
    • Yamada, H., Watanabe, K., Shimonaka, M., and Yamaguchi, Y. (1994). Molecular cloning of brevican, a novel brain proteoglycan of the aggrecan/versican family. J. Biol. Chem. 269, 10119-10126.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10119-10126
    • Yamada, H.1    Watanabe, K.2    Shimonaka, M.3    Yamaguchi, Y.4
  • 63
    • 0028097742 scopus 로고
    • Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein
    • Yang, B., Yang, B.L., Savani, R.C., and Turely, E.A. (1994). Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein. EMBO J. 13, 286-296.
    • (1994) EMBO J. , vol.13 , pp. 286-296
    • Yang, B.1    Yang, B.L.2    Savani, R.C.3    Turely, E.A.4
  • 64
    • 0028887601 scopus 로고
    • Biotinylated hyaluronan as a probe for detection of binding proteins in cells and tissue
    • Yu, Q., and Toole, B.P. (1995). Biotinylated hyaluronan as a probe for detection of binding proteins in cells and tissue. Biotechniques 19, 122-129.
    • (1995) Biotechniques , vol.19 , pp. 122-129
    • Yu, Q.1    Toole, B.P.2
  • 66
    • 0024397823 scopus 로고
    • Multiple domains of the large fibroblast proteoglycan versican
    • Zimmermann, D.R., and Ruoslahti, E. (1989). Multiple domains of the large fibroblast proteoglycan versican. EMBO J. 8, 2975-2981.
    • (1989) EMBO J. , vol.8 , pp. 2975-2981
    • Zimmermann, D.R.1    Ruoslahti, E.2


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