메뉴 건너뛰기




Volumn 3, Issue 4, 1996, Pages 261-271

Versican

Author keywords

Cell migration; Nerve pattering; Proteoglycan; Versican

Indexed keywords

CSPG2 PROTEIN, HUMAN; GLYCOPROTEIN; GLYCOSAMINOGLYCAN; LECTIN; PROTEOCHONDROITIN SULFATE; SCLEROPROTEIN; VERSICAN;

EID: 0030340040     PISSN: 10640517     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (46)

References (98)
  • 1
    • 0027211820 scopus 로고
    • Nervous tissue proteoglycans
    • Margolis, R.K., and Margolis. R.U. (1993). Nervous tissue proteoglycans. Experientia, 49, 429-4-46.
    • (1993) Experientia , vol.49 , pp. 429-446
    • Margolis, R.K.1    Margolis, R.U.2
  • 2
    • 0027420339 scopus 로고
    • Proteoglycans in the nervous system
    • Lander, A.D. (1993). Proteoglycans in the nervous system. Curr Opin. Neurobiol. 3, 716-723.
    • (1993) Curr Opin. Neurobiol. , vol.3 , pp. 716-723
    • Lander, A.D.1
  • 4
    • 0028031129 scopus 로고
    • Brain development and multiple molecular species of proteoglycan
    • Oohira, A., Katoh-Semba, R., Watanabe, E., and Matsui, F. (1994). Brain development and multiple molecular species of proteoglycan. Neurosci. Res. 20, 195-207.
    • (1994) Neurosci. Res. , vol.20 , pp. 195-207
    • Oohira, A.1    Katoh-Semba, R.2    Watanabe, E.3    Matsui, F.4
  • 5
    • 0019808655 scopus 로고
    • Fractionation and properties of a chondroitin sulfate proteoglycan and the soluble glycoproteins of brain
    • Kiang, W-L., Margolis, R.U., and Margolis, R.K. (1981). Fractionation and properties of a chondroitin sulfate proteoglycan and the soluble glycoproteins of brain. J. Biol. Chem. 265, 10529-10537.
    • (1981) J. Biol. Chem. , vol.265 , pp. 10529-10537
    • Kiang, W.-L.1    Margolis, R.U.2    Margolis, R.K.3
  • 6
    • 0025282338 scopus 로고
    • A diverse set of developmentally regulated proteoglycans is expressed in the rat central nervous system
    • Herndon, M.E., and Lander, A.D. (1990). A diverse set of developmentally regulated proteoglycans is expressed in the rat central nervous system. Neuron 4, 949-961.
    • (1990) Neuron , vol.4 , pp. 949-961
    • Herndon, M.E.1    Lander, A.D.2
  • 7
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • Lasky, L.A. (1992). Selectins: Interpreters of cell-specific carbohydrate information during inflammation. Science 258, 964-969.
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 9
    • 0023632550 scopus 로고
    • Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones
    • Doege, K., Sasaki, M., Horigan, E., Hassell, 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    Hassell, J.R.4    Yamada, Y.5
  • 10
    • 0025976188 scopus 로고
    • Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan
    • Doege, K.J., Sasaki, M., Kimura, T., and Yamada, Y. (1991). Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. J. Biol. Chem. 266, 894-902.
    • (1991) J. Biol. Chem. , vol.266 , pp. 894-902
    • Doege, K.J.1    Sasaki, M.2    Kimura, T.3    Yamada, Y.4
  • 11
    • 0027373233 scopus 로고
    • DNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia
    • Li, H., Schwartz N.B., and Vertel B., M. (1993). cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia. J. Biol. Chem. 268, 23504-23511.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23504-23511
    • Li, H.1    Schwartz, N.B.2    Vertel, B.3
  • 12
    • 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
  • 13
    • 0028233391 scopus 로고
    • Molecular cloning of brevican, a novel brain pro-teoglycan of the aggrecan/versican family
    • Yamada, H., Watanabe, K., Shimonaka, M., and Yamaguchi, Y. (1994). Molecular cloning of brevican, a novel brain pro-teoglycan 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
  • 14
    • 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
  • 15
    • 0026646196 scopus 로고
    • The high molecular weight Cat-301 chondroitin sulfate proteoglycan from brain is related to the large aggregating proteoglycan from cartilage, aggrecan
    • Fryer, H.J. L., Kelly, G.M., Molinaro, L., and Hockfield, S. (1992). The high molecular weight Cat-301 chondroitin sulfate proteoglycan from brain is related to the large aggregating proteoglycan from cartilage, aggrecan. J. Biol. Chem. 267, 9874-9883.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9874-9883
    • Fryer, H.J.L.1    Kelly, G.M.2    Molinaro, L.3    Hockfield, S.4
  • 16
    • 0027534369 scopus 로고
    • A large chondroitin sulfate proteoglycan has the characteristics of a general extracellular matrix component of adult brain
    • Iwata, M., and Carlson, S.S. (1993). A large chondroitin sulfate proteoglycan has the characteristics of a general extracellular matrix component of adult brain. J. Neurosci. 13, 195-207.
    • (1993) J. Neurosci. , vol.13 , pp. 195-207
    • Iwata, M.1    Carlson, S.S.2
  • 17
    • 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
    • 0024560984 scopus 로고
    • A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family
    • Stamenkovic, I., Amiot, M., Pesando, J.M., and Seed, B. (1989). A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family. Cell 56, 1057-1062.
    • (1989) Cell , vol.56 , pp. 1057-1062
    • Stamenkovic, I.1    Amiot, M.2    Pesando, J.M.3    Seed, B.4
  • 20
    • 0022479614 scopus 로고
    • Link protein cDNA sequence reveals a tandemly repeated protein structure
    • Doege, K., Hassell, J.R., Caterson, B., and Yamada, Y. (1986). Link protein cDNA sequence reveals a tandemly repeated protein structure. Proc. Natl. Acad. Sci. USA 83, 3761-3765.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3761-3765
    • Doege, K.1    Hassell, J.R.2    Caterson, B.3    Yamada, Y.4
  • 22
    • 0023475065 scopus 로고
    • A fibroblast chondroitin sulfate proteoglycan core protein contains lectin-like and growth factor-like sequences
    • Krusius, T., Gehlsen, K.R., and Ruoslahti, E. (1987). A fibroblast chondroitin sulfate proteoglycan core protein contains lectin-like and growth factor-like sequences. J. Biol. Chem. 262, 13120-13125.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13120-13125
    • Krusius, T.1    Gehlsen, K.R.2    Ruoslahti, E.3
  • 23
    • 0023001894 scopus 로고
    • A large chondroitin sulfate proteoglycan (PG-M) synthesized before chondrogenesis in the limb bud of chick embryo
    • Kimata, K., Oike, Y., Tani, K., Shinomura, T., Yamagata, M., Uritani, M., and Suzuki, S. (1986). A large chondroitin sulfate proteoglycan (PG-M) synthesized before chondrogenesis in the limb bud of chick embryo. J. Biol. Chem. 261, 13517-13525.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13517-13525
    • Kimata, K.1    Oike, Y.2    Tani, K.3    Shinomura, T.4    Yamagata, M.5    Uritani, M.6    Suzuki, S.7
  • 24
    • 0025281412 scopus 로고
    • The distribution of mesenchyme proteoglycan (PG-M) during wing bud outgrowth
    • Shinomura, T., Jensen, K.L., Yamagata, M., Kimata, K., and Sloursh, M. (1990). The distribution of mesenchyme proteoglycan (PG-M) during wing bud outgrowth. Anal. Embryol. (Berl. 181, 227-233.
    • (1990) Anal. Embryol. Berl. , vol.181 , pp. 227-233
    • Shinomura, T.1    Jensen, K.L.2    Yamagata, M.3    Kimata, K.4    Sloursh, M.5
  • 25
    • 0027212199 scopus 로고
    • cDNA cloning of PG-M, a large chondroitin sulfate proteoglycan expressed during chondrogenesis in chick limb buds
    • Shinomura, T., Nishida, Y, Ito, K., and Kimata, K. (1993). cDNA cloning of PG-M, a large chondroitin sulfate proteoglycan expressed during chondrogenesis in chick limb buds. J. Biol. Chem. 268, 14461-14469.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14461-14469
    • Shinomura, T.1    Nishida, Y.2    Ito, K.3    Kimata, K.4
  • 26
    • 0028959255 scopus 로고
    • Multiple forms of mouse PG-M, a large chondroitin sulfate proteoglycan generated by alternative splicing
    • Ito, K., Shinomura, T., Zako, M., Ujita, M., and Kimata, K. (1995). Multiple forms of mouse PG-M, a large chondroitin sulfate proteoglycan generated by alternative splicing. J. Biol. Chem. 270, 958-965.
    • (1995) J. Biol. Chem. , vol.270 , pp. 958-965
    • Ito, K.1    Shinomura, T.2    Zako, M.3    Ujita, M.4    Kimata, K.5
  • 27
    • 0027090482 scopus 로고
    • Mapping of the versican proteoglycan gene (CSPG2) to the long arm of human chromosome 5 (5q12-5q14)
    • Iozzo, R.V., Naso, M.F., Cannizzaro, L.A., Wasmuth, J.J., and McPherson, J.D. (1992). Mapping of the versican proteoglycan gene (CSPG2) to the long arm of human chromosome 5 (5q12-5q14). Genomics 14, 845-851.
    • (1992) Genomics , vol.14 , pp. 845-851
    • Iozzo, R.V.1    Naso, M.F.2    Cannizzaro, L.A.3    Wasmuth, J.J.4    McPherson, J.D.5
  • 28
    • 0029129803 scopus 로고
    • Expression pattern and mapping of the murine versican gene (Cspg2) to chromosome 13
    • Naso, M.F., Morgan, J.L., Buchberg, A.M., Siracusa, L.D., and Iozzo, R.V. (1995). Expression pattern and mapping of the murine versican gene (Cspg2) to chromosome 13. Genomics 29, 297-300.
    • (1995) Genomics , vol.29 , pp. 297-300
    • Naso, M.F.1    Morgan, J.L.2    Buchberg, A.M.3    Siracusa, L.D.4    Iozzo, R.V.5
  • 29
    • 0028556893 scopus 로고
    • Characterization of the complete genomic structure of the human versican gene and functional analysis of its promoter
    • Naso, M.F., Zimmermann, D.R., and Iozzo, R.V. (1994). Characterization of the complete genomic structure of the human versican gene and functional analysis of its promoter. J. Biol. Chem. 269, 32999-33008.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32999-33008
    • Naso, M.F.1    Zimmermann, D.R.2    Iozzo, R.V.3
  • 30
    • 0028566656 scopus 로고
    • A novel glycosaminoglycan attachment domain identified in two alternative splice variants of human versican
    • Dours-Zimmermann, M.T., and Zimmermann, D.R. (1994). A novel glycosaminoglycan attachment domain identified in two alternative splice variants of human versican. J. Biol. Chem. 269, 32992-32998.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32992-32998
    • Dours-Zimmermann, M.T.1    Zimmermann, D.R.2
  • 31
    • 0028959172 scopus 로고
    • Expression of PG-M (V3), an alternatively spliced form of PG-M without a chondroitin sulfate attachment region in mouse and human tissues
    • Zako, M., Shinomura, T., Ujita, M., Ito, K., and Kimata, K. (1995). Expression of PG-M (V3), an alternatively spliced form of PG-M without a chondroitin sulfate attachment region in mouse and human tissues. J. Biol. Chem. 270, 3914-3918.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3914-3918
    • Zako, M.1    Shinomura, T.2    Ujita, M.3    Ito, K.4    Kimata, K.5
  • 32
    • 0028902876 scopus 로고
    • Up-regulation of a chondroitin sulfate epitope during regeneration of mouse sciatic nerve: Evidence that the immunoreactive molecules are related to the chondroitin sulfate proteoglycans decorin and versican
    • Braunewell, K-H., Martini, R., LeBaron, R., Kresse, H., Faissner. A., Schmitz, B., and Schachner, M. (1995). Up-regulation of a chondroitin sulfate epitope during regeneration of mouse sciatic nerve: evidence that the immunoreactive molecules are related to the chondroitin sulfate proteoglycans decorin and versican. Eur. J. Neurosci. 7, 792-804.
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 792-804
    • Braunewell, K.-H.1    Martini, R.2    Lebaron, R.3    Kresse, H.4    Faissner, A.5    Schmitz, B.6    Schachner, M.7
  • 33
    • 0027235791 scopus 로고
    • Tissue variation of two large chondroitin sulfate proteoglycans (PGM/versican and PG-H/aggrecan) in chick embryos
    • Yamagata, M., Shinomura, T., and Kimata, K. (1993). Tissue variation of two large chondroitin sulfate proteoglycans (PGM/versican and PG-H/aggrecan) in chick embryos. Anat. Embryol 187, 433-444.
    • (1993) Anat. Embryol , vol.187 , pp. 433-444
    • Yamagata, M.1    Shinomura, T.2    Kimata, K.3
  • 34
    • 0027769533 scopus 로고
    • Expression of versican mRNA is developmentally regulated in the brain of the embryonic chick and the developing rat
    • Crawford, T.J., Melhado, I.G., and Jirik, F.R. (1993). Expression of versican mRNA is developmentally regulated in the brain of the embryonic chick and the developing rat. Dev. Brain Res. 76, 264-267.
    • (1993) Dev. Brain Res. , vol.76 , pp. 264-267
    • Crawford, T.J.1    Melhado, I.G.2    Jirik, F.R.3
  • 35
    • 0027389847 scopus 로고
    • Versican, a hyaluronate-binding proteoglycan of embryonal precartilaginous mesenchyma, is mainly expressed postnatally in rat brain
    • Bignami, A., Perides, G., and Rahemtulla, F. (1993). Versican, a hyaluronate-binding proteoglycan of embryonal precartilaginous mesenchyma, is mainly expressed postnatally in rat brain. J. Neurosci. Res. 34, 97-106.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 97-106
    • Bignami, A.1    Perides, G.2    Rahemtulla, F.3
  • 36
    • 0029076219 scopus 로고
    • Versican is selectively expressed in embryonic tissues that act as barriers to neural crest cell migration and axon outgrowth
    • Landolt, R.M., Vaughan, L., Winterhalter, K.H., and Zimmermann, D.R. (1995). Versican is selectively expressed in embryonic tissues that act as barriers to neural crest cell migration and axon outgrowth. Development 121, 2303-2312.
    • (1995) Development , vol.121 , pp. 2303-2312
    • Landolt, R.M.1    Vaughan, L.2    Winterhalter, K.H.3    Zimmermann, D.R.4
  • 37
    • 0029134007 scopus 로고
    • Association of versican with dermal matrices and its potential role in hair follicle development and cycling
    • du Gros, D.L., LeBaron, R.G., and Couchman, J.R. (1995). Association of versican with dermal matrices and its potential role in hair follicle development and cycling. J. Invest. Dermato 105, 426-431.
    • (1995) J. Invest. Dermato , vol.105 , pp. 426-431
    • Du Gros, D.L.1    Lebaron, R.G.2    Couchman, J.R.3
  • 38
    • 0026045179 scopus 로고
    • Effects of platelet-derived growth factor and transforming growth factorASI on the synthesis of a large versican-like chondroitin sulfate proteoglycan by arterial smooth muscle cells
    • Schonherr, E., Jarvelainen, H.T., Sandell, L.J., and Wight, T.N. (1991). Effects of platelet-derived growth factor and transforming growth factorASI on the synthesis of a large versican-like chondroitin sulfate proteoglycan by arterial smooth muscle cells. J. Biol. Chem. 266, 17640-17647.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17640-17647
    • Schonherr, E.1    Jarvelainen, H.T.2    Sandell, L.J.3    Wight, T.N.4
  • 40
    • 0028297190 scopus 로고
    • Versican is expressed in the proliferating zone in the epidermis and in association with the elastic network of the dermis
    • Zimmermann, D.R., Dours-Zimmermann, M.T., Schubert, M., and Bruckner-Tuderman, L. (1994). Versican is expressed in the proliferating zone in the epidermis and in association with the elastic network of the dermis. J. Cell Biol. 124, 817-825.
    • (1994) J. Cell Biol. , vol.124 , pp. 817-825
    • Zimmermann, D.R.1    Dours-Zimmermann, M.T.2    Schubert, M.3    Bruckner-Tuderman, L.4
  • 41
    • 0029037685 scopus 로고
    • Differential expression of the versican and decorin genes in photoaged and sun-protected skin
    • Bernstein, E.F., Fisher, L.W., Li, K., LeBaron, R.G., Tan, E.M.L., and Uitto, J. (1995). Differential expression of the versican and decorin genes in photoaged and sun-protected skin. Lab. Invest. 72, 662-669.
    • (1995) Lab. Invest. , vol.72 , pp. 662-669
    • Bernstein, E.F.1    Fisher, L.W.2    Li, K.3    Lebaron, R.G.4    Tan, E.M.L.5    Uitto, J.6
  • 43
    • 0026549103 scopus 로고
    • TGF-β1 -responsive element: Closely associated binding sites for USF and CCAAT binding transcription factor-nuclear factor 1 in type 1 plasminogen activator inhibitor gene
    • Riccio, A., Pedone, P.V., Lund, L.R., Diesen, T., Olsen, H.S., and Andreasen, P.A. (1992). TGF-β1 -responsive element: closely associated binding sites for USF and CCAAT binding transcription factor-nuclear factor 1 in type 1 plasminogen activator inhibitor gene. Mol. Cell. Biol. 12, 1846-1855.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1846-1855
    • Riccio, A.1    Pedone, P.V.2    Lund, L.R.3    Diesen, T.4    Olsen, H.S.5    Andreasen, P.A.6
  • 44
    • 0025967317 scopus 로고
    • Transcription factor AP-2 is expressed in neural crest cell linages during mouse embryogenesis
    • Mitchell, P.J., Timmons, P.M., Hébert, J.M., Rigby, P.W.J., and Tijan, R. (1991). Transcription factor AP-2 is expressed in neural crest cell linages during mouse embryogenesis. Genes Dev. 5, 105-119.
    • (1991) Genes Dev. , vol.5 , pp. 105-119
    • Mitchell, P.J.1    Timmons, P.M.2    Hébert, J.M.3    Rigby, P.W.J.4    Tijan, R.5
  • 45
    • 0026777803 scopus 로고
    • Two immunologically and developmentally distinct chondroitin sulfate proteoglycans in embryonic chick brain
    • Krueger, R.C., Jr, Hennig, A.K., and Schwartz, N.B. (1992). Two immunologically and developmentally distinct chondroitin sulfate proteoglycans in embryonic chick brain. J. Biol. Chem. 267, 12149-12161.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12149-12161
    • Krueger Jr., R.C.1    Hennig, A.K.2    Schwartz, N.B.3
  • 46
    • 0027203504 scopus 로고
    • Interleukin-1 p regulation of fibroblast proteoglycan synthesis involves a decrease in versican steady-state mRNA levels
    • Qwarnstrom, E.E., Jarvelainen, H.T., Kinsella, M.G., Ostberg, CO., Sandell, L.J., Page, R.C., and Wight, T.N. (1993). Interleukin-1 p regulation of fibroblast proteoglycan synthesis involves a decrease in versican steady-state mRNA levels. Biochem. J. 294, 613-620.
    • (1993) Biochem. J. , vol.294 , pp. 613-620
    • Qwarnstrom, E.E.1    Jarvelainen, H.T.2    Kinsella, M.G.3    Ostberg, C.O.4    Sandell, L.J.5    Page, R.C.6    Wight, T.N.7
  • 47
    • 0025834976 scopus 로고
    • Differential regulation of extracellular matrix proteoglycan (PG) gene expression. Transforming growth factor-\S1 up-regulates biglycan (PGI), and versican (large fibroblast PG) but down-regulates decorin (PGII) mRNA levels in human fibroblasts in culture
    • Kahari, V-M., Larjava, H., and Uitto, J. (1991). Differential regulation of extracellular matrix proteoglycan (PG) gene expression. Transforming growth factor-\S1 up-regulates biglycan (PGI), and versican (large fibroblast PG) but down-regulates decorin (PGII) mRNA levels in human fibroblasts in culture. J Biol. Chem. 266, 10608-10615.
    • (1991) J Biol. Chem. , vol.266 , pp. 10608-10615
    • Kahari, V.-M.1    Larjava, H.2    Uitto, J.3
  • 48
    • 0024438644 scopus 로고
    • Transforming growth factor (type β) promotes the addition of chondroitin sulfate chains to the cell surface proteoglycan (syndecan) of mouse mammary epithelia
    • Rapraeger, A. (1989). Transforming growth factor (type β) promotes the addition of chondroitin sulfate chains to the cell surface proteoglycan (syndecan) of mouse mammary epithelia. J. Cell Biol. 109, 2509-2518.
    • (1989) J. Cell Biol. , vol.109 , pp. 2509-2518
    • Rapraeger, A.1
  • 49
    • 0028915753 scopus 로고
    • Functional involvement of sciatic nerve-derived versican- And decorin-like molecules and other chondroitin sulfate proteoglycans in ECM-mediated cell adhesion and neurite outgrowth
    • Braunwell, K-H., Pesheva, P., McCarthy, J.B., Furcht, L.T., Schmitz, B., and Schachner, M. (1995). Functional involvement of sciatic nerve-derived versican- and decorin-like molecules and other chondroitin sulfate proteoglycans in ECM-mediated cell adhesion and neurite outgrowth. Eur. J. Neurosci. 7, 805-814.
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 805-814
    • Braunwell, K.-H.1    Pesheva, P.2    McCarthy, J.B.3    Furcht, L.T.4    Schmitz, B.5    Schachner, M.6
  • 50
    • 0025146856 scopus 로고
    • Monoclonal antibodies against chondroitin sulfate isomers: Their use as probes for investigating proteoglycan metabolism
    • Caterson, B., Griffin, J., Mahmoodian, F., and Sorrell, J.M. (1990). Monoclonal antibodies against chondroitin sulfate isomers: their use as probes for investigating proteoglycan metabolism. Biochem. Soc. Trans. 18, 820-823.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 820-823
    • Caterson, B.1    Griffin, J.2    Mahmoodian, F.3    Sorrell, J.M.4
  • 51
    • 0024392884 scopus 로고
    • Proteoglycan biosynthesis in murine monocytic leukemic (M1) cells before and after differentiation
    • McQuillan, D.J., Yanagishita, M., Hascall, V.C., and Bickel, M. (1989). Proteoglycan biosynthesis in murine monocytic leukemic (M1) cells before and after differentiation. J. Biol. Chem. 264, 13245-13251.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13245-13251
    • McQuillan, D.J.1    Yanagishita, M.2    Hascall, V.C.3    Bickel, M.4
  • 52
    • 0023812798 scopus 로고
    • Distinct synthetic and structural characteristics of proteoglycans produced by cultured artery smooth muscle cells of atherosclerosis-susceptible pigeons
    • Edwards, I.J., and Wagner, W.D. (1988). Distinct synthetic and structural characteristics of proteoglycans produced by cultured artery smooth muscle cells of atherosclerosis-susceptible pigeons. J. Biol. Chem. 263, 9612-9620.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9612-9620
    • Edwards, I.J.1    Wagner, W.D.2
  • 53
    • 0023184727 scopus 로고
    • Induction of ornithine decarboxylase activity and putrescine synthesis in arterial smooth muscle cells stimulated with platelet-derived growth factor
    • Thyberg, J., and Fredholm, B.B. (1987). Induction of ornithine decarboxylase activity and putrescine synthesis in arterial smooth muscle cells stimulated with platelet-derived growth factor. Exp. Cell Res. 170, 160-169.
    • (1987) Exp. Cell Res. , vol.170 , pp. 160-169
    • Thyberg, J.1    Fredholm, B.B.2
  • 54
    • 0027332279 scopus 로고
    • Alternate exon usage is a commonly used mechanism for increasing coding diversity within genes coding for extracellular matrix proteins
    • Boyd, C.D., Pierce, R.A., Schwarzbauer, J.E., Doege, K., and Sandell, L.J. (1993). Alternate exon usage is a commonly used mechanism for increasing coding diversity within genes coding for extracellular matrix proteins. Matrix 13, 457-469.
    • (1993) Matrix , vol.13 , pp. 457-469
    • Boyd, C.D.1    Pierce, R.A.2    Schwarzbauer, J.E.3    Doege, K.4    Sandell, L.J.5
  • 55
    • 0024590223 scopus 로고
    • Isolation and partial characterization of a glial hyaluronate-binding protein
    • Perides, G., Lane, W.S., Andrews, D., Dahl, D., and Bignami, A. (1989). Isolation and partial characterization of a glial hyaluronate-binding protein. J. Biol. Chem. 264, 5981-5987.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5981-5987
    • Perides, G.1    Lane, W.S.2    Andrews, D.3    Dahl, D.4    Bignami, A.5
  • 56
    • 0029560294 scopus 로고
    • Glial hyaluronate-binding protein: A product of metalloproteinase digestion of versican?
    • Perides, G., Asher, R.A., Lark, M.W., Lane, W.S., Robinson, R.A., and Bignami, A. (1995). Glial hyaluronate-binding protein: a product of metalloproteinase digestion of versican? Biocliem. J. 312, 377-384.
    • (1995) Biocliem. J. , vol.312 , pp. 377-384
    • Perides, G.1    Asher, R.A.2    Lark, M.W.3    Lane, W.S.4    Robinson, R.A.5    Bignami, A.6
  • 57
    • 0025776382 scopus 로고
    • Catabolism of aggrecan in cartilage expiants. Identification of a major cleavage site within the interglobular domain
    • Sandy, J.D., Neame, P.J., Boynton, R.E., and Flannery, C.R. (1991). Catabolism of aggrecan in cartilage expiants. Identification of a major cleavage site within the interglobular domain. J. Biol. Chem. 266, 8683-8685.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8683-8685
    • Sandy, J.D.1    Neame, P.J.2    Boynton, R.E.3    Flannery, C.R.4
  • 58
    • 0027445981 scopus 로고
    • The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis
    • Lohmander, L.S., Neame, P.J., and Sandy, J.D. (1993). The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis. Arthritis Rheum. 36, 1214-1222.
    • (1993) Arthritis Rheum. , vol.36 , pp. 1214-1222
    • Lohmander, L.S.1    Neame, P.J.2    Sandy, J.D.3
  • 59
    • 0023609134 scopus 로고
    • The tandemly repeated sequences of cartilage link protein contain the sites for interaction with hyaluronic acid
    • Goetinck, P.F., Stripe, N.S., Tsonis, P.A., and Carlone, D. (1987). The tandemly repeated sequences of cartilage link protein contain the sites for interaction with hyaluronic acid. J. Cell Biol. 105, 2403-2408.
    • (1987) J. Cell Biol. , vol.105 , pp. 2403-2408
    • Goetinck, P.F.1    Stripe, N.S.2    Tsonis, P.A.3    Carlone, D.4
  • 60
  • 61
    • 0027082785 scopus 로고
    • Isolation of a large aggregating proteoglycan from human brain
    • Perides, G., Rahemtulla, F., Lane, W.S., Asher, R.A. and Bignami, A. (1992). Isolation of a large aggregating proteoglycan from human brain. J. Biol. Chem. 267, 23883-23887.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23883-23887
    • Perides, G.1    Rahemtulla, F.2    Lane, W.S.3    Asher, R.A.4    Bignami, A.5
  • 63
    • 0024406159 scopus 로고
    • Isolation of the N-terminal globular protein domains from cartilage proteoglycans
    • Fosang, A.J., and Hardingham, T.E. (1989). Isolation of the N-terminal globular protein domains from cartilage proteoglycans. Biochem. J. 261, 801-809.
    • (1989) Biochem. J. , vol.261 , pp. 801-809
    • Fosang, A.J.1    Hardingham, T.E.2
  • 64
    • 0028360757 scopus 로고
    • Interactions with tenascin and differential effects in cell adhesion of neurocan and phosphacan, two major chondroitin sulfate proteoglycans of nervous tissue
    • Grumet, M., Milev, P., Sakurai, T., Karthikeyan, L., Bourdon, M., Margolis, R.K., and Margolis, R.U. (1994). Interactions with tenascin and differential effects in cell adhesion of neurocan and phosphacan, two major chondroitin sulfate proteoglycans of nervous tissue. J. Biol. Chem. 269, 12142-12146.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12142-12146
    • Grumet, M.1    Milev, P.2    Sakurai, T.3    Karthikeyan, L.4    Bourdon, M.5    Margolis, R.K.6    Margolis, R.U.7
  • 66
    • 0028235153 scopus 로고
    • Receptor tyrosine phosphatase β is expressed in the form of proteoglycan and binds to the extracellular matrix protein tenascin
    • Barnea, G., Grumet, M., Milev, P., Silvennoinen, O., Levy, J.B., Sap, J., and Schlessinger, J. (1994). Receptor tyrosine phosphatase β is expressed in the form of proteoglycan and binds to the extracellular matrix protein tenascin. J. Biol. Chem. 269, 14349-14352.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14349-14352
    • Barnea, G.1    Grumet, M.2    Milev, P.3    Silvennoinen, O.4    Levy, J.B.5    Sap, J.6    Schlessinger, J.7
  • 67
    • 0028783449 scopus 로고
    • The versican C-type lectin domain recognizes the adhesion protein tenascin-R
    • Aspberg, A., Binkert, C., Ruoslahti, E. (1995). The versican C-type lectin domain recognizes the adhesion protein tenascin-R. Proc. Natl. Acad. Sci. USA 92, 10590-10594.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10590-10594
    • Aspberg, A.1    Binkert, C.2    Ruoslahti, E.3
  • 68
    • 0028104981 scopus 로고
    • Expression and binding activity of the carboxy-terminal portion of the core protein of PG-M, a large chondroitin sulfate proteoglycan
    • Ujita, M., Shinomura, T., Ito, K., Kitagawa, Y., and Kimata, K. (1994). Expression and binding activity of the carboxy-terminal portion of the core protein of PG-M, a large chondroitin sulfate proteoglycan. J. Biol. Chem. 269, 27603-27609.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27603-27609
    • Ujita, M.1    Shinomura, T.2    Ito, K.3    Kitagawa, Y.4    Kimata, K.5
  • 69
    • 0022707292 scopus 로고
    • Adhesion and cytoskeletal organization of fibroblasts in response to fibronectin fragments
    • Woods, A., Couchman, J.R., Johansson, S., and Höök, M. (1986). Adhesion and cytoskeletal organization of fibroblasts in response to fibronectin fragments. EMBO J. 5, 665-670.
    • (1986) EMBO J. , vol.5 , pp. 665-670
    • Woods, A.1    Couchman, J.R.2    Johansson, S.3    Höök, M.4
  • 70
    • 0023870741 scopus 로고
    • Adhesion of glycosaminoglycan-deficient Chinese hamster ovary cell mutants to fibronectin substrata
    • LeBaron, R.G., Esko, J.D., Woods, A., Johansson, S., and Höök, M. (1988). Adhesion of glycosaminoglycan-deficient Chinese hamster ovary cell mutants to fibronectin substrata. J. Cell Biol. 106, 945-952.
    • (1988) J. Cell Biol. , vol.106 , pp. 945-952
    • Lebaron, R.G.1    Esko, J.D.2    Woods, A.3    Johansson, S.4    Höök, M.5
  • 71
    • 0027315260 scopus 로고
    • A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation
    • Woods, A., McCarthy, J.B., Furcht, L.T., and Couchman, J.R. (1993). A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation. Mol. Biol. Cell 4, 605-613.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 605-613
    • Woods, A.1    McCarthy, J.B.2    Furcht, L.T.3    Couchman, J.R.4
  • 72
    • 0022981629 scopus 로고
    • Chondroitin sulfate proteoglycan (PG-M-like proteoglycan) is involved in the binding of hyaluronic acid to cellular fibronectin
    • Yamagata, M., Yamada, K.M., Yoneda, M., Suzuki, S., and Kimata, K. (1986). Chondroitin sulfate proteoglycan (PG-M-like proteoglycan) is involved in the binding of hyaluronic acid to cellular fibronectin. J. Biol. Chem. 261, 13526-13535.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13526-13535
    • Yamagata, M.1    Yamada, K.M.2    Yoneda, M.3    Suzuki, S.4    Kimata, K.5
  • 73
    • 0023890664 scopus 로고
    • Molecular organization and function of the complement system
    • Muller-Eberhard, H.J. (1988). Molecular organization and function of the complement system. Annu. Rev. Biochem. 57, 321-347.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 321-347
    • Muller-Eberhard, H.J.1
  • 77
    • 0027143843 scopus 로고
    • Colocalization of tenascin with versican, a hyaluronate-binding chondroitin sulfate proteoglycan
    • Perides, G., Erickson, H.P., Rahemtulla, F., and Bignami, A. (1993). Colocalization of tenascin with versican, a hyaluronate-binding chondroitin sulfate proteoglycan. Anat. Embryol. 188, 467-179.
    • (1993) Anat. Embryol. , vol.188 , pp. 467-1179
    • Perides, G.1    Erickson, H.P.2    Rahemtulla, F.3    Bignami, A.4
  • 78
    • 0025038449 scopus 로고
    • Hyaluronan and its binding properties, the hyaladherins
    • Toole, B.P. (1990). Hyaluronan and its binding properties, the hyaladherins. Curr. Opin. Cell Biol. 2, 839-44.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 839-844
    • Toole, B.P.1
  • 79
    • 0026587707 scopus 로고
    • Ultrastructural localization of hyaluronan in myelin sheaths of the rat central and rat and human peripheral nervous systems using hyaluronan-binding protein-gold and link protein-gold
    • Eggli, P.S., Lucocq, J., Ott, P., Graber, W., and Van Der Zypen, E. (1992). Ultrastructural localization of hyaluronan in myelin sheaths of the rat central and rat and human peripheral nervous systems using hyaluronan-binding protein-gold and link protein-gold. Neuroscience 48, 737-744.
    • (1992) Neuroscience , vol.48 , pp. 737-744
    • Eggli, P.S.1    Lucocq, J.2    Ott, P.3    Graber, W.4    Van Der Zypen, E.5
  • 80
    • 0025194419 scopus 로고
    • Clinical aspects of chondroprotection
    • Huskisson, E.C. (1990). Clinical aspects of chondroprotection. Semin. Arthritis Rheum. 19 (suppl. 1), 30-32.
    • (1990) Semin. Arthritis Rheum. , vol.19 , Issue.1 SUPPL. , pp. 30-32
    • Huskisson, E.C.1
  • 81
    • 0025308440 scopus 로고
    • Chondroprotection, myth or reality: An experimental approach
    • Ghosh, P., Wells, C., Smith, M., and Hutadilok, N. (1990). Chondroprotection, myth or reality: an experimental approach. Semin. Arthritis Rheum. 19 (suppl. 1), 3-9.
    • (1990) Semin. Arthritis Rheum. , vol.19 , Issue.SUPPL. 1 , pp. 3-9
    • Ghosh, P.1    Wells, C.2    Smith, M.3    Hutadilok, N.4
  • 82
    • 0028607601 scopus 로고
    • Osteoarthritis and chondroprotection
    • Mevorach, D., and Menkes, C.J. (1994). Osteoarthritis and chondroprotection. Isr. J. Med. Sci. 30, 928-931.
    • (1994) Isr. J. Med. Sci. , vol.30 , pp. 928-931
    • Mevorach, D.1    Menkes, C.J.2
  • 83
    • 0025744729 scopus 로고
    • Restrictin: A chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11
    • Rathjen, F.G., Wolff, J.M., and Chiquet-Ehrismann, R. (1991). Restrictin: A chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11. Develop 113, 151-164.
    • (1991) Develop , vol.113 , pp. 151-164
    • Rathjen, F.G.1    Wolff, J.M.2    Chiquet-Ehrismann, R.3
  • 84
    • 0026244872 scopus 로고
    • Anti-adhesive molecules of the extracellular matrix
    • Chiquet-Ehrismann, R. (1991). Anti-adhesive molecules of the extracellular matrix. Curr. Opin. Cell Biol. 3, 800-804.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 800-804
    • Chiquet-Ehrismann, R.1
  • 85
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions
    • Sage, E.H., and Bornstein, P. (1991). Extracellular proteins that modulate cell-matrix interactions. J. Biol. Chem. 266, 14831-14834.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 86
    • 0027992168 scopus 로고
    • Tenascin-R (J1 160/180) inhibits fibronectin-mediated cell adhesion-functional relatedness to tenascin-C
    • Pesheva, P., Probstmeier, R., Skubitz, A.P., McCarthy, J.B., Furcht, L.T., and Schachner, M. (1994). Tenascin-R (J1 160/180) inhibits fibronectin-mediated cell adhesion-functional relatedness to tenascin-C. J. Cell Sci. 107, 2323-2333.
    • (1994) J. Cell Sci. , vol.107 , pp. 2323-2333
    • Pesheva, P.1    Probstmeier, R.2    Skubitz, A.P.3    McCarthy, J.B.4    Furcht, L.T.5    Schachner, M.6
  • 87
    • 0028132870 scopus 로고
    • Repression of a malignant cell-substratum adhesion phenotype by inhibiting the production of the anti-adhesive proteoglycan, PG-M/versican
    • Yamagata, M., and Kimata, K. (1994). Repression of a malignant cell-substratum adhesion phenotype by inhibiting the production of the anti-adhesive proteoglycan, PG-M/versican. J. Cell Sci. 107, 2581-2590.
    • (1994) J. Cell Sci. , vol.107 , pp. 2581-2590
    • Yamagata, M.1    Kimata, K.2
  • 88
    • 0027381062 scopus 로고
    • Selective distributions of proteoglycans and their ligands in pericellular matrix of cultured fibroblasts
    • Yamagata, M., Saga, S., Kato, M., Bernfield, M., and Kimata, K. (1993). Selective distributions of proteoglycans and their ligands in pericellular matrix of cultured fibroblasts. J. Cell Sci. 106, 55-65.
    • (1993) J. Cell Sci. , vol.106 , pp. 55-65
    • Yamagata, M.1    Saga, S.2    Kato, M.3    Bernfield, M.4    Kimata, K.5
  • 89
    • 0020603516 scopus 로고
    • Effect of a proteoglycan produced by rat tumor cells on their adhesion to fibronectin-collagen substrata
    • Brennan, M.J., Oldberg, Å., Hayman, E.G., and Ruoslahti, E. (1983). Effect of a proteoglycan produced by rat tumor cells on their adhesion to fibronectin-collagen substrata. Cancer Res. 43, 4302-4307.
    • (1983) Cancer Res. , vol.43 , pp. 4302-4307
    • Brennan, M.J.1    Oldberg, Å.2    Hayman, E.G.3    Ruoslahti, E.4
  • 90
    • 0023581851 scopus 로고
    • Fibronectin-mediated adhesion of fibroblasts: Inhibition by dermatan sulfate proteoglycan and evidence for a cryptic glycosaminoglycan-binding domain
    • Lewandowska, K., Choi, H.U., Rosenberg, L.C., Zardi, L., and Culp, L.A. (1987). Fibronectin-mediated adhesion of fibroblasts: Inhibition by dermatan sulfate proteoglycan and evidence for a cryptic glycosaminoglycan-binding domain. J. Cell Biol. 105, 1443-1454.
    • (1987) J. Cell Biol. , vol.105 , pp. 1443-1454
    • Lewandowska, K.1    Choi, H.U.2    Rosenberg, L.C.3    Zardi, L.4    Culp, L.A.5
  • 91
    • 0024389990 scopus 로고
    • Regulation of cell substrate adhesion by proteoglycans immobilized on extracellular substrates
    • Yamagata, M., Suzuki, S., Akiyama, S.K., Yamada, K.M., and Kimata, K. (1989). Regulation of cell substrate adhesion by proteoglycans immobilized on extracellular substrates. J. Biol. Chem. 264-8012-8018.
    • (1989) J. Biol. Chem.
    • Yamagata, M.1    Suzuki, S.2    Akiyama, S.K.3    Yamada, K.M.4    Kimata, K.5
  • 92
    • 0026674234 scopus 로고
    • Regulation of cell substrate adhesion: Effects of small galactosaminoglycan-containing proteoglycans
    • Bidanset, D.J., LeBaron, R., Rosenberg, L., Murphy-Ullrich, J.E., and Höök, M. (1992). Regulation of cell substrate adhesion: Effects of small galactosaminoglycan-containing proteoglycans. J. Cell Biol. 118, 1523-1531.
    • (1992) J. Cell Biol. , vol.118 , pp. 1523-1531
    • Bidanset, D.J.1    Lebaron, R.2    Rosenberg, L.3    Murphy-Ullrich, J.E.4    Höök, M.5
  • 93
    • 0023033084 scopus 로고
    • Conditioning of native substrates by chondroitin sulfate proteoglycans during cardiac mesenchymal cell migration
    • Funderburg, F.M., and Markwald, R.R. (1986). Conditioning of native substrates by chondroitin sulfate proteoglycans during cardiac mesenchymal cell migration. J. Cell Biol. 103, 2475-2487.
    • (1986) J. Cell Biol. , vol.103 , pp. 2475-2487
    • Funderburg, F.M.1    Markwald, R.R.2
  • 94
    • 0030340041 scopus 로고    scopus 로고
    • Functions of brain chondroitin sulfate proteoglycans during development; interactions with adhesion molecules
    • Grumet, M., Friedlander, D.R., and Sakurai, T. (1996). Functions of brain chondroitin sulfate proteoglycans during development; interactions with adhesion molecules. Perspectives on Developmental Neurobiology. Grumet et. al. 1, 319-330
    • (1996) Perspectives on Developmental Neurobiology. Grumet Et. Al. , vol.1 , pp. 319-330
    • Grumet, M.1    Friedlander, D.R.2    Sakurai, T.3
  • 95
    • 0025349329 scopus 로고
    • Molecular and cellular characterization of the glial roof plate of the spinal cord and optic tectum: A possible role for a proteoglycan in the development of an axon barrier
    • Snow, D.M., Steindler, D.A., and Silver, J. (1990). Molecular and cellular characterization of the glial roof plate of the spinal cord and optic tectum: A possible role for a proteoglycan in the development of an axon barrier. Dev. Biol. 138, 359-376.
    • (1990) Dev. Biol. , vol.138 , pp. 359-376
    • Snow, D.M.1    Steindler, D.A.2    Silver, J.3
  • 96
    • 0028200196 scopus 로고
    • Thalamocortical axons extend along a chondroitin sulfate proteoglycan-enriched pathway coincident with the neocortical subplate and distinct from the efferent path
    • Bicknese, A.R., Sheppard, A.M., O'Leary, D.D.M., and Pearlman, A.L. (1994). Thalamocortical axons extend along a chondroitin sulfate proteoglycan-enriched pathway coincident with the neocortical subplate and distinct from the efferent path. J. Neurosci. 14, 3500-3510.
    • (1994) J. Neurosci. , vol.14 , pp. 3500-3510
    • Bicknese, A.R.1    Sheppard, A.M.2    O'Leary, D.D.M.3    Pearlman, A.L.4
  • 97
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellen, L., and Lindhal, U. (1991). Proteoglycans: Structures and interactions. Annu. Rev. Biochem. 60, 443-475.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindhal, U.2
  • 98
    • 0028555816 scopus 로고
    • Age-related changes of scierai hydration and sulfated glycosaminoglycans
    • Brown, C.T., Vural, M., Johnson, M., and Trinkaus-Randall, V. (1994). Age-related changes of scierai hydration and sulfated glycosaminoglycans. Mech. Ageing Dev. 77, 97-102.
    • (1994) Mech. Ageing Dev. , vol.77 , pp. 97-102
    • Brown, C.T.1    Vural, M.2    Johnson, M.3    Trinkaus-Randall, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.