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Volumn 134, Issue 6, 1996, Pages 1499-1512

Tenascin-Y: A protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue

Author keywords

[No Author keywords available]

Indexed keywords

TENASCIN;

EID: 0029822205     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.134.6.1499     Document Type: Article
Times cited : (85)

References (60)
  • 1
    • 0027474006 scopus 로고
    • Cell- and heparin-binding domains of the hexabrachion arm identified by tenasein expression proteins
    • Aukhil, I., P. Joshi, Y. Yan, and H.P. Erickson. 1993. Cell- and heparin-binding domains of the hexabrachion arm identified by tenasein expression proteins. J. Biol. Chem. 268:2542-2553.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2542-2553
    • Aukhil, I.1    Joshi, P.2    Yan, Y.3    Erickson, H.P.4
  • 2
    • 0027339605 scopus 로고
    • Tena, a Drosophila gene related to tenascin, shows selective transcript localization
    • Baumgartner, S., and R. Chiquet-Ehrismann. 1993. Tena, a Drosophila gene related to tenascin, shows selective transcript localization. Mech. Dev. 40:165-176.
    • (1993) Mech. Dev. , vol.40 , pp. 165-176
    • Baumgartner, S.1    Chiquet-Ehrismann, R.2
  • 3
    • 0024469811 scopus 로고
    • Molecular cloning and sequencing of ama-1, the gene encoding the largest subunit of Caenorhabditis elegans RNA polymerase II
    • Bird, D.M., and D.L. Riddle. 1989. Molecular cloning and sequencing of ama-1, the gene encoding the largest subunit of Caenorhabditis elegans RNA polymerase II. Mol. Cell Biol. 9:4119-4130.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 4119-4130
    • Bird, D.M.1    Riddle, D.L.2
  • 4
    • 0001183058 scopus 로고
    • Mobile modules and motifs
    • Bork, P. 1992. Mobile modules and motifs. Curr. Opin. Struct. Biol. 2:413-421.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 413-421
    • Bork, P.1
  • 5
    • 0027231385 scopus 로고
    • Tenascin-X: A novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B
    • Bristow, J., M. Kian Tee, S.E. Gitelman, S.H. Mellon, and W.L. Miller. 1993. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J. Cell Biol. 122:265-278.
    • (1993) J. Cell Biol. , vol.122 , pp. 265-278
    • Bristow, J.1    Kian Tee, M.2    Gitelman, S.E.3    Mellon, S.H.4    Miller, W.L.5
  • 6
    • 0029142882 scopus 로고
    • Embryonic expression of tenascin-X suggests a role in limb, muscle, and heart development
    • Burch, G.H., M.A. Bedolli, S. McDonough, S.M. Rosenthal, and J. Bristow. 1995. Embryonic expression of tenascin-X suggests a role in limb, muscle, and heart development. Dev. Dyn. 203:491-504.
    • (1995) Dev. Dyn. , vol.203 , pp. 491-504
    • Burch, G.H.1    Bedolli, M.A.2    McDonough, S.3    Rosenthal, S.M.4    Bristow, J.5
  • 8
    • 0029120352 scopus 로고
    • Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle
    • Busby, T.F., W.S. Argraves, S.A. Brew, I. Pechik, G.L. Gilliland, and K.C. Ingham. 1995. Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle. J. Biol. Chem. 270:18558-18562.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18558-18562
    • Busby, T.F.1    Argraves, W.S.2    Brew, S.A.3    Pechik, I.4    Gilliland, G.L.5    Ingham, K.C.6
  • 9
    • 0025736963 scopus 로고
    • Isolation of chick tenascin variants and fragments. A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant
    • Chiquet, M., N. Vručinić Filipi, S. Schenk, K. Beck, and R. Chiquet-Ehrismann. 1991. Isolation of chick tenascin variants and fragments. A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant. Eur. J. Biochem. 199;379-388.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 379-388
    • Chiquet, M.1    Vručinić Filipi, N.2    Schenk, S.3    Beck, K.4    Chiquet-Ehrismann, R.5
  • 10
    • 0021270360 scopus 로고
    • Chick myotendinous antigen I. A monoclonal antibody as a marker for tendon and muscle morphogenesis
    • Chiquet, M., and D.M. Fambrough. 1984a. Chick myotendinous antigen I. A monoclonal antibody as a marker for tendon and muscle morphogenesis. J. Cell Biol. 98:1926-1936.
    • (1984) J. Cell Biol. , vol.98 , pp. 1926-1936
    • Chiquet, M.1    Fambrough, D.M.2
  • 11
    • 0021262798 scopus 로고
    • Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits
    • Chiquet, M., and D.M. Fambrough. 1984b. Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits. J. Cell Biol. 98:1937-1946.
    • (1984) J. Cell Biol. , vol.98 , pp. 1937-1946
    • Chiquet, M.1    Fambrough, D.M.2
  • 12
    • 0025354001 scopus 로고
    • What distinguishes tenascin from fibronectin?
    • Chiquet-Ehrismann, R. 1990. What distinguishes tenascin from fibronectin? FASEB J. 4:2598-2604.
    • (1990) FASEB J. , vol.4 , pp. 2598-2604
    • Chiquet-Ehrismann, R.1
  • 13
    • 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
  • 14
    • 0026252643 scopus 로고
    • Tenascin variants: Differential binding to fibronectin and distinct distribution in cell cultures and tissues
    • Chiquet-Ehrismann, R., Y. Matsuoka, U. Hofer, J. Spring, C. Bernasconi, and M. Chiquet. 1991. Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues. Cell Regul. 2:927-938.
    • (1991) Cell Regul. , vol.2 , pp. 927-938
    • Chiquet-Ehrismann, R.1    Matsuoka, Y.2    Hofer, U.3    Spring, J.4    Bernasconi, C.5    Chiquet, M.6
  • 15
    • 0027672437 scopus 로고
    • Tenascin and other adhesion-modulating proteins in cancer
    • Chiquet-Ehrismann, R. 1993. Tenascin and other adhesion-modulating proteins in cancer. Semin. Cancer Biol. 4:301-310.
    • (1993) Semin. Cancer Biol. , vol.4 , pp. 301-310
    • Chiquet-Ehrismann, R.1
  • 17
    • 0028859440 scopus 로고
    • Tenascins, a growing family of extracellular matrix proteins
    • Chiquet-Ehrismann, R. 1995. Tenascins, a growing family of extracellular matrix proteins. Experientia. 51:853-862.
    • (1995) Experientia , vol.51 , pp. 853-862
    • Chiquet-Ehrismann, R.1
  • 18
    • 0029379601 scopus 로고
    • The complexity in regulating the expression of tenascins
    • Chiquet-Ehrismann, R., C. Hagios, and S. Schenk. 1995. The complexity in regulating the expression of tenascins. Bioessays. 17:873-878.
    • (1995) Bioessays , vol.17 , pp. 873-878
    • Chiquet-Ehrismann, R.1    Hagios, C.2    Schenk, S.3
  • 19
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 21
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle, R.F. 1995. The multiplicity of domains in proteins. Annu. Rev. Biochem. 64:287-314.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 22
    • 0028574361 scopus 로고
    • Domain organizations of extracellular matrix proteins and their evolution
    • Engel, J., V.P. Efimov, and P. Maurer. 1994. Domain organizations of extracellular matrix proteins and their evolution. Development. (Suppl). 35-42.
    • (1994) Development. (Suppl) , pp. 35-42
    • Engel, J.1    Efimov, V.P.2    Maurer, P.3
  • 23
    • 0027685702 scopus 로고
    • Tenascin-C. tenascin-R, and tenascin-X - A family of talented proteins in search of functions
    • Erickson, H.P. 1993. Tenascin-C. tenascin-R, and tenascin-X - a family of talented proteins in search of functions. Curr. Opin. Cell Biol. 5:869-876.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 24
    • 0028694581 scopus 로고
    • Evolution of the tenascin family - Implications for function of the C-terminal fibrinogen-like domain
    • Erickson, H.P. 1994. Evolution of the tenascin family - implications for function of the C-terminal fibrinogen-like domain. Perspect. Dev. Neurobiol. 2:9-19.
    • (1994) Perspect. Dev. Neurobiol. , vol.2 , pp. 9-19
    • Erickson, H.P.1
  • 25
    • 0021166341 scopus 로고
    • A six-armed oligomer isolated from cell surface fibronectin preparations
    • Erickson, H.P., and J.L. Iglesias. 1984. A six-armed oligomer isolated from cell surface fibronectin preparations. Nature (Lond) 311:267-269.
    • (1984) Nature (Lond) , vol.311 , pp. 267-269
    • Erickson, H.P.1    Iglesias, J.L.2
  • 27
    • 0028813381 scopus 로고
    • A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C
    • Fischer, D., R. Chiquet-Ehrismann, C. Bernasconi, and M. Chiquet. 1995. A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C. J. Biol. Chem. 270:3378-3384.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3378-3384
    • Fischer, D.1    Chiquet-Ehrismann, R.2    Bernasconi, C.3    Chiquet, M.4
  • 28
    • 0027397492 scopus 로고
    • Molecular characterization and in situ mRNA localization of the neural recognition molecule J1-160/180: A modular structure similar to tenascin
    • Fuss, B., E.S. Wintergerst, U. Bartsch, and M. Schachner. 1993. Molecular characterization and in situ mRNA localization of the neural recognition molecule J1-160/180: a modular structure similar to tenascin. J. Cell Biol. 120: 1237-1249.
    • (1993) J. Cell Biol. , vol.120 , pp. 1237-1249
    • Fuss, B.1    Wintergerst, E.S.2    Bartsch, U.3    Schachner, M.4
  • 29
    • 0029072597 scopus 로고
    • Distinct tissue distribution in pigs of tenascin-X and tenascin-C transcripts
    • Geffrotin, C., J.J. Garrido, L. Trement, and M. Vaiman. 1995. Distinct tissue distribution in pigs of tenascin-X and tenascin-C transcripts. Eur. J. Biochem. 231:83-92.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 83-92
    • Geffrotin, C.1    Garrido, J.J.2    Trement, L.3    Vaiman, M.4
  • 30
    • 0018263844 scopus 로고
    • Why genes in pieces?
    • Gilbert, W. 1978. Why genes in pieces? Nature (Lond). 271:501.
    • (1978) Nature (Lond) , vol.271 , pp. 501
    • Gilbert, W.1
  • 32
    • 0025312816 scopus 로고
    • Chromosomal localization of the human hexabrachion (tenascin) gene and evidence for recent reduplication within the gene
    • Gulcher, J.R., M.J. Alexakos, M.M. Le Beau, R.S. Lemons, and K. Stefansson. 1990. Chromosomal localization of the human hexabrachion (tenascin) gene and evidence for recent reduplication within the gene. Genomics 6:616-622.
    • (1990) Genomics , vol.6 , pp. 616-622
    • Gulcher, J.R.1    Alexakos, M.J.2    Le Beau, M.M.3    Lemons, R.S.4    Stefansson, K.5
  • 34
    • 0029597870 scopus 로고
    • Distinct sites on tenascin-C mediate repellent or adhesive interactions with different neuronal cell types
    • Husmann, K., S. Carbonetto, and M. Schachner. 1995. Distinct sites on tenascin-C mediate repellent or adhesive interactions with different neuronal cell types. Cell Adhes. Commun. 3:293-310.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 293-310
    • Husmann, K.1    Carbonetto, S.2    Schachner, M.3
  • 35
    • 0025819448 scopus 로고
    • The IgA-binding β antigen of the c protein complex of group B streptococci: Sequence determination of its gene and detection of two binding regions
    • Jerlström, P.G., G.S. Chhatwal, and K.M. Timmis. 1991. The IgA-binding β antigen of the c protein complex of group B streptococci: sequence determination of its gene and detection of two binding regions. Mol. Microbiol. 5:843-849.
    • (1991) Mol. Microbiol. , vol.5 , pp. 843-849
    • Jerlström, P.G.1    Chhatwal, G.S.2    Timmis, K.M.3
  • 36
    • 0028987604 scopus 로고
    • A "minimal essential Mhc" and an "unrecognized Mhc": Two extremes in selection for polymorphism
    • Kaufman, J., H. Völk, and H.-J. Wallny. 1995. A "minimal essential Mhc" and an "unrecognized Mhc": two extremes in selection for polymorphism. Immunol. Rev. 143:63-88.
    • (1995) Immunol. Rev. , vol.143 , pp. 63-88
    • Kaufman, J.1    Völk, H.2    Wallny, H.-J.3
  • 37
    • 0026716529 scopus 로고
    • A major oligomeric fibroblast proteoglycan identified as a novel large form of type-XII collagen
    • Koch, M., C. Bernasconi, and M. Chiquet. 1992. A major oligomeric fibroblast proteoglycan identified as a novel large form of type-XII collagen. Eur. J. Biochem. 207:847-856.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 847-856
    • Koch, M.1    Bernasconi, C.2    Chiquet, M.3
  • 38
    • 0029093272 scopus 로고
    • Large and small splice variants of collagen XII: Differential expression and ligand binding
    • Koch, M., B. Bohrmann, M. Matthison, C. Hagios, B. Trueb, and M. Chiquet. 1995. Large and small splice variants of collagen XII: Differential expression and ligand binding. J. Cell Biol. 130:1005-1014.
    • (1995) J. Cell Biol. , vol.130 , pp. 1005-1014
    • Koch, M.1    Bohrmann, B.2    Matthison, M.3    Hagios, C.4    Trueb, B.5    Chiquet, M.6
  • 39
    • 0026705722 scopus 로고
    • Extracellular matrix protein tenascin-like gene found in human MHC class III region
    • Matsumoto, K.-I., N. Ishihara, A. Ando, H. Inoko, and T. Ikemura. 1992. Extracellular matrix protein tenascin-like gene found in human MHC class III region. Immunogenetics. 36:400-403.
    • (1992) Immunogenetics , vol.36 , pp. 400-403
    • Matsumoto, K.-I.1    Ishihara, N.2    Ando, A.3    Inoko, H.4    Ikemura, T.5
  • 40
    • 0028353447 scopus 로고
    • The distribution of tenascin-X is distinct and often reciprocal to that of tenascin-C
    • Matsumoto, K.-I., Y. Saga, T. Ikemura, T. Sakakura, and R. Chiquet-Ehrismann. 1994. The distribution of tenascin-X is distinct and often reciprocal to that of tenascin-C. J. Cell Biol. 125:483-493.
    • (1994) J. Cell Biol. , vol.125 , pp. 483-493
    • Matsumoto, K.-I.1    Saga, Y.2    Ikemura, T.3    Sakakura, T.4    Chiquet-Ehrismann, R.5
  • 42
    • 0009313254 scopus 로고
    • The Aorta, J. Lindsay, Jr. and J.W. Hurst, editors. Grune and Stratton, New York
    • Morse, D.E. 1979. Embryology, anatomy, and histology of the aorta. In The Aorta, J. Lindsay, Jr. and J.W. Hurst, editors. Grune and Stratton, New York. 15-37.
    • (1979) Embryology, Anatomy, and Histology of the Aorta. , pp. 15-37
    • Morse, D.E.1
  • 43
    • 0026321941 scopus 로고
    • Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin
    • Murphy-Ullrich, J.E., V.A. Lightner, I. Aukhil, Y.Z. Yan, H.P. Erickson, and M. Höök. 1991. Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J. Cell Biol. 115:1127-1136.
    • (1991) J. Cell Biol. , vol.115 , pp. 1127-1136
    • Murphy-Ullrich, J.E.1    Lightner, V.A.2    Aukhil, I.3    Yan, Y.Z.4    Erickson, H.P.5    Höök, M.6
  • 44
    • 0026633247 scopus 로고
    • The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs
    • Nörenberg, U., H. Wille, J.M. Wolff, R. Frank, and F.G. Rathjen. 1992. The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron. 8:849-863.
    • (1992) Neuron , vol.8 , pp. 849-863
    • Nörenberg, U.1    Wille, H.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 45
    • 0025874185 scopus 로고
    • Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes
    • Otto, E., M. Kunimoto, T. McLaughlin, and V. Bennett. 1991. Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes. J. Cell Biol. 114:241-253.
    • (1991) J. Cell Biol. , vol.114 , pp. 241-253
    • Otto, E.1    Kunimoto, M.2    McLaughlin, T.3    Bennett, V.4
  • 46
    • 0020446736 scopus 로고
    • Coiled-coils in α-helix containing proteins: Analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins
    • Parry, D.A.D. 1982. Coiled-coils in α-helix containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci. Rep. 2:1017-1024.
    • (1982) Biosci. Rep. , vol.2 , pp. 1017-1024
    • Parry, D.A.D.1
  • 47
    • 13244292544 scopus 로고
    • Modular exchange principles in proteins
    • Patthy, L. 1991. Modular exchange principles in proteins. Curr. Opin. Struct. Biol. 1:351-361.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 351-361
    • Patthy, L.1
  • 48
    • 0024424947 scopus 로고
    • J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion
    • Pesheva, P., E. Spiess, and M. Schachner. 1989. J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion. J. Cell Biol. 109: 1765-1778.
    • (1989) J. Cell Biol. , vol.109 , pp. 1765-1778
    • Pesheva, P.1    Spiess, E.2    Schachner, M.3
  • 49
    • 0026732724 scopus 로고
    • Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin
    • Prieto, A.L., C. Andersson-Fisone, and K.L. Crossin. 1992. Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin. J. Cell Biol. 119:663-678.
    • (1992) J. Cell Biol. , vol.119 , pp. 663-678
    • Prieto, A.L.1    Andersson-Fisone, C.2    Crossin, K.L.3
  • 50
    • 0025744729 scopus 로고
    • Restrictin: A chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecules F11
    • Rathjen, F.G., J.M. Wolff, and R. Chiquet-Ehrismann. 1991. Restrictin: a chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecules F11. Development (Camb.). 113:151-164.
    • (1991) Development (Camb.) , vol.113 , pp. 151-164
    • Rathjen, F.G.1    Wolff, J.M.2    Chiquet-Ehrismann, R.3
  • 51
    • 0004145665 scopus 로고
    • The Macmillan Company, New York.
    • Romanoff, A.L. 1960. The avian embryo. The Macmillan Company, New York. 681-780.
    • (1960) The Avian Embryo , pp. 681-780
    • Romanoff, A.L.1
  • 54
    • 0028704499 scopus 로고
    • The perplexing multifunctionality of janusin, a tenascin-related molecule
    • Schachner, M., J. Taylor, U. Bartsch, and P. Pesheva. 1994. The perplexing multifunctionality of janusin, a tenascin-related molecule. Perspect. Dev. Neurobiol. 2:33-41.
    • (1994) Perspect. Dev. Neurobiol. , vol.2 , pp. 33-41
    • Schachner, M.1    Taylor, J.2    Bartsch, U.3    Pesheva, P.4
  • 55
    • 0024347096 scopus 로고
    • Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments
    • Spring, J., K. Beck, and R. Chiquet-Ehrismann. 1989. Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments. Cell. 59:325-334.
    • (1989) Cell , vol.59 , pp. 325-334
    • Spring, J.1    Beck, K.2    Chiquet-Ehrismann, R.3
  • 56
    • 0023951297 scopus 로고
    • Molecular and cellular biology of intermediate filaments
    • Steinert, P.M., and D.R. Roop. 1988. Molecular and cellular biology of intermediate filaments. Annu. Rev. Biochem. 57:593-625.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 57
    • 0026450768 scopus 로고
    • Myogenic cell lineages
    • Stockdale, F.E. 1992. Myogenic cell lineages. Dev. Biol. 154:284-298.
    • (1992) Dev. Biol. , vol.154 , pp. 284-298
    • Stockdale, F.E.1
  • 58
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Rev 14:4683-4690.
    • (1986) Nucleic Acids Rev , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 60
    • 0025060893 scopus 로고
    • Isolation of the chicken middle-molecular weight neurofilament (NF-M) gene and characterization of its promotor
    • Zopf, D., B. Dineva, H. Betz, and E.D. Gundelfinger. 1990. Isolation of the chicken middle-molecular weight neurofilament (NF-M) gene and characterization of its promotor. Nucleic Acids Res. 18:521-529.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 521-529
    • Zopf, D.1    Dineva, B.2    Betz, H.3    Gundelfinger, E.D.4


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