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Volumn 110, Issue 5, 1997, Pages 611-621

Ca2+-dependent interaction of S100A2 with muscle and nonmuscle tropomyosins

Author keywords

Binding; Cross linking; Localization; S100A2; Tropomyosin

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; MONOCLONAL ANTIBODY; PROTEIN S 100; TROPOMYOSIN;

EID: 0030944326     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (31)

References (69)
  • 1
    • 0023898362 scopus 로고
    • Gene encoding the β subunit of S100 protein is on chromosome 21: Implications for Down syndrome
    • Allore, R., O'Hanlon, D., Price, R., Neilson, K., Willard, H. F., Cox, D. R., Marks, A. and Dunn, R. J. (1988). Gene encoding the β subunit of S100 protein is on chromosome 21: implications for Down syndrome. Science 239, 1311-1313.
    • (1988) Science , vol.239 , pp. 1311-1313
    • Allore, R.1    O'Hanlon, D.2    Price, R.3    Neilson, K.4    Willard, H.F.5    Cox, D.R.6    Marks, A.7    Dunn, R.J.8
  • 2
    • 0029086637 scopus 로고
    • Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts
    • Amieva, M. R. and Furthmayr, H. (1995). Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts. Exp. Cell Res. 219, 180-196.
    • (1995) Exp. Cell Res. , vol.219 , pp. 180-196
    • Amieva, M.R.1    Furthmayr, H.2
  • 3
    • 0026463640 scopus 로고
    • Disulfide-linked S100β dimers and signal transduction
    • Barger, S. W., Wolchok, S. R. and Van Eldik, L. J. (1992). Disulfide-linked S100β dimers and signal transduction. Biochim. Biophys. Acta 1160, 105-112.
    • (1992) Biochim. Biophys. Acta , vol.1160 , pp. 105-112
    • Barger, S.W.1    Wolchok, S.R.2    Van Eldik, L.J.3
  • 4
    • 0023022739 scopus 로고
    • Ions binding to S100 proteins
    • Baudier, J. and Gerard, D. (1986). Ions binding to S100 proteins. J. Biol. Chem. 261, 8204-8212.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8204-8212
    • Baudier, J.1    Gerard, D.2
  • 6
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge, M. J. (1993). Inositol trisphosphate and calcium signalling. Nature 361, 315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 7
    • 0029314844 scopus 로고
    • Calcium signalling and cell proliferation
    • Berridge, M. J. (1995). Calcium signalling and cell proliferation. BioEssays 17, 491-500.
    • (1995) BioEssays , vol.17 , pp. 491-500
    • Berridge, M.J.1
  • 8
    • 0028834424 scopus 로고
    • The elemental principles of calcium signalling
    • Bootman, M. D. and Berridge, M. J. (1995). The elemental principles of calcium signalling. Cell 83, 675-678.
    • (1995) Cell , vol.83 , pp. 675-678
    • Bootman, M.D.1    Berridge, M.J.2
  • 9
    • 0023139873 scopus 로고
    • Tropomyosin distinguishes between two actin-binding sites of villin and affects actin-binding properties of brush border proteins
    • Burgess, D. R., Broschat, K. O. and Hayden, J. M. (1987). Tropomyosin distinguishes between two actin-binding sites of villin and affects actin-binding properties of brush border proteins. J. Cell Biol. 104, 29-40.
    • (1987) J. Cell Biol. , vol.104 , pp. 29-40
    • Burgess, D.R.1    Broschat, K.O.2    Hayden, J.M.3
  • 10
    • 0022993464 scopus 로고
    • Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein
    • Calabretta, B., Battinin, R., Kazcmarek, L., de Riel, J. and Baserga, R. (1986). Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein. J. Biol. Chem. 261, 12628-12632.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12628-12632
    • Calabretta, B.1    Battinin, R.2    Kazcmarek, L.3    De Riel, J.4    Baserga, R.5
  • 11
    • 0023268438 scopus 로고
    • Suppression of synthesis and utilization of tropomyosin in mouse and rat fibroblasts by transforming growth factor α: A pathway in oncogene action
    • Cooper, H. L., Battacharya, B., Bassin, R. H. and Salomon, D. S. (1987). Suppression of synthesis and utilization of tropomyosin in mouse and rat fibroblasts by transforming growth factor α: a pathway in oncogene action. Cancer Res. 47, 4493-4500.
    • (1987) Cancer Res. , vol.47 , pp. 4493-4500
    • Cooper, H.L.1    Battacharya, B.2    Bassin, R.H.3    Salomon, D.S.4
  • 12
    • 0025939163 scopus 로고
    • Perspectives in S-100 protein biology
    • Donato, R. (1991). Perspectives in S-100 protein biology. Cell Calcium 12, 713-726.
    • (1991) Cell Calcium , vol.12 , pp. 713-726
    • Donato, R.1
  • 13
    • 0027203055 scopus 로고
    • Six S100 genes are clustered on human chromosome 1q21: Identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E
    • Engelkamp, D., Schäfer, B. W., Mattei, M. G., Erne, P. and Heizmann, C. W. (1993). Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. Proc. Nat. Acad. Sci. USA 90, 6547-6551.
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 6547-6551
    • Engelkamp, D.1    Schäfer, B.W.2    Mattei, M.G.3    Erne, P.4    Heizmann, C.W.5
  • 14
    • 0028828236 scopus 로고
    • Calcium sparks in vascular smooth muscle: Relaxation regulators
    • Fay, F. S. (1995). Calcium sparks in vascular smooth muscle: relaxation regulators. Science 270, 588-589.
    • (1995) Science , vol.270 , pp. 588-589
    • Fay, F.S.1
  • 15
    • 0028147089 scopus 로고
    • Expression of intracellular calcium-binding proteins in cultured skin fibroblasts from alzheimer and normal aged donors
    • Föhr, U. G., Gibson, G. E., Tofel-Grehl, B., Schäfer, B. W. and Heizmann, C. W. (1994). Expression of intracellular calcium-binding proteins in cultured skin fibroblasts from alzheimer and normal aged donors. Biochim. Biophys. Acta 1223, 391-397.
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 391-397
    • Föhr, U.G.1    Gibson, G.E.2    Tofel-Grehl, B.3    Schäfer, B.W.4    Heizmann, C.W.5
  • 16
    • 0025190320 scopus 로고
    • Calcium-dependent control of caldesmon-actin interaction by S100
    • Fujii, T., Machino, K., Andoh, H., Satoh, T. and Kondo, Y. (1990). Calcium-dependent control of caldesmon-actin interaction by S100. J. Biochem. 107, 133-137.
    • (1990) J. Biochem. , vol.107 , pp. 133-137
    • Fujii, T.1    Machino, K.2    Andoh, H.3    Satoh, T.4    Kondo, Y.5
  • 17
    • 0027991511 scopus 로고
    • Calcium-dependent regulation of smooth muscle calponin by S100
    • Fujii, T., Oomatsuzawa, A., Kuzumaki, N. and Kondo, Y. (1994). Calcium-dependent regulation of smooth muscle calponin by S100. J. Biochem. 116, 121-127.
    • (1994) J. Biochem. , vol.116 , pp. 121-127
    • Fujii, T.1    Oomatsuzawa, A.2    Kuzumaki, N.3    Kondo, Y.4
  • 18
    • 0020971322 scopus 로고
    • Quantitative two-dimensional gel electrophoresis of proteins
    • Garrels, J. I. (1983). Quantitative two-dimensional gel electrophoresis of proteins. Meth. Enzymol. 100, 411-423.
    • (1983) Meth. Enzymol. , vol.100 , pp. 411-423
    • Garrels, J.I.1
  • 19
    • 0021943945 scopus 로고
    • Calcium-dependent conformational changes in the 36-kDa subunit of intestinal protein 1 related to the cellular 36-kDa target of Rous sarcoma virus tyrosine kinase
    • Gerke, V. and Weber, K. (1985a). Calcium-dependent conformational changes in the 36-kDa subunit of intestinal protein 1 related to the cellular 36-kDa target of Rous sarcoma virus tyrosine kinase. J. Biol. Chem. 260, 1688-1695.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1688-1695
    • Gerke, V.1    Weber, K.2
  • 20
    • 0022157945 scopus 로고
    • The regulatory chain in the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the S-100 protein of glial cells
    • Gerke, V. and Weber, K. (1985b). The regulatory chain in the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the S-100 protein of glial cells. EMBO J. 4, 2917-2920.
    • (1985) EMBO J. , vol.4 , pp. 2917-2920
    • Gerke, V.1    Weber, K.2
  • 21
    • 0028284396 scopus 로고
    • Interactions in vitro of p9Ka, the rat S-100-related, metastasis-inducing, calcium-binding protein
    • Gibbs, F. E. M., Wilkinson, M. C., Rudland, P. S. and Barraclough, A. (1994). Interactions in vitro of p9Ka, the rat S-100-related, metastasis-inducing, calcium-binding protein. J. Biol. Chem. 269, 18992-18999.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18992-18999
    • Gibbs, F.E.M.1    Wilkinson, M.C.2    Rudland, P.S.3    Barraclough, A.4
  • 24
    • 0028822231 scopus 로고
    • Specificity of dimer formation in tropomyosins: Influence of alternatively spliced exons on homodimer and heterodimer assembly
    • Gimona, M., Watakabe, A. and Helfman, D.M. (1995). Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly. Proc. Nat. Acad. Sci. USA 92, 9776-9780.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 9776-9780
    • Gimona, M.1    Watakabe, A.2    Helfman, D.M.3
  • 25
    • 0002750064 scopus 로고    scopus 로고
    • Calponin
    • (ed. M. Barany), Academic Press
    • Gimona, M. and Small, J.V. (1996). Calponin. In Smooth Muscle Biochemistry (ed. M. Barany), pp. 91-103. Academic Press.
    • (1996) Smooth Muscle Biochemistry , pp. 91-103
    • Gimona, M.1    Small, J.V.2
  • 26
    • 0001171815 scopus 로고
    • Amino-terminal sequence of p36 and associated p10: Identification of the site of tyrosine phosphorylation and homology with S-100
    • Glenney, J. R. Jr and Tack, B. (1985). Amino-terminal sequence of p36 and associated p10: identification of the site of tyrosine phosphorylation and homology with S-100. Proc. Nat. Acad. Sci. USA 82, 7884-7888.
    • (1985) Proc. Nat. Acad. Sci. USA , vol.82 , pp. 7884-7888
    • Glenney J.R., Jr.1    Tack, B.2
  • 27
    • 0024593613 scopus 로고
    • Isolation of a new member of the S100 protein family: Amino acid sequence, tissue, and subcellular distribution
    • Glenney, J. R. Jr. Kindy, M. S. and Zokas, L. (1989). Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution. J. Cell Biol. 108, 569-578.
    • (1989) J. Cell Biol. , vol.108 , pp. 569-578
    • Glenney J.R., Jr.1    Kindy, M.S.2    Zokas, L.3
  • 29
    • 0025978546 scopus 로고
    • Intracellular calcium-binding proteins: More sights than insights
    • Heizmann, C. W. and Hunziker, W. (1991), Intracellular calcium-binding proteins: more sights than insights. Trends Biochem. Sci. 16, 98-103.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 98-103
    • Heizmann, C.W.1    Hunziker, W.2
  • 30
    • 0030032040 scopus 로고    scopus 로고
    • Calcium binding and conformational response in EF-hand proteins
    • Ikura, M. (1996). Calcium binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21, 14-17.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 14-17
    • Ikura, M.1
  • 31
    • 0028678827 scopus 로고
    • Calcium-Binding Proteins 1: EF-hands
    • Kawasaki, H. and Kretsinger, R.H. (1994). Calcium-Binding Proteins 1: EF-hands. Protein Profile 1, 343-517.
    • (1994) Protein Profile , vol.1 , pp. 343-517
    • Kawasaki, H.1    Kretsinger, R.H.2
  • 34
    • 0026607123 scopus 로고
    • Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment
    • Lee, S. W., Tomasetto, C., Swisshelm, K., Keyomarsi, K. and Sager, R. (1992). Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment. Proc. Nat. Acad. Sci. USA 89, 2504-2508.
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , pp. 2504-2508
    • Lee, S.W.1    Tomasetto, C.2    Swisshelm, K.3    Keyomarsi, K.4    Sager, R.5
  • 35
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller, J. P. and Helfman, D.M. (1991). The molecular basis for tropomyosin isoform diversity. BioEssays 13, 429-437.
    • (1991) BioEssays , vol.13 , pp. 429-437
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 36
    • 0020048612 scopus 로고
    • Lack of tropomyosin correlates with the absence of stress fibers in transformed rat kidney cells
    • Leonardi, C. L., Warren, R. H. and Rubin, R. W. (1982). Lack of tropomyosin correlates with the absence of stress fibers in transformed rat kidney cells. Biochim. Biophys. Acta 720, 154-162.
    • (1982) Biochim. Biophys. Acta , vol.720 , pp. 154-162
    • Leonardi, C.L.1    Warren, R.H.2    Rubin, R.W.3
  • 38
    • 0023071607 scopus 로고
    • Isolation and spectroscopic analyses of S-100 proteins and their interactions with metal ions
    • Mani, R. S. and Kay, C. M. (1987). Isolation and spectroscopic analyses of S-100 proteins and their interactions with metal ions. Meth. Enzymol. 139, 168-187.
    • (1987) Meth. Enzymol. , vol.139 , pp. 168-187
    • Mani, R.S.1    Kay, C.M.2
  • 39
    • 0025162271 scopus 로고
    • 2+-binding protein from smooth muscle
    • 2+-binding protein from smooth muscle. Biochemistry 29, 1398-1404.
    • (1990) Biochemistry , vol.29 , pp. 1398-1404
    • Mani, R.S.1    Kay, C.M.2
  • 40
    • 0027441188 scopus 로고
    • Calcium-dependent regulation of the caldesmon-heavy meromyosin interaction by caltropin
    • Mani, R. S. and Kay, C. M. (1993). Calcium-dependent regulation of the caldesmon-heavy meromyosin interaction by caltropin. Biochemistry 32, 11217-11223.
    • (1993) Biochemistry , vol.32 , pp. 11217-11223
    • Mani, R.S.1    Kay, C.M.2
  • 41
    • 0025472547 scopus 로고
    • S100 proteins and Down syndrome
    • Marks, A., and Allore, R. (1990). S100 proteins and Down syndrome. BioEssays 12, 381-383.
    • (1990) BioEssays , vol.12 , pp. 381-383
    • Marks, A.1    Allore, R.2
  • 42
    • 0013844612 scopus 로고
    • A soluble protein characteristic of the nervous system
    • Moore, B. E. (1965). A soluble protein characteristic of the nervous system. Biochem. Biophys. Res. Commun. 19, 739-744.
    • (1965) Biochem. Biophys. Res. Commun. , vol.19 , pp. 739-744
    • Moore, B.E.1
  • 44
    • 0028086183 scopus 로고
    • Metastasis-associated mts 1 gene expression correlates with increased p53 detection in the B16 murine melanoma
    • Parker, C., Lakshmi, M. S., Piura, B. and Sherbet, G. V. (1994a). Metastasis-associated mts 1 gene expression correlates with increased p53 detection in the B16 murine melanoma. DNA Cell Biol. 13, 343-351.
    • (1994) DNA Cell Biol. , vol.13 , pp. 343-351
    • Parker, C.1    Lakshmi, M.S.2    Piura, B.3    Sherbet, G.V.4
  • 45
    • 0028170642 scopus 로고
    • Induction of 18A2/mts 1 gene expression and its effects on metastasis and cell cycle control
    • Parker, C., Whittaker, P. A., Usmani, B. A., Lakshmi, M. S. and Sherbet, G. V. (1994b). Induction of 18A2/mts 1 gene expression and its effects on metastasis and cell cycle control. DNA Cell Biol. 13, 1021-1028.
    • (1994) DNA Cell Biol. , vol.13 , pp. 1021-1028
    • Parker, C.1    Whittaker, P.A.2    Usmani, B.A.3    Lakshmi, M.S.4    Sherbet, G.V.5
  • 46
    • 0027133538 scopus 로고
    • Evaluation of storage Phosphor Imaging for quantitative analysis of 2D gels using the QUEST II system
    • Patterson, S. D. and Latter, G. I. (1993). Evaluation of storage Phosphor Imaging for quantitative analysis of 2D gels using the QUEST II system. BioTechniques 15, 1076-1083.
    • (1993) BioTechniques , vol.15 , pp. 1076-1083
    • Patterson, S.D.1    Latter, G.I.2
  • 48
    • 0028246569 scopus 로고
    • Purification and characterization of recombinant human calcium-binding S100 proteins CAPL and CACY
    • Pedrocchi, M., Schäfer, B. W., Durussel, I. Cox, J. A. and Heizmann, C. W. (1994b). Purification and characterization of recombinant human calcium-binding S100 proteins CAPL and CACY. Biochemistry 33, 6732-6738.
    • (1994) Biochemistry , vol.33 , pp. 6732-6738
    • Pedrocchi, M.1    Schäfer, B.W.2    Durussel, I.3    Cox, J.A.4    Heizmann, C.W.5
  • 49
    • 0026713920 scopus 로고
    • In vitro and in vivo characterization of four fibroblast tropomyosins produced in bacteria: TM-2, TM-3, TM-5a and TM-5b are co-localized in interphase fibroblasts
    • Pittenger, M. F. and Helfman, D.M. (1992). In vitro and in vivo characterization of four fibroblast tropomyosins produced in bacteria: TM-2, TM-3, TM-5a and TM-5b are co-localized in interphase fibroblasts. J. Cell Biol. 118, 841-858.
    • (1992) J. Cell Biol. , vol.118 , pp. 841-858
    • Pittenger, M.F.1    Helfman, D.M.2
  • 50
    • 0029091378 scopus 로고
    • Alternatively spliced exons in the β tropomyosin gene exhibit different affinities for F-uctin and effects with nonmuscle caldesmon
    • Pittenger, M. F., Kistler, A. and Helfman, D. M. (1995). Alternatively spliced exons in the β tropomyosin gene exhibit different affinities for F-uctin and effects with nonmuscle caldesmon. J. Cell Sci. 108, 3253-3265.
    • (1995) J. Cell Sci. , vol.108 , pp. 3253-3265
    • Pittenger, M.F.1    Kistler, A.2    Helfman, D.M.3
  • 51
    • 0027240578 scopus 로고
    • Expression of transduced tropomyosin 1 cDNA suppresses neoplastic growth of cells transformed by the ras oncogene
    • Prasad, G. L., Fuldner, R. A. and Cooper, H. L. (1993). Expression of transduced tropomyosin 1 cDNA suppresses neoplastic growth of cells transformed by the ras oncogene. Proc. Nat. Acad. Sci. USA 90, 7039-1043.
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 7039-11043
    • Prasad, G.L.1    Fuldner, R.A.2    Cooper, H.L.3
  • 52
    • 0027999172 scopus 로고
    • Increased coexpression of CTFR and S100 calcium binding proteins MRP8 and MRP14 mRNAs in cystic fibrosis human tracheal gland
    • Renaud, W., Merten, M. and Figarella, C. (1994). Increased coexpression of CTFR and S100 calcium binding proteins MRP8 and MRP14 mRNAs in cystic fibrosis human tracheal gland. Biochem. Biophys. Res. Commun. 201, 1518-1525.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 1518-1525
    • Renaud, W.1    Merten, M.2    Figarella, C.3
  • 53
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schäfer, B. W. and Heizmann, C. W. (1996) The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biochem. Sci. 21, 134-140.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 134-140
    • Schäfer, B.W.1    Heizmann, C.W.2
  • 54
    • 0028173033 scopus 로고
    • S100β protein expression in alzheimer disease: Potential role in the pathogenesis of neuritic plaques
    • Sheng, J. G., Mrak, R. E. and Griffin, W. S. T. (1994). S100β protein expression in alzheimer disease: potential role in the pathogenesis of neuritic plaques. J. Neurosci. Res. 39, 398-404.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 398-404
    • Sheng, J.G.1    Mrak, R.E.2    Griffin, W.S.T.3
  • 56
    • 84988058290 scopus 로고
    • Urea-glycerol-acrylamide gel electrophoresis of acidic low molecular weight muscle proteins: Rapid determination of myosin light chain phosphorylation in myosin, actomyosin and whole muscle samples
    • Sobieszek, A. and Jertschin, P. (1986). Urea-glycerol-acrylamide gel electrophoresis of acidic low molecular weight muscle proteins: Rapid determination of myosin light chain phosphorylation in myosin, actomyosin and whole muscle samples. Electrophoresis 7, 417-425.
    • (1986) Electrophoresis , vol.7 , pp. 417-425
    • Sobieszek, A.1    Jertschin, P.2
  • 57
    • 0028072007 scopus 로고
    • Restoration of microfilament bundle organization in v-raf-transformed NRK cells after transduction with tropomyosin 2 cDNA
    • Takenaga, K. and Masuda, A. (1994). Restoration of microfilament bundle organization in v-raf-transformed NRK cells after transduction with tropomyosin 2 cDNA. Cancer Lett. 87, 47-53.
    • (1994) Cancer Lett. , vol.87 , pp. 47-53
    • Takenaga, K.1    Masuda, A.2
  • 58
    • 0024203908 scopus 로고
    • Suppression of synthesis of tropomyosin isoform 2 in metastatic v-Ha-ras-transformed NIH 3T3 cells
    • Takenaga, K., Nakamura, Y. and Sakiyama, S. (1988). Suppression of synthesis of tropomyosin isoform 2 in metastatic v-Ha-ras-transformed NIH 3T3 cells. Biochem. Biophys. Res. Commun. 157, 1111-1116.
    • (1988) Biochem. Biophys. Res. Commun. , vol.157 , pp. 1111-1116
    • Takenaga, K.1    Nakamura, Y.2    Sakiyama, S.3
  • 59
    • 0027931271 scopus 로고
    • Expression of a calcium binding protein, pEL98 (MTS1) during differentiation of human promyelocytic leukemia HL-60 cells
    • Takenaga, K., Nakamura, Y. and Sakiyama, S. (1994a). Expression of a calcium binding protein, pEL98 (MTS1) during differentiation of human promyelocytic leukemia HL-60 cells. Biochem. Biophys. Res. Commun. 202, 94-101.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 94-101
    • Takenaga, K.1    Nakamura, Y.2    Sakiyama, S.3
  • 60
    • 0028305678 scopus 로고
    • Cellular localization of pEL98 protein, an S100-related calcium binding protein, in fibroblasts and its tissue distribution analyzed by monoclonal antibodies
    • Takenaga, K., Nakamura, Y. and Sakiyama, S. (1994b). Cellular localization of pEL98 protein, an S100-related calcium binding protein, in fibroblasts and its tissue distribution analyzed by monoclonal antibodies. Cell Struct. Funct. 19, 133-141.
    • (1994) Cell Struct. Funct. , vol.19 , pp. 133-141
    • Takenaga, K.1    Nakamura, Y.2    Sakiyama, S.3
  • 61
    • 0028329819 scopus 로고
    • Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin
    • Takenaga, K., Nakamura, Y., Sakiyama, S., Hasegawa, Y., Sato, K. and Endo, H. (1994c). Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin. J. Cell Biol. 124, 757-768.
    • (1994) J. Cell Biol. , vol.124 , pp. 757-768
    • Takenaga, K.1    Nakamura, Y.2    Sakiyama, S.3    Hasegawa, Y.4    Sato, K.5    Endo, H.6
  • 62
    • 0028070116 scopus 로고
    • Involvement of S100-related protein pEL98 (or mts1) in cell motility and tumor invasion
    • Takenaga, K., Nakamura, Y., Endo, H. and Sakiyama, S. (1994d). Involvement of S100-related protein pEL98 (or mts1) in cell motility and tumor invasion. Jpn J. Cancer Res. 85, 831-839.
    • (1994) Jpn J. Cancer Res. , vol.85 , pp. 831-839
    • Takenaga, K.1    Nakamura, Y.2    Endo, H.3    Sakiyama, S.4
  • 63
    • 0025844894 scopus 로고
    • Inducible expression of calcyclin, a gene with strong homology to S-100 protein, during neuroblastoma cell differentiation and its prevalent expression in Schwann-like cell lines
    • Tonini, G. P., Casalaro, A., Cara, A. and Di Martino, D. (1991). Inducible expression of calcyclin, a gene with strong homology to S-100 protein, during neuroblastoma cell differentiation and its prevalent expression in Schwann-like cell lines. Cancer Res. 51, 1733-1737.
    • (1991) Cancer Res. , vol.51 , pp. 1733-1737
    • Tonini, G.P.1    Casalaro, A.2    Cara, A.3    Di Martino, D.4
  • 64
    • 0028999850 scopus 로고
    • Gene expression and protein localisation of calcyclin, a calcium-binding protein of the S-100 family in fresh neuroblastomas
    • Tonini, G. P., Fabretti, G., Kuznicki, J., Massimo, L., Scaruffi, P., Brisigotti, M. and Mazzocco, K. (1995). Gene expression and protein localisation of calcyclin, a calcium-binding protein of the S-100 family in fresh neuroblastomas. Eur. J. Cancer 31 A, 499-504.
    • (1995) Eur. J. Cancer , vol.31 A , pp. 499-504
    • Tonini, G.P.1    Fabretti, G.2    Kuznicki, J.3    Massimo, L.4    Scaruffi, P.5    Brisigotti, M.6    Mazzocco, K.7
  • 65
    • 0028102425 scopus 로고
    • S100β expression in Alzheimer's disease: Relation to neuropathology in brain regions
    • Van Eldik, L. J. and Griffin, W. S. T. (1994). S100β expression in Alzheimer's disease: relation to neuropathology in brain regions. Biochim. Biophys. Acta 1223, 398-403.
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 398-403
    • Van Eldik, L.J.1    Griffin, W.S.T.2
  • 66
    • 0027536846 scopus 로고
    • Characterization of the smooth muscle calponin and calmodulin complex
    • Wills, F. L., McCubbin, W. D. and Kay, C. M. (1993). Characterization of the smooth muscle calponin and calmodulin complex. Biochemistry 32, 2321-2328.
    • (1993) Biochemistry , vol.32 , pp. 2321-2328
    • Wills, F.L.1    McCubbin, W.D.2    Kay, C.M.3
  • 67
    • 0028287716 scopus 로고
    • Smooth muscle calponin-caltropin interaction: Effects on biological activity and stability of calponin
    • Wills, F. L., McCubbin, W. D. and Kay, C. M. (1994a). Smooth muscle calponin-caltropin interaction: effects on biological activity and stability of calponin. Biochemistry 33, 5562-5569.
    • (1994) Biochemistry , vol.33 , pp. 5562-5569
    • Wills, F.L.1    McCubbin, W.D.2    Kay, C.M.3
  • 68
    • 0028584314 scopus 로고
    • Two domains of interaction with calcium binding proteins can be mapped using fragments of calponin
    • Wills, F. L., McCubbin, W. D., Gimona, M., Strasser, P. and Kay, C. M. (1994b). Two domains of interaction with calcium binding proteins can be mapped using fragments of calponin. Protein Sci. 3, 2311-2321.
    • (1994) Protein Sci. , vol.3 , pp. 2311-2321
    • Wills, F.L.1    McCubbin, W.D.2    Gimona, M.3    Strasser, P.4    Kay, C.M.5
  • 69
    • 0024583495 scopus 로고
    • Analysis of the calcium-modulating proteins, S100 and calmodulin, and their target proteins during C6 glioma cell differentiation
    • Zimmer, D. B. and Van Eldik, L. J. (1989). Analysis of the calcium-modulating proteins, S100 and calmodulin, and their target proteins during C6 glioma cell differentiation. J. Cell Biol. 108, 141-151.
    • (1989) J. Cell Biol. , vol.108 , pp. 141-151
    • Zimmer, D.B.1    Van Eldik, L.J.2


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