메뉴 건너뛰기




Volumn 32, Issue 5-6, 2002, Pages 269-278

Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALNEXIN; CALRETICULIN; CHAPERONE; GLOBULAR PROTEIN; GLYCOPROTEIN; HEAT SHOCK PROTEIN 47; MEMBRANE PROTEIN; CALCIUM BINDING PROTEIN;

EID: 0036877146     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0143416002001884     Document Type: Review
Times cited : (390)

References (88)
  • 1
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • Baumann O, Walz B. Endoplasmic reticulum of animal cells and its organization into structural and functional domains. Int Rev Cytol 2001; 205: 149-214.
    • (2001) Int. Rev. Cytol. , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 3
    • 0028965533 scopus 로고
    • Molecular chaperones in antigen presentation
    • Williams DB, Watts TH. Molecular chaperones in antigen presentation. Curr Opin Immunol 1995; 7: 77-84.
    • (1995) Curr. Opin. Immunol. , vol.7 , pp. 77-84
    • Williams, D.B.1    Watts, T.H.2
  • 5
    • 0033200131 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum: Lessons from hereditary myeloperoxidase deficiency
    • Nauseef WM. Quality control in the endoplasmic reticulum: lessons from hereditary myeloperoxidase deficiency. J Lab Clin Med 1999; 134: 215-221.
    • (1999) J. Lab. Clin. Med. , vol.134 , pp. 215-221
    • Nauseef, W.M.1
  • 6
    • 0034235397 scopus 로고    scopus 로고
    • Calcium, a signaling molecule in the endoplasmic reticulum?
    • Corbett EF, Michalak M. Calcium, a signaling molecule in the endoplasmic reticulum? Trends Biochem Sci 2000; 25: 307-311.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 307-311
    • Corbett, E.F.1    Michalak, M.2
  • 7
    • 0032007324 scopus 로고    scopus 로고
    • Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96r
    • Nicchitta CV. Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96r. Curr Opin Immunol 1998; 10: 103-109.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 103-109
    • Nicchitta, C.V.1
  • 8
    • 0033525232 scopus 로고    scopus 로고
    • 2+ regulation of interactions between endoplasmic reticulum chaperones
    • 2+ regulation of interactions between endoplasmic reticulum chaperones. J Biol Chem 1999; 274: 6203-6211.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6203-6211
    • Corbett, E.F.1    Oikawa, K.2    Francois, P.3
  • 9
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • Molinari M, Helenius A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 2000; 288: 331-333.
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 10
    • 0034733916 scopus 로고    scopus 로고
    • Glycoprotein folding in the endoplasmic reticulum: A tale of three chaperones?
    • High S, Lecomte FJ, Russell SJ, Abell BM, Oliver JD. Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones? FEBS Lett 2000; 476: 38-41.
    • (2000) FEBS Lett. , vol.476 , pp. 38-41
    • High, S.1    Lecomte, F.J.2    Russell, S.J.3    Abell, B.M.4    Oliver, J.D.5
  • 12
    • 0033209269 scopus 로고    scopus 로고
    • Introduction: Molecular chaperones of the ER, their role in protein folding and genetic disease
    • Brooks DA. Introduction: molecular chaperones of the ER, their role in protein folding and genetic disease. Semin Cell Dev Biol 1999; 10: 441-442.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 441-442
    • Brooks, D.A.1
  • 13
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman MY, Goldberg AL. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 2001; 29: 15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 15
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth C, Koch GEL. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 1989; 59: 729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.E.L.2
  • 16
    • 0025313861 scopus 로고
    • Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum
    • Lodish HF, Kong N. Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J Biol Chem 1990; 265: 10893-10899.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10893-10899
    • Lodish, H.F.1    Kong, N.2
  • 17
    • 0026654505 scopus 로고
    • Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum
    • Lodish HF, Kong N, Wikstrom L. Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum. J Biol Chem 1992; 267: 12753-12760.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12753-12760
    • Lodish, H.F.1    Kong, N.2    Wikstrom, L.3
  • 18
    • 0032968164 scopus 로고    scopus 로고
    • Capacitative calcium entry channels
    • Putney Jr JW, McKay RR. Capacitative calcium entry channels. Bioessays 1999; 21: 38-46.
    • (1999) Bioessays , vol.21 , pp. 38-46
    • Putney J.W., Jr.1    McKay, R.R.2
  • 19
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
    • McCracken AA, Brodsky JL. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J Cell Biol 1996; 132: 291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 20
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: Reverse protein flow of no return
    • Sommer T, Wolf DH. Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J 1997; 11: 1227-1233.
    • (1997) FASEB J. , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 22
    • 0033485263 scopus 로고    scopus 로고
    • Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins
    • Saito Y, Ihara Y, Leach MR, Cohen-Doyle MF, Williams DB. Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J 1999; 18: 6718-6729.
    • (1999) EMBO J. , vol.18 , pp. 6718-6729
    • Saito, Y.1    Ihara, Y.2    Leach, M.R.3    Cohen-Doyle, M.F.4    Williams, D.B.5
  • 23
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A. Setting the standards: quality control in the secretory pathway. Science 1999; 286: 1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 24
    • 18444413218 scopus 로고    scopus 로고
    • E3 ubiquitin ligase that recognizes sugar chains
    • Yoshida Y, Chiba T, Tokunaga F et al. E3 ubiquitin ligase that recognizes sugar chains. Nature 2002; 418: 438-442.
    • (2002) Nature , vol.418 , pp. 438-442
    • Yoshida, Y.1    Chiba, T.2    Tokunaga, F.3
  • 26
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething MJ. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 1999; 10: 465-472.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 27
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou WJ, Cameron PH, Thomas DY, Bergeron JJM. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 1993; 364: 771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 28
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C, Braakman I, Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA 1994; 91: 913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 29
    • 0028932360 scopus 로고
    • The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
    • Ware FE, Vassilakos A, Peterson PA, Jackson MR, Lehrman MA, Williams DB. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J Biol Chem 1995; 270: 4697-4704.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4697-4704
    • Ware, F.E.1    Vassilakos, A.2    Peterson, P.A.3    Jackson, M.R.4    Lehrman, M.A.5    Williams, D.B.6
  • 30
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach MR, Cohen-Doyle MF, Thomas DY, Williams DB. Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J Biol Chem 2002; 277: 29686-29697.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29686-29697
    • Leach, M.R.1    Cohen-Doyle, M.F.2    Thomas, D.Y.3    Williams, D.B.4
  • 31
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc: Glycoprotein glucosyltransferase
    • Sousa MC, Ferrero-Garcia MA, Parodi AJ. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 1992; 31: 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 32
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver JD, van der Wal FJ, Bulleid NJ, High S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 1997; 275: 86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 33
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJM, Thomas DY. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem 1998; 273: 6009-6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.M.5    Thomas, D.Y.6
  • 35
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos A, Michalak M, Lehrman MA, Williams DB. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 1998; 37: 3480-3490.
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 36
    • 0033197741 scopus 로고    scopus 로고
    • Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
    • Ihara Y, Cohen-Doyle MF, Saito Y, Williams DB. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol Cell 1999; 4: 331-341.
    • (1999) Mol. Cell , vol.4 , pp. 331-341
    • Ihara, Y.1    Cohen-Doyle, M.F.2    Saito, Y.3    Williams, D.B.4
  • 37
    • 0034282386 scopus 로고    scopus 로고
    • The conformation of calreticulin is influenced by the endoplasmic reticulum lumenal environment
    • Corbett EF, Michalak KM, Oikawa K et al. The conformation of calreticulin is influenced by the endoplasmic reticulum lumenal environment. J Biol Chem 2000; 275: 27177-27185.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27177-27185
    • Corbett, E.F.1    Michalak, K.M.2    Oikawa, K.3
  • 39
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag JD, Bergeron JJM, Li Y et al. The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol Cell 2001; 8: 633-644.
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.M.2    Li, Y.3
  • 41
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein
    • Smith MJ, Koch GLE. Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J 1989; 8: 3581-3586.
    • (1989) EMBO J. , vol.8 , pp. 3581-3586
    • Smith, M.J.1    Koch, G.L.E.2
  • 42
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RAF, Michalak M. Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 1989; 264: 21522-21528.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21522-21528
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.F.4    Michalak, M.5
  • 44
    • 0025937289 scopus 로고
    • SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane
    • Wada I, Rindress D, Cameron PH et al. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J Biol Chem 1991; 266: 19599-19610.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19599-19610
    • Wada, I.1    Rindress, D.2    Cameron, P.H.3
  • 45
    • 0035802110 scopus 로고    scopus 로고
    • Functional specialization of calreticulin domains
    • Nakamura K, Zuppini A, Arnaudeau S et al. Functional specialization of calreticulin domains. J Cell Biol 2001; 154: 961-972.
    • (2001) J. Cell Biol. , vol.154 , pp. 961-972
    • Nakamura, K.1    Zuppini, A.2    Arnaudeau, S.3
  • 47
    • 0028141914 scopus 로고
    • ERcalcistorin/protein disulfide isomerase (PDI). Sequence determination and expression of a cDNA clone encoding a calcium storage protein with PDI activity from endoplasmic reticulum of the sea urchin egg
    • Lucero HA, Lebeche D, Kammer B. ERcalcistorin/protein disulfide isomerase (PDI). Sequence determination and expression of a cDNA clone encoding a calcium storage protein with PDI activity from endoplasmic reticulum of the sea urchin egg. J Biol Chem 1994; 269: 23112-23119.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23112-23119
    • Lucero, H.A.1    Lebeche, D.2    Kammer, B.3
  • 49
    • 0036467162 scopus 로고    scopus 로고
    • Thioredoxin and peptide methionine sulfoxide reductase: Convergence of similar structure and function in distinct structural folds
    • Gladyshev VN. Thioredoxin and peptide methionine sulfoxide reductase: convergence of similar structure and function in distinct structural folds. Proteins 2002; 46: 149-152.
    • (2002) Proteins , vol.46 , pp. 149-152
    • Gladyshev, V.N.1
  • 50
    • 0029819346 scopus 로고    scopus 로고
    • Identifying and characterizing a structural domain of protein disulfide isomerase
    • Darby NJ, Kemmink J, Creighton TE. Identifying and characterizing a structural domain of protein disulfide isomerase. Biochemistry 1996; 35: 10517-10528.
    • (1996) Biochemistry , vol.35 , pp. 10517-10528
    • Darby, N.J.1    Kemmink, J.2    Creighton, T.E.3
  • 51
    • 0025361036 scopus 로고
    • The involvement of calcium in transport of secretory proteins from the endoplasmic reticulum
    • Sambrook JF. The involvement of calcium in transport of secretory proteins from the endoplasmic reticulum. Cell 1990; 61: 197-199.
    • (1990) Cell , vol.61 , pp. 197-199
    • Sambrook, J.F.1
  • 52
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh S, Burns K, Andrin C, Michalak M. Interaction of calreticulin with protein disulfide isomerase. J Biol Chem 1995; 270: 31338-31344.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31338-31344
    • Baksh, S.1    Burns, K.2    Andrin, C.3    Michalak, M.4
  • 55
    • 0034698838 scopus 로고    scopus 로고
    • Changes in endoplasmic reticulum luminal environment affect cell sensitivity to apoptosis
    • Nakamura K, Bossy-Wetzel E, Burns K et al. Changes in endoplasmic reticulum luminal environment affect cell sensitivity to apoptosis. J Cell Biol 2000; 150: 731-740.
    • (2000) J. Cell Biol. , vol.150 , pp. 731-740
    • Nakamura, K.1    Bossy-Wetzel, E.2    Burns, K.3
  • 56
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman RJ. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev 1999; 13: 1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 57
    • 0029128663 scopus 로고
    • 2+ stores and reveals aspects of their lumenal microenvironment and function
    • 2+ stores and reveals aspects of their lumenal microenvironment and function. J Cell Biol 1995; 130: 847-855.
    • (1995) J. Cell Biol. , vol.130 , pp. 847-855
    • Bastianutto, C.1    Clementi, E.2    Codazzi, F.3
  • 60
    • 0032563599 scopus 로고    scopus 로고
    • Differential modulation of SERCA2 isoforms by calreticulin
    • John LM, Lechleiter JD, Camacho P. Differential modulation of SERCA2 isoforms by calreticulin. J Cell Biol 1998; 142: 963-973.
    • (1998) J. Cell Biol. , vol.142 , pp. 963-973
    • John, L.M.1    Lechleiter, J.D.2    Camacho, P.3
  • 61
    • 0033535353 scopus 로고    scopus 로고
    • Calreticulin is essential for cardiac development
    • Mesaeli N, Nakamura K, Zvaritch E et al. Calreticulin is essential for cardiac development. J Cell Biol 1999; 144: 857-868.
    • (1999) J. Cell Biol. , vol.144 , pp. 857-868
    • Mesaeli, N.1    Nakamura, K.2    Zvaritch, E.3
  • 63
    • 0031843044 scopus 로고    scopus 로고
    • Delayed activation of the store-operated calcium current induced by calreticulin overexpression in RBL-1 cells
    • Fasolato C, Pizzo P, Pozzan T. Delayed activation of the store-operated calcium current induced by calreticulin overexpression in RBL-1 cells. Mol Biol Cell 1998; 9: 1513-1522.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1513-1522
    • Fasolato, C.1    Pizzo, P.2    Pozzan, T.3
  • 67
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: From the ER lumen to the extracellular space
    • Johnson S, Michalak M, Opas M, Eggleton P. The ins and outs of calreticulin: from the ER lumen to the extracellular space. Trends Cell Biol 2001; 11: 122-129.
    • (2001) Trends Cell Biol. , vol.11 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 68
    • 0033591411 scopus 로고    scopus 로고
    • Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion
    • Fadel MP, Dziak E, Lo CM et al. Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion. J Biol Chem 1999; 274: 15085-15094.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15085-15094
    • Fadel, M.P.1    Dziak, E.2    Lo, C.M.3
  • 71
    • 0031259778 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and cadherin/catenin function
    • Daniel JM, Reynolds AB. Tyrosine phosphorylation and cadherin/catenin function. Bioessays 1997; 19: 883-891.
    • (1997) Bioessays , vol.19 , pp. 883-891
    • Daniel, J.M.1    Reynolds, A.B.2
  • 72
    • 0031081425 scopus 로고    scopus 로고
    • Signaling through focal adhesion kinase
    • Hanks SK, Polte TR. Signaling through focal adhesion kinase. Bioessays 1997; 19: 137-145.
    • (1997) Bioessays , vol.19 , pp. 137-145
    • Hanks, S.K.1    Polte, T.R.2
  • 73
    • 0032387687 scopus 로고    scopus 로고
    • Regulation of integrin-mediated adhesion during cell migration
    • Cox EA, Huttenlocher A. Regulation of integrin-mediated adhesion during cell migration. Microsc Res Tech 1998; 43: 412-419.
    • (1998) Microsc. Res. Tech. , vol.43 , pp. 412-419
    • Cox, E.A.1    Huttenlocher, A.2
  • 75
    • 0030067021 scopus 로고    scopus 로고
    • Assembly of focal adhesions: Progress, paradigms, and portents
    • Craig SW, Johnson RP. Assembly of focal adhesions: progress, paradigms, and portents. Curr Opin Cell Biol 1996; 8: 74-85.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 74-85
    • Craig, S.W.1    Johnson, R.P.2
  • 78
    • 0034683570 scopus 로고    scopus 로고
    • Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis
    • Nagai N, Hosokawa M, Itohara S et al. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J Cell Biol 2000; 150: 1499-1506.
    • (2000) J. Cell Biol. , vol.150 , pp. 1499-1506
    • Nagai, N.1    Hosokawa, M.2    Itohara, S.3
  • 79
    • 0036234543 scopus 로고    scopus 로고
    • NFAT signaling: Choreographing the social lives of cells
    • Crabtree GR, Olson EN. NFAT signaling: choreographing the social lives of cells. Cell 2002; 109 (Suppl): S67-79.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Crabtree, G.R.1    Olson, E.N.2
  • 81
    • 0035951849 scopus 로고    scopus 로고
    • Calcium, calcineurin, and the control of transcription
    • Crabtree GR. Calcium, calcineurin, and the control of transcription. J Biol Chem 2001; 276: 2313-2316.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2313-2316
    • Crabtree, G.R.1
  • 82
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Rusnak F, Mertz P. Calcineurin: form and function. Physiol Rev 2000; 80: 1483-1521.
    • (2000) Physiol. Rev. , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 83
    • 0026632557 scopus 로고
    • FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin
    • O'Keefe SJ, Tamura J, Kincaid RL, Tocci MJ, O'Neill EA. FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin. Nature 1992; 357: 692-694.
    • (1992) Nature , vol.357 , pp. 692-694
    • O'Keefe, S.J.1    Tamura, J.2    Kincaid, R.L.3    Tocci, M.J.4    O'Neill, E.A.5
  • 85
    • 0034720882 scopus 로고    scopus 로고
    • 3 receptors that may modulate excitation-contraction coupling in the heart
    • 3 receptors that may modulate excitation-contraction coupling in the heart. Curr Biol 2000; 10: 939-942.
    • (2000) Curr. Biol. , vol.10 , pp. 939-942
    • Lipp, P.1    Laine, M.2    Tovey, S.C.3
  • 87
    • 0036086064 scopus 로고    scopus 로고
    • The unfolded protein response in nutrient sensing and differentiation
    • Kaufman RJ, Scheuner D, Schroder M et al. The unfolded protein response in nutrient sensing and differentiation. Nat Rev Mol Cell Biol 2002; 3: 411-421.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 411-421
    • Kaufman, R.J.1    Scheuner, D.2    Schroder, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.