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Volumn 112, Issue 20, 1999, Pages 3549-3558

Fibrillin assembly: Dimer formation mediated by amino-terminal sequences

Author keywords

Dimer; Fibrillin; Microfibril assembly

Indexed keywords

CALRETICULIN; CHAPERONE; FIBRILLIN; GLYCINE; PROLINE; PROTEIN DISULFIDE ISOMERASE; PROTEINASE K;

EID: 0032700974     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (44)

References (27)
  • 2
    • 0030000090 scopus 로고    scopus 로고
    • Solution structure of a pair of calcium-binding epidermal growth factor-like domains of fibrillin-1, the Marfan gene product
    • Downing, A. K., Knott, V., Werner, J. M., Cardy, C., Campbell, I. D. and Handford, P. A. (1996). Solution structure of a pair of calcium-binding epidermal growth factor-like domains of fibrillin-1, the Marfan gene product. Cell 85, 597-605.
    • (1996) Cell , vol.85 , pp. 597-605
    • Downing, A.K.1    Knott, V.2    Werner, J.M.3    Cardy, C.4    Campbell, I.D.5    Handford, P.A.6
  • 3
    • 0024521529 scopus 로고
    • The protein components of the 12-nanometer microfibrils of elastic and non-elastic tissues
    • Gibson, M. A., Kumaratilake, J. S. and Cleary, E. G. (1989). The protein components of the 12-nanometer microfibrils of elastic and non-elastic tissues. J. Biol. Chem. 264, 4590-4598.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4590-4598
    • Gibson, M.A.1    Kumaratilake, J.S.2    Cleary, E.G.3
  • 4
    • 0032096395 scopus 로고    scopus 로고
    • Atomic force microscopy and modeling of natural elastic fibrillin polymers
    • Hanssen, E., Franc, S. and Garrone, R. (1998). Atomic force microscopy and modeling of natural elastic fibrillin polymers. Biol. Cell 90, 223-228.
    • (1998) Biol. Cell , vol.90 , pp. 223-228
    • Hanssen, E.1    Franc, S.2    Garrone, R.3
  • 5
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 7
    • 0033040626 scopus 로고    scopus 로고
    • Fibrillin degradation by matrix metalloproteinases: Identification of amino- and carboxy-terminal cleavage sites
    • in press
    • Hindson, V. J., Ashworth, J. L., Rock, M. J., Cunliffe, S., Shuttleworth, C. A. and Kielty, C. M. (1999). Fibrillin degradation by matrix metalloproteinases: identification of amino- and carboxy-terminal cleavage sites. FEBS Lett. (in press).
    • (1999) FEBS Lett.
    • Hindson, V.J.1    Ashworth, J.L.2    Rock, M.J.3    Cunliffe, S.4    Shuttleworth, C.A.5    Kielty, C.M.6
  • 8
    • 0026029066 scopus 로고
    • Extraction of beaded structures and their identification as fibrillin-containing matrix microfibrils
    • Keene, D. R., Maddox, B. K., Kuo, H.-J, Sakai, L. Y. and Glanville, R. W. (1991). Extraction of beaded structures and their identification as fibrillin-containing matrix microfibrils. J. Histochem. Cytochem. 39, 441-449.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 441-449
    • Keene, D.R.1    Maddox, B.K.2    Kuo, H.-J.3    Sakai, L.Y.4    Glanville, R.W.5
  • 9
    • 0027375471 scopus 로고
    • Synthesis and assembly of fibrillin by fibroblasts and smooth muscle cells
    • Kielty, C. M. and Shuttleworth, C. A. (1993). Synthesis and assembly of fibrillin by fibroblasts and smooth muscle cells. J. Cell Sci. 106, 167-173.
    • (1993) J. Cell Sci. , vol.106 , pp. 167-173
    • Kielty, C.M.1    Shuttleworth, C.A.2
  • 10
    • 0029115657 scopus 로고
    • Fibrillin-containing microfibrils: Structure and function in health and disease
    • Kielty, C. M. and Shuttleworth, C. A. (1995). Fibrillin-containing microfibrils: structure and function in health and disease. Int. J. Biochem. Cell Biol. 27, 747-760.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 747-760
    • Kielty, C.M.1    Shuttleworth, C.A.2
  • 11
    • 0002097152 scopus 로고
    • The collagen family: Structure, assembly and organisation in the extracellular matrix
    • ed. P. M. Royce and B. Steinmann. New York: Wiley Liss
    • Kielty, C. M., Hopkinson, I. and Grant, M. E. (1993). The collagen family: structure, assembly and organisation in the extracellular matrix. In Connective Tissue and its Heritable Disorders (ed. P. M. Royce and B. Steinmann), pp. 103-147. New York: Wiley Liss.
    • (1993) Connective Tissue and Its Heritable Disorders , pp. 103-147
    • Kielty, C.M.1    Hopkinson, I.2    Grant, M.E.3
  • 12
    • 0031055069 scopus 로고    scopus 로고
    • Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen
    • Lees, J. F., Tasab, M. and Bulleid, N. J. (1997). Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen. EMBO J. 16, 908-916.
    • (1997) EMBO J. , vol.16 , pp. 908-916
    • Lees, J.F.1    Tasab, M.2    Bulleid, N.J.3
  • 14
    • 0027313286 scopus 로고
    • Genomic organisation of the sequence coding for fibrillin-1, the defective gene product in Marfan syndrome
    • Pereira, L., D'Alessio, M., Ramirez, F., Lynch, J. R., Sykes, B., Pangilinan, T. and Bonadio, J. (1993). Genomic organisation of the sequence coding for fibrillin-1, the defective gene product in Marfan syndrome. Hum. Mol. Genet. 2, 961-968.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 961-968
    • Pereira, L.1    D'Alessio, M.2    Ramirez, F.3    Lynch, J.R.4    Sykes, B.5    Pangilinan, T.6    Bonadio, J.7
  • 15
    • 0031470781 scopus 로고    scopus 로고
    • Alignment of fibrillin molecules in elastic microfibrils is defined by transglutaminase-derived crosslinks
    • Qian, R. Q. and Glanville, R. W. (1997). Alignment of fibrillin molecules in elastic microfibrils is defined by transglutaminase-derived crosslinks. Biochem. 36, 15841-15847.
    • (1997) Biochem. , vol.36 , pp. 15841-15847
    • Qian, R.Q.1    Glanville, R.W.2
  • 16
    • 0032937875 scopus 로고    scopus 로고
    • Carboxy-terminal conversion of profibrillin to fibrillin at a basic site by PACE/furin-like activity required for incorporation in the matrix
    • Raghunath, M., Putnam, E. A., Ritty, T., Hamstra, D., Park, E-S., Tschödrich-Rotter, M., Peters, R., Rehemtulla, A. and Milewicz, D. M. (1999). Carboxy-terminal conversion of profibrillin to fibrillin at a basic site by PACE/furin-like activity required for incorporation in the matrix. J. Cell Sci. 112, 1093-1100.
    • (1999) J. Cell Sci. , vol.112 , pp. 1093-1100
    • Raghunath, M.1    Putnam, E.A.2    Ritty, T.3    Hamstra, D.4    Park, E.-S.5    Tschödrich-Rotter, M.6    Peters, R.7    Rehemtulla, A.8    Milewicz, D.M.9
  • 17
    • 0029665565 scopus 로고    scopus 로고
    • Fibrillin mutations and related phenotypes
    • Ramirez, F. (1996). Fibrillin mutations and related phenotypes. Curr. Opin. Genet. Dev. 6, 309-315.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 309-315
    • Ramirez, F.1
  • 21
    • 0010410523 scopus 로고
    • Disulphide bonds crosslink molecules of fibrillin in the connective tissue space
    • ed. A. Tamburro and J. M. Davidson. Congedo Editore, Galatina, Italy
    • Sakai, L. Y. (1990). Disulphide bonds crosslink molecules of fibrillin in the connective tissue space. In Elastin: Chemical and Biological Aspects (ed. A. Tamburro and J. M. Davidson), pp. 213-227. Congedo Editore, Galatina, Italy.
    • (1990) Elastin: Chemical and Biological Aspects , pp. 213-227
    • Sakai, L.Y.1
  • 22
    • 0028929503 scopus 로고
    • Fibrillin: Monomers and microfibrils
    • Sakai, L. Y. and Keene, D. R. (1994). Fibrillin: monomers and microfibrils. Methods Enzymol. 245, 29-42.
    • (1994) Methods Enzymol. , vol.245 , pp. 29-42
    • Sakai, L.Y.1    Keene, D.R.2
  • 24
    • 0029024163 scopus 로고
    • The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilised mammalian cells
    • Wilson, R., Allen, A. J., Oliver, J., Brookman, J. L., High., S. and Bulleid, N. J. (1995). The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilised mammalian cells. Biochem. J. 307, 679-687.
    • (1995) Biochem. J. , vol.307 , pp. 679-687
    • Wilson, R.1    Allen, A.J.2    Oliver, J.3    Brookman, J.L.4    High, S.5    Bulleid, N.J.6
  • 25
    • 0032540353 scopus 로고    scopus 로고
    • Protein disulphide isomerase acts as a molecular chaperone during the assembly of procollagen
    • Wilson, R., Lees, J. F. and Bulleid, N. J. (1998). Protein disulphide isomerase acts as a molecular chaperone during the assembly of procollagen. J. Biol. Chem. 273, 9637-9643.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9637-9643
    • Wilson, R.1    Lees, J.F.2    Bulleid, N.J.3
  • 26
    • 0030781430 scopus 로고    scopus 로고
    • Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils
    • Yuan, X., Downing, A. K., Knott, V. and Handford, P. A. (1997). Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils. EMBO J. 16, 6659-6666.
    • (1997) EMBO J. , vol.16 , pp. 6659-6666
    • Yuan, X.1    Downing, A.K.2    Knott, V.3    Handford, P.A.4
  • 27
    • 0343247046 scopus 로고
    • Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices
    • Zhang, H., Hu, W. and Ramirez, F. (1994). Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices. J. Cell Biol. 129, 1165-1176.
    • (1994) J. Cell Biol. , vol.129 , pp. 1165-1176
    • Zhang, H.1    Hu, W.2    Ramirez, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.