메뉴 건너뛰기




Volumn 70, Issue , 2005, Pages 405-436

Fibrillin microfibrils

Author keywords

[No Author keywords available]

Indexed keywords

FIBRILLIN; FIBRILLIN 1; FIBRILLIN 2;

EID: 17444387827     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(05)70012-7     Document Type: Article
Times cited : (124)

References (106)
  • 2
    • 0033491095 scopus 로고    scopus 로고
    • Regulation of fibrillin carboxy-terminal furin processing by N-glycosylation, and association of amino- and carboxy-terminal sequences
    • Ashworth J.L., Kelly V., Rock M.J., Shuttleworth C.A., Kielty C.M. Regulation of fibrillin carboxy-terminal furin processing by N-glycosylation, and association of amino- and carboxy-terminal sequences. J. Cell Sci. 112:1999a;4163-4171
    • (1999) J. Cell Sci. , vol.112 , pp. 4163-4171
    • Ashworth, J.L.1    Kelly, V.2    Rock, M.J.3    Shuttleworth, C.A.4    Kielty, C.M.5
  • 8
    • 0036421519 scopus 로고    scopus 로고
    • Three-dimensional reconstructions of extracellular matrix polymers using automated electron tomography
    • Baldock C., Gilpin C., Koster A., Ziese U., Kadler K.E., Kielty C.M., Holmes D.F. Three-dimensional reconstructions of extracellular matrix polymers using automated electron tomography. J. Struct. Biol. 138:2002;130-135
    • (2002) J. Struct. Biol. , vol.138 , pp. 130-135
    • Baldock, C.1    Gilpin, C.2    Koster, A.3    Ziese, U.4    Kadler, K.E.5    Kielty, C.M.6    Holmes, D.F.7
  • 10
    • 0033780943 scopus 로고    scopus 로고
    • Differential effect of FBN1 mutations on in vitro proteolysis of recombinant fibrillin-1 fragments
    • Booms P., Tiecke F., Rosenberg T., Hagemeier C., Robinson P.N. Differential effect of FBN1 mutations on in vitro proteolysis of recombinant fibrillin-1 fragments. Hum. Genet. 107:2000;216-224
    • (2000) Hum. Genet. , vol.107 , pp. 216-224
    • Booms, P.1    Tiecke, F.2    Rosenberg, T.3    Hagemeier, C.4    Robinson, P.N.5
  • 13
    • 0032513005 scopus 로고    scopus 로고
    • Metal ion dependency of microfibrils supports a rod-like conformation for fibrillin-1 calcium-binding epidermal growth factor-like domains
    • Cardy C.M., Handford P.A. Metal ion dependency of microfibrils supports a rod-like conformation for fibrillin-1 calcium-binding epidermal growth factor-like domains. J. Mol. Biol. 276:1998;855-860
    • (1998) J. Mol. Biol. , vol.276 , pp. 855-860
    • Cardy, C.M.1    Handford, P.A.2
  • 16
    • 1242271343 scopus 로고    scopus 로고
    • Differential expression of fibrillin-3 adds to microfibril variety in human and avian, but not rodent, connective tissues
    • Corson G.M., Charbonneau N.L., Keene D.R., Sakai L.Y. Differential expression of fibrillin-3 adds to microfibril variety in human and avian, but not rodent, connective tissues. Genomics. 83:2004;461-472
    • (2004) Genomics , vol.83 , pp. 461-472
    • Corson, G.M.1    Charbonneau, N.L.2    Keene, D.R.3    Sakai, L.Y.4
  • 17
    • 0025096646 scopus 로고
    • Fibrillin immunoreactive fibers constitute a unique network in the human dermis: Immunohistochemical comparison of the distributions of fibrillin, vitronectin, amyloid P component, and orcein stainable structures in normal skin and elastosis
    • Dahlbäck K., Ljungquist A., Lofberg H., Dahlbäck B., Engvall E., Sakai L.Y. Fibrillin immunoreactive fibers constitute a unique network in the human dermis: Immunohistochemical comparison of the distributions of fibrillin, vitronectin, amyloid P component, and orcein stainable structures in normal skin and elastosis. J. Invest. Dermatol. 94:1990;284-291
    • (1990) J. Invest. Dermatol. , vol.94 , pp. 284-291
    • Dahlbäck, K.1    Ljungquist, A.2    Lofberg, H.3    Dahlbäck, B.4    Engvall, E.5    Sakai, L.Y.6
  • 18
    • 0033982504 scopus 로고    scopus 로고
    • Role of the latent transforming growth factor beta binding protein family in fibrillin-containing microfibrils in bone cells in vitro and in vivo
    • Dallas S.L., Keene D.R., Saharinen J., Sakai L.Y., Mundy G.R., Bonewald L.F. Role of the latent transforming growth factor beta binding protein family in fibrillin-containing microfibrils in bone cells in vitro and in vivo. J. Bone Mineral Res. 15:2000;68-81
    • (2000) J. Bone Mineral Res. , vol.15 , pp. 68-81
    • Dallas, S.L.1    Keene, D.R.2    Saharinen, J.3    Sakai, L.Y.4    Mundy, G.R.5    Bonewald, L.F.6
  • 20
    • 0030000090 scopus 로고    scopus 로고
    • Solution structure of a pair of calcium-binding epidermal growth factor-like domains: Implications for the Marfan syndrome and other genetic disorders
    • Downing A.K., Knott V., Werner J.M., Cardy C.M., Campbell I.D., Handford P.A. Solution structure of a pair of calcium-binding epidermal growth factor-like domains: Implications for the Marfan syndrome and other genetic disorders. Cell. 85:1996;597-605
    • (1996) Cell , vol.85 , pp. 597-605
    • Downing, A.K.1    Knott, V.2    Werner, J.M.3    Cardy, C.M.4    Campbell, I.D.5    Handford, P.A.6
  • 22
    • 0024521529 scopus 로고
    • The protein components of the 12-nanometer microfibrils of elastic and non-elastic tissues
    • Gibson M.A., Kumaratilake J.S., Cleary E.G. The protein components of the 12-nanometer microfibrils of elastic and non-elastic tissues. J. Biol. Chem. 264:1989;4590-4598
    • (1989) J. Biol. Chem. , vol.264 , pp. 4590-4598
    • Gibson, M.A.1    Kumaratilake, J.S.2    Cleary, E.G.3
  • 23
    • 0028857166 scopus 로고
    • Bovine latent transforming growth factor β1-binding protein-2: Molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils
    • Gibson M.A., Hatzinikolas G., Davis E.C., Baker E., Sutherland G.R., Mecham R.P. Bovine latent transforming growth factor β1-binding protein-2: Molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils. Mol. Cell. Biol. 15:1995;6932-6942
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6932-6942
    • Gibson, M.A.1    Hatzinikolas, G.2    Davis, E.C.3    Baker, E.4    Sutherland, G.R.5    Mecham, R.P.6
  • 24
    • 0031875947 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-2 (MAGP-2) is specifically associated with fibrillin-containing microfibrils and exhibits more restricted patterns of tissue localisation and developmental expression than its structural relative MAGP-1
    • Gibson M.A., Finnis M.L., Kumaratilake J.L., Cleary E.G. Microfibril-associated glycoprotein-2 (MAGP-2) is specifically associated with fibrillin-containing microfibrils and exhibits more restricted patterns of tissue localisation and developmental expression than its structural relative MAGP-1. J. Histochem. Cytochem. 46:1998;871-885
    • (1998) J. Histochem. Cytochem. , vol.46 , pp. 871-885
    • Gibson, M.A.1    Finnis, M.L.2    Kumaratilake, J.L.3    Cleary, E.G.4
  • 25
    • 0033532072 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via alphaVbeta3 integrin
    • Gibson M.A., Leavesley D.I., Ashman L.K. Microfibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via alphaVbeta3 integrin. J. Biol. Chem. 274:1999;13060-13065
    • (1999) J. Biol. Chem. , vol.274 , pp. 13060-13065
    • Gibson, M.A.1    Leavesley, D.I.2    Ashman, L.K.3
  • 26
    • 0031567592 scopus 로고    scopus 로고
    • Sequence and expression of a novel member (LTBP-4) of the family of latent transforming growth factor-β binding proteins
    • Giltay R., Kostka G., Timpl R. Sequence and expression of a novel member (LTBP-4) of the family of latent transforming growth factor-β binding proteins. FEBS Lett. 411:1997;164-168
    • (1997) FEBS Lett. , vol.411 , pp. 164-168
    • Giltay, R.1    Kostka, G.2    Timpl, R.3
  • 28
    • 3142673750 scopus 로고    scopus 로고
    • MAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrils
    • Hanssen E., Hew F.H., Moore E., Gibson M.A. MAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrils. J. Biol. Chem. 279:2004;29185-29194
    • (2004) J. Biol. Chem. , vol.279 , pp. 29185-29194
    • Hanssen, E.1    Hew, F.H.2    Moore, E.3    Gibson, M.A.4
  • 30
    • 0030447195 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-1 (MAGP-1) is specifically located on the beads of the beaded-filament structure for fibrillin-containing microfibrils as visualized by the rotary shadowing technique
    • Henderson M., Polewski R., Fanning J.C., Gibson M.A. Microfibril- associated glycoprotein-1 (MAGP-1) is specifically located on the beads of the beaded-filament structure for fibrillin-containing microfibrils as visualized by the rotary shadowing technique. J. Histochem. Cytochem. 44:1996;1389-1397
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 1389-1397
    • Henderson, M.1    Polewski, R.2    Fanning, J.C.3    Gibson, M.A.4
  • 31
    • 0033040626 scopus 로고    scopus 로고
    • Fibrillin degradation by matrix metalloproteinases: Identification of amino- and carboxy-terminal cleavage sites
    • Hindson V.J., Ashworth J.L., Rock M.J., Cunliffe S., Shuttleworth C.A., Kielty C.M. Fibrillin degradation by matrix metalloproteinases: Identification of amino- and carboxy-terminal cleavage sites. FEBS Lett. 452:1999;195-198
    • (1999) FEBS Lett. , vol.452 , pp. 195-198
    • Hindson, V.J.1    Ashworth, J.L.2    Rock, M.J.3    Cunliffe, S.4    Shuttleworth, C.A.5    Kielty, C.M.6
  • 32
    • 0036201881 scopus 로고    scopus 로고
    • Expression of 36-kDa microfibril-associated glycoprotein (MAGP-36) in human keratinocytes and its localization in skin
    • Hirano E., Fujimoto N., Tajima S., Akiyama M., Ishibashi R., Okamoto K. Expression of 36-kDa microfibril-associated glycoprotein (MAGP-36) in human keratinocytes and its localization in skin. J. Dermatol. Sci. 28:2002;60-67
    • (2002) J. Dermatol. Sci. , vol.28 , pp. 60-67
    • Hirano, E.1    Fujimoto, N.2    Tajima, S.3    Akiyama, M.4    Ishibashi, R.5    Okamoto, K.6
  • 33
    • 0026667717 scopus 로고
    • Characterization of an associated microfibril protein through recombinant DNA techniques
    • Horrigan S.K., Rich C.B., Streeten B.W., Li Z.Y., Foster J.A. Characterization of an associated microfibril protein through recombinant DNA techniques. J. Biol. Chem. 267:1992;10087-10095
    • (1992) J. Biol. Chem. , vol.267 , pp. 10087-10095
    • Horrigan, S.K.1    Rich, C.B.2    Streeten, B.W.3    Li, Z.Y.4    Foster, J.A.5
  • 34
    • 0037040276 scopus 로고    scopus 로고
    • Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks
    • Isogai Z, Aspberg A., Keene D.R., Ono R.N., Reinhardt D.P., Sakai L.Y. Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks. J. Biol. Chem. 277:2002;4565-4572
    • (2002) J. Biol. Chem. , vol.277 , pp. 4565-4572
    • Isogai, Z.1    Aspberg, A.2    Keene, D.R.3    Ono, R.N.4    Reinhardt, D.P.5    Sakai, L.Y.6
  • 36
    • 0035955677 scopus 로고    scopus 로고
    • Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1
    • Jensen S.A., Reinhardt D.P., Gibson M.A., Weiss A.S. Protein interaction studies of MAGP-1 with tropoelastin and fibrillin-1. J. Biol. Chem. 276:2001;39661-39666
    • (2001) J. Biol. Chem. , vol.276 , pp. 39661-39666
    • Jensen, S.A.1    Reinhardt, D.P.2    Gibson, M.A.3    Weiss, A.S.4
  • 38
    • 0026029066 scopus 로고
    • Extraction of extensible beaded structure and their identification as extracellular matrix fibrillin-containing microfibrils
    • Keene D.R., Maddox B.K., Kuo H-J., Sakai L.Y., Glanville R.W. Extraction of extensible beaded structure and their identification as extracellular matrix fibrillin-containing microfibrils. J. Histochem. Cytochem. 39:1991;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
  • 40
    • 0027141134 scopus 로고
    • The role of calcium in the organisation of fibrillin microfibrils
    • Kielty C.M., Shuttleworth C.A. The role of calcium in the organisation of fibrillin microfibrils. FEBS Lett. 336:1993;323-326
    • (1993) FEBS Lett. , vol.336 , pp. 323-326
    • Kielty, C.M.1    Shuttleworth, C.A.2
  • 41
    • 0027958825 scopus 로고
    • Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin
    • Kielty C.M., Woolley D.E., Whittaker S.P., Shuttleworth C.A. Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin. FEBS Lett. 351:1994;85-89
    • (1994) FEBS Lett. , vol.351 , pp. 85-89
    • Kielty, C.M.1    Woolley, D.E.2    Whittaker, S.P.3    Shuttleworth, C.A.4
  • 42
    • 0029893742 scopus 로고    scopus 로고
    • Fibrillin: Evidence that chondroitin sulphate proteoglycans are components of microfibrils and associate with newly synthesised monomers
    • Kielty C.M., Whittaker S.P., Shuttleworth C.A. Fibrillin: Evidence that chondroitin sulphate proteoglycans are components of microfibrils and associate with newly synthesised monomers. FEBS Lett. 386:1996;169-173
    • (1996) FEBS Lett. , vol.386 , pp. 169-173
    • Kielty, C.M.1    Whittaker, S.P.2    Shuttleworth, C.A.3
  • 43
    • 1842413692 scopus 로고    scopus 로고
    • Microfibrillar elements of the dermal matrix
    • Kielty C.M., Shuttleworth C.A. Microfibrillar elements of the dermal matrix. Microsc. Res. Tech. 38:1997;407-427
    • (1997) Microsc. Res. Tech. , vol.38 , pp. 407-427
    • Kielty, C.M.1    Shuttleworth, C.A.2
  • 50
    • 0242383972 scopus 로고    scopus 로고
    • Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta
    • Lack J., O'Leary J.M., Knott V., Yuan X., Rifkin D.B., Handford P.A., Downing A.K. Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta. J. Mol. Biol. 334:2003;281-291
    • (2003) J. Mol. Biol. , vol.334 , pp. 281-291
    • Lack, J.1    O'Leary, J.M.2    Knott, V.3    Yuan, X.4    Rifkin, D.B.5    Handford, P.A.6    Downing, A.K.7
  • 53
    • 0037184979 scopus 로고    scopus 로고
    • Homo- and heterotypic fibrillin-1 and -2 interactions constitute the basis for the assembly of microfibrils
    • Lin G., Tiedemann K., Vollbrandt T., Peters H., Batge B., Brinckmann J., Reinhardt D.P. Homo- and heterotypic fibrillin-1 and -2 interactions constitute the basis for the assembly of microfibrils. J. Biol. Chem. 277:2002;50795-50804
    • (2002) J. Biol. Chem. , vol.277 , pp. 50795-50804
    • Lin, G.1    Tiedemann, K.2    Vollbrandt, T.3    Peters, H.4    Batge, B.5    Brinckmann, J.6    Reinhardt, D.P.7
  • 54
    • 0030891826 scopus 로고    scopus 로고
    • The gene for microfibril-associated protein-1 (MFAP1) is located several megabases centromeric to FBN1 and is not mutated in Marfan syndrome
    • Liu W.G., Faraco J., Qian C.P., Francke U. The gene for microfibril-associated protein-1 (MFAP1) is located several megabases centromeric to FBN1 and is not mutated in Marfan syndrome. Human Genet. 99:1997;578-584
    • (1997) Human Genet. , vol.99 , pp. 578-584
    • Liu, W.G.1    Faraco, J.2    Qian, C.P.3    Francke, U.4
  • 56
    • 0002553444 scopus 로고
    • Elastic fiber structure and assembly
    • P.D. Yurchenco, D.E. Birk, & R.P. Mecham. New York: Academic Press
    • Mecham R.P., Davis E.C. Elastic fiber structure and assembly. Yurchenco P.D., Birk D.E., Mecham R.P. "Extracellular Matrix Assembly and Structure" 1994;281-314 Academic Press, New York
    • (1994) "extracellular Matrix Assembly and Structure" , pp. 281-314
    • Mecham, R.P.1    Davis, E.C.2
  • 58
    • 0035958015 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain with code for large proteins in vitro
    • Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain with code for large proteins in vitro. DNA Res. 8:2001;85-95
    • (2001) DNA Res. , vol.8 , pp. 85-95
    • Nagase, T.1    Nakayama, M.2    Nakajima, D.3    Kikuno, R.4    Ohara, O.5
  • 61
    • 0034672359 scopus 로고    scopus 로고
    • The latent transforming growth factor beta binding protein (LTBP) family
    • Oklu R., Hesketh R. The latent transforming growth factor beta binding protein (LTBP) family. Biochem. J. 352:2000;601-610
    • (2000) Biochem. J. , vol.352 , pp. 601-610
    • Oklu, R.1    Hesketh, R.2
  • 62
    • 0035847046 scopus 로고    scopus 로고
    • The proteoglycans aggrecan and versican form networks with fibulin-2 through their lectin domain binding
    • Olin A.I., Morgelin M., Sasaki T., Timpl R., Heinegärd D., Aspberg A. The proteoglycans aggrecan and versican form networks with fibulin-2 through their lectin domain binding. J. Biol. Chem. 276:2000;1253-1261
    • (2000) J. Biol. Chem. , vol.276 , pp. 1253-1261
    • Olin, A.I.1    Morgelin, M.2    Sasaki, T.3    Timpl, R.4    Heinegärd, D.5    Aspberg, A.6
  • 64
    • 0029867570 scopus 로고    scopus 로고
    • Cell adhesion and integrin binding to recombinant human fibrillin-1
    • Pfaff M., Reinhardt D.P., Sakai L.Y., Timpl R. Cell adhesion and integrin binding to recombinant human fibrillin-1. FEBS Lett. 384:1996;247-250
    • (1996) FEBS Lett. , vol.384 , pp. 247-250
    • Pfaff, M.1    Reinhardt, D.P.2    Sakai, L.Y.3    Timpl, R.4
  • 65
    • 0031470781 scopus 로고    scopus 로고
    • Alignment of fibrillin molecules in elastic microfibrils is defined by transglutaminase-derived cross-links
    • Qian R.Q., Glanville R.W. Alignment of fibrillin molecules in elastic microfibrils is defined by transglutaminase-derived cross-links. Biochemistry. 36:1997;15841-15847
    • (1997) Biochemistry , vol.36 , pp. 15841-15847
    • Qian, R.Q.1    Glanville, R.W.2
  • 66
    • 0031691462 scopus 로고    scopus 로고
    • The cutaneous microfibrillar apparatus contains latent transforming growth factor-beta binding protein-1 (LTBP-1) and is a repository for latent TGF-beta 1
    • Raghunath M., Unsold C., Kubitscheck U., Bruckner-Tuderman L., Peters R., Meuli M. The cutaneous microfibrillar apparatus contains latent transforming growth factor-beta binding protein-1 (LTBP-1) and is a repository for latent TGF-beta 1. J. Invest. Dermatol. 111:1998;559-564
    • (1998) J. Invest. Dermatol. , vol.111 , pp. 559-564
    • Raghunath, M.1    Unsold, C.2    Kubitscheck, U.3    Bruckner-Tuderman, L.4    Peters, R.5    Meuli, M.6
  • 71
    • 0034697304 scopus 로고    scopus 로고
    • Mutations in calcium-binding epidermal growth factor modules render fibrillin-1 susceptible to proteolysis. A potential disease-causing mechanism in Marfan syndrome
    • Reinhardt D.P., Ono R.N., Notbohm H., Muller P.K., Bachinger H.P., Sakai L.Y. Mutations in calcium-binding epidermal growth factor modules render fibrillin-1 susceptible to proteolysis. A potential disease-causing mechanism in Marfan syndrome. J. Biol. Chem. 275:2000a;12339-12345
    • (2000) J. Biol. Chem. , vol.275 , pp. 12339-12345
    • Reinhardt, D.P.1    Ono, R.N.2    Notbohm, H.3    Muller, P.K.4    Bachinger, H.P.5    Sakai, L.Y.6
  • 72
    • 0034695559 scopus 로고    scopus 로고
    • Initial steps in assembly of microfibrils. Formation of disulfide-cross-linked multimers containing fibrillin-1
    • Reinhardt D.P., Gambee J.E., Ono R.N., Bachinger H.P., Sakai L.Y. Initial steps in assembly of microfibrils. Formation of disulfide-cross-linked multimers containing fibrillin-1. J. Biol. Chem. 275:2000b;2205-2210
    • (2000) J. Biol. Chem. , vol.275 , pp. 2205-2210
    • Reinhardt, D.P.1    Gambee, J.E.2    Ono, R.N.3    Bachinger, H.P.4    Sakai, L.Y.5
  • 74
    • 0142231565 scopus 로고    scopus 로고
    • Fibrillin-1 and -2 contain heparin-binding sites important for matrix deposition and that support cell attachment
    • Ritty T.M., Broekelmann T.J., Werneck C.C., Mecham R.P. Fibrillin-1 and -2 contain heparin-binding sites important for matrix deposition and that support cell attachment. Biochem. J. 375:2003;425-432
    • (2003) Biochem. J. , vol.375 , pp. 425-432
    • Ritty, T.M.1    Broekelmann, T.J.2    Werneck, C.C.3    Mecham, R.P.4
  • 75
    • 0034776552 scopus 로고    scopus 로고
    • The molecular pathogenesis of the Marfan syndrome
    • Robinson P.N., Booms P. The molecular pathogenesis of the Marfan syndrome. Cell Mol. Life Sci. 58:2001;1698-1707
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1698-1707
    • Robinson, P.N.1    Booms, P.2
  • 76
  • 78
    • 0032540880 scopus 로고    scopus 로고
    • Identification and characterization of a new latent transforming growth factor-β-binding protein, LTBP-4
    • Saharinen J., Taipale J., Monni O., Keski-Oja J. Identification and characterization of a new latent transforming growth factor-β-binding protein, LTBP-4. J. Biol. Chem. 273:1998;18459-18469
    • (1998) J. Biol. Chem. , vol.273 , pp. 18459-18469
    • Saharinen, J.1    Taipale, J.2    Monni, O.3    Keski-Oja, J.4
  • 79
  • 81
    • 0037192804 scopus 로고    scopus 로고
    • Identification of a matrix binding domain in the microfibril-associated glycoproteins 1 and 2 (MAGP1 and 2) and intracellular localization of alternative splice forms
    • Segade F., Trask B.C., Broekelmann T.J., Pierce R.A., Mecham R.P. Identification of a matrix binding domain in the microfibril-associated glycoproteins 1 and 2 (MAGP1 and 2) and intracellular localization of alternative splice forms. J. Biol. Chem. 277:2002;11050-11057
    • (2002) J. Biol. Chem. , vol.277 , pp. 11050-11057
    • Segade, F.1    Trask, B.C.2    Broekelmann, T.J.3    Pierce, R.A.4    Mecham, R.P.5
  • 82
    • 0030772330 scopus 로고    scopus 로고
    • Scanning transmission electron microscopy mass analysis of fibrillin-containing microfibrils from foetal elastic tissues
    • Sherratt M.J., Holmes D.F., Shuttleworth C.A., Kielty C.M. Scanning transmission electron microscopy mass analysis of fibrillin-containing microfibrils from foetal elastic tissues. Int. J. Biochem. Cell Biol. 29:1997;1063-1070
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 1063-1070
    • Sherratt, M.J.1    Holmes, D.F.2    Shuttleworth, C.A.3    Kielty, C.M.4
  • 85
    • 2142640338 scopus 로고    scopus 로고
    • Substrate dependent morphology of supra-molecular assemblies: Fibrillin and type VI collagen microfibrils
    • Sherratt M.J., Holmes D.F., Shuttleworth C.A., Kielty C.M. Substrate dependent morphology of supra-molecular assemblies: Fibrillin and type VI collagen microfibrils. Biophys. J. 86:2004;3211-3222
    • (2004) Biophys. J. , vol.86 , pp. 3211-3222
    • Sherratt, M.J.1    Holmes, D.F.2    Shuttleworth, C.A.3    Kielty, C.M.4
  • 86
    • 0032415040 scopus 로고    scopus 로고
    • Cellular and extracellular biology of the latent transforming growth factor-beta binding proteins
    • Sinha S., Nevett C., Shuttleworth C.A., Kielty C.M. Cellular and extracellular biology of the latent transforming growth factor-beta binding proteins. Matrix Biol. 17:1998;529-545
    • (1998) Matrix Biol. , vol.17 , pp. 529-545
    • Sinha, S.1    Nevett, C.2    Shuttleworth, C.A.3    Kielty, C.M.4
  • 87
    • 0036194882 scopus 로고    scopus 로고
    • Expression of latent TGFbeta binding proteins and association with TGFbeta-1 and fibrillin-1 in the response to arterial injury
    • Sinha S., Shuttleworth C.A., Heagerty A.M., Kielty C.M. Expression of latent TGFbeta binding proteins and association with TGFbeta-1 and fibrillin-1 in the response to arterial injury. Cardiovasc. Res. 53:2002;971-983
    • (2002) Cardiovasc. Res. , vol.53 , pp. 971-983
    • Sinha, S.1    Shuttleworth, C.A.2    Heagerty, A.M.3    Kielty, C.M.4
  • 88
    • 0012955959 scopus 로고    scopus 로고
    • Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1
    • Smallridge R.S., Whiteman P., Werner J.M., Campbell I.D., Handford P.A., Downing A.K. Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1. J. Biol. Chem. 278:2003;12199-12206
    • (2003) J. Biol. Chem. , vol.278 , pp. 12199-12206
    • Smallridge, R.S.1    Whiteman, P.2    Werner, J.M.3    Campbell, I.D.4    Handford, P.A.5    Downing, A.K.6
  • 89
    • 0029813731 scopus 로고    scopus 로고
    • Latent transforming growth-factor-β1 and its binding-protein are components of extracellular-matrix microfibrils
    • Taipale J., Saharinen J., Hedman K., Keski-Oja J. Latent transforming growth-factor-β1 and its binding-protein are components of extracellular-matrix microfibrils. J. Histochem. Cytochem. 44:1996;875-889
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 875-889
    • Taipale, J.1    Saharinen, J.2    Hedman, K.3    Keski-Oja, J.4
  • 90
    • 0035929624 scopus 로고    scopus 로고
    • Interactions of fibrillin-1 with heparin/heparan sulphate, implications for microfibrillar assembly
    • Tiedemann K., Bätge B., Müller P.K., Reinhardt D.P. Interactions of fibrillin-1 with heparin/heparan sulphate, implications for microfibrillar assembly. J. Biol. Chem. 276:2001;36035-36042
    • (2001) J. Biol. Chem. , vol.276 , pp. 36035-36042
    • Tiedemann, K.1    Bätge, B.2    Müller, P.K.3    Reinhardt, D.P.4
  • 91
    • 0032776492 scopus 로고    scopus 로고
    • Ultrastructural distribution of 36-kDa microfibril-associated glycoprotein (MAGP-36) in human and bovine tissues
    • Toyoshima T., Yamashita K., Shishibori T., Itano T., Kobayashi R. Ultrastructural distribution of 36-kDa microfibril-associated glycoprotein (MAGP-36) in human and bovine tissues. J. Histochem. Cytochem. 47:1999;1049-1056
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 1049-1056
    • Toyoshima, T.1    Yamashita, K.2    Shishibori, T.3    Itano, T.4    Kobayashi, R.5
  • 92
    • 0033564643 scopus 로고    scopus 로고
    • N-terminal domains of fibrillin 1 and fibrillin 2 direct the formation of homodimers: A possible first step in microfibril assembly
    • Trask T.M., Ritty T.M., Broekelmann T., Tisdale C., Mecham R.P. N-terminal domains of fibrillin 1 and fibrillin 2 direct the formation of homodimers: A possible first step in microfibril assembly. Biochem J. 340:1999;693-701
    • (1999) Biochem J. , vol.340 , pp. 693-701
    • Trask, T.M.1    Ritty, T.M.2    Broekelmann, T.3    Tisdale, C.4    Mecham, R.P.5
  • 93
    • 0034111432 scopus 로고    scopus 로고
    • The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin
    • Trask B.C., Trask T.M., Broekelmann T., Mecham R.P. The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin. Mol. Biol. Cell. 11:2000;1499-1507
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1499-1507
    • Trask, B.C.1    Trask, T.M.2    Broekelmann, T.3    Mecham, R.P.4
  • 94
    • 0025980347 scopus 로고
    • Rotary shadowing of elastic system microfibrils in the ocular zonule, vitreous, and ligamentum nuchae
    • Wallace R.N., Streeten B.W., Hanna R.B. Rotary shadowing of elastic system microfibrils in the ocular zonule, vitreous, and ligamentum nuchae. Curr. Eye Res. 10:1991);99-109
    • (1991) Curr. Eye Res. , vol.10 , pp. 99-109
    • Wallace, R.N.1    Streeten, B.W.2    Hanna, R.B.3
  • 96
    • 0032895768 scopus 로고    scopus 로고
    • Fibrillin-rich microfibrils are reduced in photoaged skin. Distribution at the dermal-epidermal junction
    • Watson R.E., Griffiths C.E., Craven N.M., Shuttleworth C.A., Kielty C.M. Fibrillin-rich microfibrils are reduced in photoaged skin. Distribution at the dermal-epidermal junction. J. Invest. Dermatol. 112:1999;782-788
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 782-788
    • Watson, R.E.1    Griffiths, C.E.2    Craven, N.M.3    Shuttleworth, C.A.4    Kielty, C.M.5
  • 98
    • 0030823297 scopus 로고    scopus 로고
    • Fibrillin-rich microfibrils: An X-ray diffraction study and elastomeric properties
    • Wess T.J., Purslow P., Kielty C.M. Fibrillin-rich microfibrils: An X-ray diffraction study and elastomeric properties. FEBS Lett. 413:1997;424-428
    • (1997) FEBS Lett. , vol.413 , pp. 424-428
    • Wess, T.J.1    Purslow, P.2    Kielty, C.M.3
  • 100
    • 0031658374 scopus 로고    scopus 로고
    • X-ray diffraction studies of fibrillin-rich microfibrils: Effects of tissue extension on axial and lateral packing
    • Wess T.J., Purslow P.P., Kielty C.M. X-ray diffraction studies of fibrillin-rich microfibrils: Effects of tissue extension on axial and lateral packing. J. Struct. Biol. 122:1998b;123-127
    • (1998) J. Struct. Biol. , vol.122 , pp. 123-127
    • Wess, T.J.1    Purslow, P.P.2    Kielty, C.M.3
  • 101
    • 0037388618 scopus 로고    scopus 로고
    • Defective secretion of recombinant fragments of fibrillin-1: Implications of protein misfolding for the pathogenesis of Marfan syndrome and related disorders
    • Whiteman P., Handford P.A. Defective secretion of recombinant fragments of fibrillin-1: Implications of protein misfolding for the pathogenesis of Marfan syndrome and related disorders. Hum. Mol. Genet. 12:2003;727-737
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 727-737
    • Whiteman, P.1    Handford, P.A.2
  • 103
    • 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., Handford P.A. Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils. EMBO J. 16:1997;6659-6666
    • (1997) EMBO J. , vol.16 , pp. 6659-6666
    • Yuan, X.1    Downing, A.K.2    Knott, V.3    Handford, P.A.4
  • 104
    • 0028267099 scopus 로고
    • Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices
    • Zhang H., Apfelroth S.D., Hu W., Davis E.C., Sanguineti C., Bonadio J., Mecham R.P., Ramirez F. Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices. J. Cell Biol. 124:1994;855-863
    • (1994) J. Cell Biol. , vol.124 , pp. 855-863
    • Zhang, H.1    Apfelroth, S.D.2    Hu, W.3    Davis, E.C.4    Sanguineti, C.5    Bonadio, J.6    Mecham, R.P.7    Ramirez, F.8
  • 105
    • 0029023792 scopus 로고
    • Developmental expression of fibrillin genes suggests heterogeneity of extracellular microfibrils
    • Zhang H., Hu W., Ramirez F. Developmental expression of fibrillin genes suggests heterogeneity of extracellular microfibrils. J. Cell Biol. 129:1995;1165-1176
    • (1995) J. Cell Biol. , vol.129 , pp. 1165-1176
    • Zhang, H.1    Hu, W.2    Ramirez, F.3
  • 106
    • 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., Schubert M., Bruckner-Tuderman L. Versican is expressed in the proliferating zone in the epidermis and in association with the elastic network of the dermis. J. Cell Biol. 124:1994;817-825
    • (1994) J. Cell Biol. , vol.124 , pp. 817-825
    • Zimmermann, D.R.1    Dours-Zimmermann, M.2    Schubert, M.3    Bruckner-Tuderman, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.