메뉴 건너뛰기




Volumn 8, Issue 1, 2014, Pages 75-80

1H, 13C and 15N assignments of the four N-terminal domains of human fibrillin-1

Author keywords

Bone morphogenetic proteins; Extracellular matrix; Human fibrillin 1 N terminus; Microfibril assembly; NMR resonance assignments

Indexed keywords

ACTIN BINDING PROTEIN; CARBON; FIBRILLIN; HYDROGEN; NITROGEN;

EID: 84897114634     PISSN: 18742718     EISSN: 1874270X     Source Type: Journal    
DOI: 10.1007/s12104-012-9456-0     Document Type: Article
Times cited : (5)

References (26)
  • 1
    • 27544456339 scopus 로고    scopus 로고
    • A simple method to predict protein flexibility using secondary chemical shifts
    • 10.1021/ja054842f
    • Berjanskii MV, Wishart DS (2005) A simple method to predict protein flexibility using secondary chemical shifts. J Am Chem Soc 127(43):14970-14971
    • (2005) J Am Chem Soc , vol.127 , Issue.43 , pp. 14970-14971
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 2
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork P, Downing A, Kieffer B, Campbell I (1996) Structure and distribution of modules in extracellular proteins. Q Rev Biophys 29(2):119-167
    • (1996) Q Rev Biophys , vol.29 , Issue.2 , pp. 119-167
    • Bork, P.1    Downing, A.2    Kieffer, B.3    Campbell, I.4
  • 3
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • 10.1007/BF00197809
    • Delaglio F, Grzesiek S, Vuister G, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277-293
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 6
    • 0032096395 scopus 로고    scopus 로고
    • Atomic force microscopy and modeling of natural elastic fibrillin polymers
    • Hanssen E, Franc S, Garrone R (1998) Atomic force microscopy and modeling of natural elastic fibrillin polymers. Biol Cell 90(3):223
    • (1998) Biol Cell , vol.90 , Issue.3 , pp. 223
    • Hanssen, E.1    Franc, S.2    Garrone, R.3
  • 7
    • 44349128895 scopus 로고    scopus 로고
    • Biogenesis of extracellular microfibrils: Multimerization of the fibrillin-1 C terminus into bead-like structures enables self-assembly
    • 2008PNAS.105.6548H 10.1073/pnas.0706335105
    • Hubmacher D, El-Hallous EI, Nelea V, Kaartinen MT, Lee ER, Reinhardt DP (2008) Biogenesis of extracellular microfibrils: Multimerization of the fibrillin-1 C terminus into bead-like structures enables self-assembly. Proc Natl Acad Sci USA 105(18):6548
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.18 , pp. 6548
    • Hubmacher, D.1    El-Hallous, E.I.2    Nelea, V.3    Kaartinen, M.T.4    Lee, E.R.5    Reinhardt, D.P.6
  • 8
    • 65149089049 scopus 로고    scopus 로고
    • Structure and interdomain interactions of a hybrid domain: A disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins
    • 10.1016/j.str.2009.03.014
    • Jensen SA, Iqbal S, Lowe ED, Redfield C, Handford PA (2009) Structure and interdomain interactions of a hybrid domain: A disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins. Structure 17(5):759
    • (2009) Structure , vol.17 , Issue.5 , pp. 759
    • Jensen, S.A.1    Iqbal, S.2    Lowe, E.D.3    Redfield, C.4    Handford, P.A.5
  • 9
    • 0029977996 scopus 로고    scopus 로고
    • Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1
    • 10.1006/jmbi.1996.0003
    • Knott V, Downing AK, Cardy CM, Handford P (1996) Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1. J Mol Biol 255(1):22
    • (1996) J Mol Biol , vol.255 , Issue.1 , pp. 22
    • Knott, V.1    Downing, A.K.2    Cardy, C.M.3    Handford, P.4
  • 11
    • 0025900544 scopus 로고
    • Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes
    • 1991Natur.352.330L 10.1038/352330a0
    • Lee B, Godfrey M, Vitale E, Hori H, Mattei MG, Sarfarazi M, Tsipouras P, Ramirez F, Hollister DW (1991) Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes. Nature 352(6333):330-334
    • (1991) Nature , vol.352 , Issue.6333 , pp. 330-334
    • Lee, B.1    Godfrey, M.2    Vitale, E.3    Hori, H.4    Mattei, M.G.5    Sarfarazi, M.6    Tsipouras, P.7    Ramirez, F.8    Hollister, D.W.9
  • 13
    • 0037184979 scopus 로고    scopus 로고
    • Homo- And heterotypic fibrillin-1 and -2 interactions constitute the basis for the assembly of microfibrils
    • 10.1074/jbc.M210611200
    • Lin G, Tiedemann K, Vollbrandt T, Peters H, Batge B, Brinckmann J, Reinhardt DP (2002) Homo- And heterotypic fibrillin-1 and -2 interactions constitute the basis for the assembly of microfibrils. J Biol Chem 277(52):50795
    • (2002) J Biol Chem , vol.277 , Issue.52 , pp. 50795
    • Lin, G.1    Tiedemann, K.2    Vollbrandt, T.3    Peters, H.4    Batge, B.5    Brinckmann, J.6    Reinhardt, D.P.7
  • 16
    • 0027313286 scopus 로고
    • Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome
    • 10.1093/hmg/2.7.961
    • Pereira L, D'Alessio M, Ramirez F, Lynch JR, Sykes B, Pangilinan T, Bonadio J (1993) Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome. Hum Mol Genet 2(7):961
    • (1993) Hum Mol Genet , vol.2 , Issue.7 , pp. 961
    • Pereira, L.1    D'Alessio, M.2    Ramirez, F.3    Lynch, J.R.4    Sykes, B.5    Pangilinan, T.6    Bonadio, J.7
  • 17
    • 70349325817 scopus 로고    scopus 로고
    • Extracellular microfibrils: Contextual platforms for TGFbeta and BMP signaling
    • Ramirez F, Rifkin DB (2009) Extracellular microfibrils: Contextual platforms for TGFbeta and BMP signaling. Curr Opin Cell Biol
    • (2009) Curr Opin Cell Biol
    • Ramirez, F.1    Rifkin, D.B.2
  • 18
    • 78651325952 scopus 로고    scopus 로고
    • TB domain proteins: Evolutionary insights into the multifaceted roles of fibrillins and LTBPs
    • Robertson I, Jensen S, Handford P (2011) TB domain proteins: Evolutionary insights into the multifaceted roles of fibrillins and LTBPs. Biochem J 433(2):263-276
    • (2011) Biochem J , vol.433 , Issue.2 , pp. 263-276
    • Robertson, I.1    Jensen, S.2    Handford, P.3
  • 19
    • 0023002893 scopus 로고
    • Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils
    • 10.1083/jcb.103.6.2499
    • Sakai L, Keene D, Engvall E (1986) Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils. J Cell Biol 103(6 Pt 1):2499-2509
    • (1986) J Cell Biol , vol.103 , Issue.6 PART 1 , pp. 2499-2509
    • Sakai, L.1    Keene, D.2    Engvall, E.3
  • 20
    • 0026315446 scopus 로고
    • Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils
    • Sakai LY, Keene DR, Glanville RW, Bachinger HP (1991) Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils. J Biol Chem 266(22):14763
    • (1991) J Biol Chem , vol.266 , Issue.22 , pp. 14763
    • Sakai, L.Y.1    Keene, D.R.2    Glanville, R.W.3    Bachinger, H.P.4
  • 22
    • 79953144610 scopus 로고    scopus 로고
    • Prodomains of transforming growth factor beta (TGFbeta) superfamily members specify different functions: Extracellular matrix interactions and growth factor bioavailability
    • 10.1074/jbc.M110.188615
    • Sengle G, Ono RN, Sasaki T, Sakai LY (2011) Prodomains of transforming growth factor beta (TGFbeta) superfamily members specify different functions: Extracellular matrix interactions and growth factor bioavailability. J Biol Chem 286(7):5087-5099
    • (2011) J Biol Chem , vol.286 , Issue.7 , pp. 5087-5099
    • Sengle, G.1    Ono, R.N.2    Sasaki, T.3    Sakai, L.Y.4
  • 23
    • 84863112496 scopus 로고    scopus 로고
    • Identification of helix capping and beta-turn motifs from NMR chemical shifts
    • 10.1007/s10858-012-9602-0
    • Shen Y, Bax A (2012) Identification of helix capping and beta-turn motifs from NMR chemical shifts. J Biomol NMR 52(3):211-232
    • (2012) J Biomol NMR , vol.52 , Issue.3 , pp. 211-232
    • Shen, Y.1    Bax, A.2
  • 24
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • 10.1007/s10858-009-9333-z
    • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213-223
    • (2009) J Biomol NMR , vol.44 , Issue.4 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 26
    • 0030781430 scopus 로고    scopus 로고
    • Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils
    • 10.1093/emboj/16.22.6659
    • Yuan X, Downing A, Knott V, Handford P (1997) Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils. EMBO J 16(22):6659-6666
    • (1997) EMBO J , vol.16 , Issue.22 , pp. 6659-6666
    • Yuan, X.1    Downing, A.2    Knott, V.3    Handford, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.