메뉴 건너뛰기




Volumn 19, Issue 11, 2010, Pages 2231-2239

Phenotypic effects of Ehlers-Danlos syndrome-associated mutation on the FnIII domain of tenascin-X

Author keywords

Ehlers Danlos syndrome; Mechanotransduction; Molecular dynamics simulations; Mutation; Single molecule force spectroscopy; Tenascin X

Indexed keywords

COLLAGEN; FIBRONECTIN; SCLEROPROTEIN; TENASCIN; TENASCIN X; UNCLASSIFIED DRUG;

EID: 78349240376     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.503     Document Type: Article
Times cited : (7)

References (53)
  • 1
    • 0028859440 scopus 로고
    • Tenascins, a growing family of extracellular matrix proteins
    • Chiquet-Ehrismann R (1995) Tenascins, a growing family of extracellular matrix proteins. Experientia 51:853-862.
    • (1995) Experientia , vol.51 , pp. 853-862
    • Chiquet-Ehrismann, R.1
  • 3
    • 0027685702 scopus 로고
    • Tenascin-C, tenascin-R and tenascin-X: A family of talented proteins in search of functions
    • Erickson HP (1993) Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions. Curr Opin Cell Biol 5:869-876.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 4
    • 0034117025 scopus 로고    scopus 로고
    • The tenascin family of ECM glycoproteins: Structure, function, and regulation during embryonic development and tissue remodeling
    • Jones FS, Jones PL (2000) The tenascin family of ECM glycoproteins: structure, function, and regulation during embryonic development and tissue remodeling. Dev Dyn 218:235-259.
    • (2000) Dev Dyn , vol.218 , pp. 235-259
    • Jones, F.S.1    Jones, P.L.2
  • 6
    • 0033179677 scopus 로고    scopus 로고
    • Cell adhesion to tenascin-X. Mapping of cell adhesion sites and identification of integrin receptors
    • DOI 10.1046/j.1432-1327.1999.00563.x
    • Elefteriou F, Exposito JY, Garrone R, Lethias C (1999) Cell adhesion to tenascin-X mapping of cell adhesion sites and identification of integrin receptors. Eur J Biochem 263:840-848. (Pubitemid 29361958)
    • (1999) European Journal of Biochemistry , vol.263 , Issue.3 , pp. 840-848
    • Elefteriou, F.1    Exposito, J.-Y.2    Garrone, R.3    Lethias, C.4
  • 7
    • 0038236713 scopus 로고    scopus 로고
    • Tenascins: Regulation and putative functions during pathological stress
    • DOI 10.1002/path.1415
    • Chiquet-Ehrismann R, Chiquet M (2003) Tenascins: regulation and putative functions during pathological stress. J Pathol 200:488-499. (Pubitemid 36818249)
    • (2003) Journal of Pathology , vol.200 , Issue.4 , pp. 488-499
    • Chiquet-Ehrismann, R.1    Chiquet, M.2
  • 8
    • 34247640656 scopus 로고    scopus 로고
    • Wound healing in tenascin-X deficient mice suggests that tenascin-X is invloved in matrix maturation rather than matric deposition
    • DOI 10.1080/03008200601166160, PII 776294457
    • Egging D, van Vlijmen-Willems I, van Tongeren T, Schalkwijk J, Peeters A (2007) Wound healing in tenascin-X deficient mice suggests that tenascin-x is involved in matrix maturation rather than matrix deposition. Connect Tissue Res 48:93-98. (Pubitemid 46680961)
    • (2007) Connective Tissue Research , vol.48 , Issue.2 , pp. 93-98
    • Egging, D.1    Van Vlijmen-Willems, I.2    Van Tongeren, T.3    Schalkwijk, J.4    Peeters, A.5
  • 9
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: Converting force into biochemical signals
    • Vogel V (2006) Mechanotransduction involving multimodular proteins: converting force into biochemical signals. Annu Rev Biophys Biomol Struct 35:459-488.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 459-488
    • Vogel, V.1
  • 12
    • 2342470816 scopus 로고    scopus 로고
    • Ehlers-danlos syndrome - Molecular genetics beyond the collagens
    • DOI 10.1111/j.0022-202X.2004.22435.x
    • Uitto J, Ringpfeil F (2004) Ehlers-Danlos syndrome-molecular genetics beyond the collagens. J Invest Dermatol 122:xii-xiii. (Pubitemid 38580985)
    • (2004) Journal of Investigative Dermatology , vol.122 , Issue.4
    • Uitto, J.1    Ringpfeil, F.2
  • 14
    • 15844369376 scopus 로고    scopus 로고
    • Elastic fiber abnormalities in hypermobility type Ehlers-Danlos syndrome patients with tenascin-X mutations
    • DOI 10.1111/j.1399-0004.2005.00401.x
    • Zweers MC, Dean WB, van Kuppevelt TH, Bristow J, Schalkwijk J (2005) Elastic fiber abnormalities in hypermobility type Ehlers-Danlos syndrome patients with tenascin-X mutations. Clin Genet 67:330-334. (Pubitemid 40424829)
    • (2005) Clinical Genetics , vol.67 , Issue.4 , pp. 330-334
    • Zweers, M.C.1    Dean, W.B.2    Van Kuppevelt, T.H.3    Bristow, J.4    Schalkwijk, J.5
  • 16
    • 18244362337 scopus 로고    scopus 로고
    • Tenascin-X deficiency in autosomal recessive Ehlers-Danlos syndrome
    • DOI 10.1002/ajmg.a.30671
    • Bristow J, Carey W, Egging D, Schalkwijk J (2005) Tenascin-X, collagen, elastin, and the Ehlers-Danlos syndrome. Am J Med Genet C Semin Med Genet 139:24-30. (Pubitemid 40627669)
    • (2005) American Journal of Medical Genetics , vol.135 A , Issue.1 , pp. 75-80
    • Lindor, N.M.1    Bristow, J.2
  • 18
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 19
    • 74249106219 scopus 로고    scopus 로고
    • I-TASSER: Fully automated protein structure prediction in CASP8
    • Zhang Y (2009) I-TASSER: fully automated protein structure prediction in CASP8. Proteins 77:100-113.
    • (2009) Proteins , vol.77 , pp. 100-113
    • Zhang, Y.1
  • 20
    • 17644392830 scopus 로고    scopus 로고
    • TM-align: A protein structure alignment algorithm based on the TM-score
    • Zhang Y, Skolnick J (2005) TM-align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res 33:2302-2309.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2302-2309
    • Zhang, Y.1    Skolnick, J.2
  • 21
    • 33645793799 scopus 로고    scopus 로고
    • Structure modeling of all identified G protein-coupled receptors in the human genome
    • Zhang Y, Devries ME, Skolnick J (2006) Structure modeling of all identified G protein-coupled receptors in the human genome. PLoS Comput Biol 2:e13.
    • (2006) PLoS Comput Biol , vol.2
    • Zhang, Y.1    Devries, M.E.2    Skolnick, J.3
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, D.S.2    Thornton, J.M.3
  • 23
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • Wiederstein M, Sippl MJ (2007) ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res 35:W407-W410.
    • (2007) Nucleic Acids Res , vol.35
    • Wiederstein, M.1    Sippl, M.J.2
  • 24
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP (1992) Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258:987-991.
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendrickson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 25
    • 58149512051 scopus 로고    scopus 로고
    • Nanomechanical properties of Tenascin-X revealed by single-molecule force spectroscopy
    • Jollymore A, Lethias C, Peng Q, Cao Y, Li H (2009) Nanomechanical properties of Tenascin-X revealed by single-molecule force spectroscopy. J Mol Biol 385:1277-1286.
    • (2009) J Mol Biol , vol.385 , pp. 1277-1286
    • Jollymore, A.1    Lethias, C.2    Peng, Q.3    Cao, Y.4    Li, H.5
  • 26
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser AF, Marszalek PE, Erickson HP, Fernandez JM (1998) The molecular elasticity of the extracellular matrix protein tenascin. Nature 393:181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 27
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 30
    • 60849131856 scopus 로고    scopus 로고
    • Mechanical design of the third FnIII domain of tenascin-C
    • Peng Q, Zhuang S, Wang M, Cao Y, Khor Y, Li H (2009) Mechanical design of the third FnIII domain of tenascin-C. J Mol Biol 386:1327-1342.
    • (2009) J Mol Biol , vol.386 , pp. 1327-1342
    • Peng, Q.1    Zhuang, S.2    Wang, M.3    Cao, Y.4    Khor, Y.5    Li, H.6
  • 31
    • 20544465799 scopus 로고    scopus 로고
    • Mechanical unfolding of TNfn3: The unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation
    • Ng SP, Rounsevell RW, Steward A, Geierhaas CD, Williams PM, Paci E, Clarke J (2005) Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation. J Mol Biol 350:776-789.
    • (2005) J Mol Biol , vol.350 , pp. 776-789
    • Ng, S.P.1    Rounsevell, R.W.2    Steward, A.3    Geierhaas, C.D.4    Williams, P.M.5    Paci, E.6    Clarke, J.7
  • 34
    • 0032530836 scopus 로고    scopus 로고
    • A database of macromolecular motions
    • Gerstein M, Krebs W (1998) A database of macromolecular motions. Nucleic Acids Res 26:4280-4290.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4280-4290
    • Gerstein, M.1    Krebs, W.2
  • 35
    • 0036227252 scopus 로고    scopus 로고
    • Molecular dynamics simulations as a tool for improving protein stability
    • Pikkemaat MG, Linssen AB, Berendsen HJ, Janssen DB (2002) Molecular dynamics simulations as a tool for improving protein stability. Protein Eng 15:185-192.
    • (2002) Protein Eng , vol.15 , pp. 185-192
    • Pikkemaat, M.G.1    Linssen, A.B.2    Berendsen, H.J.3    Janssen, D.B.4
  • 36
    • 14744270583 scopus 로고    scopus 로고
    • Protein stability and ligand binding: New paradigms from in-silico experiments
    • Verma CS, Fischer S (2005) Protein stability and ligand binding: new paradigms from in-silico experiments. Biophys Chem 115:295-302.
    • (2005) Biophys Chem , vol.115 , pp. 295-302
    • Verma, C.S.1    Fischer, S.2
  • 37
    • 51749110001 scopus 로고    scopus 로고
    • Structure and dynamics of the anti-AMCV scFv(F8): Effects of selected mutations on the antigen combining site
    • Arcangeli C, Cantale C, Galeffi P, Rosato V (2008) Structure and dynamics of the anti-AMCV scFv(F8): effects of selected mutations on the antigen combining site. J Struct Biol 164:119-133.
    • (2008) J Struct Biol , vol.164 , pp. 119-133
    • Arcangeli, C.1    Cantale, C.2    Galeffi, P.3    Rosato, V.4
  • 38
    • 0022555901 scopus 로고
    • Study of protein dynamics by X-ray diffraction
    • Ringe D, Petsko GA (1986) Study of protein dynamics by X-ray diffraction. Meth Enzymol 131:389-433.
    • (1986) Meth Enzymol , vol.131 , pp. 389-433
    • Ringe, D.1    Petsko, G.A.2
  • 39
    • 0033955909 scopus 로고    scopus 로고
    • Protein thermal stability: Insights from atomic displacement parameters (B values)
    • Parthasarathy S, Murthy MR (2000) Protein thermal stability: insights from atomic displacement parameters (B values). Protein Eng 13:9-13.
    • (2000) Protein Eng , vol.13 , pp. 9-13
    • Parthasarathy, S.1    Murthy, M.R.2
  • 40
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus M, McCammon JA (2002) Molecular dynamics simulations of biomolecules. Nat Struct Biol 9:646-652.
    • (2002) Nat Struct Biol , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 41
    • 0031571127 scopus 로고    scopus 로고
    • Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin
    • Carr PA, Erickson HP, Palmer AG, III (1997) Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin. Structure 5:949-959.
    • (1997) Structure , vol.5 , pp. 949-959
    • Carr, P.A.1    Erickson, H.P.2    Palmer III, A.G.3
  • 42
    • 0031758464 scopus 로고    scopus 로고
    • Native protein fluctuations: The conformational-motion temperature and the inverse correlation of protein flexibility with protein stability
    • Tang KE, Dill KA (1998) Native protein fluctuations: the conformational-motion temperature and the inverse correlation of protein flexibility with protein stability. J Biomol Struct Dyn 16:397-411.
    • (1998) J Biomol Struct Dyn , vol.16 , pp. 397-411
    • Tang, K.E.1    Dill, K.A.2
  • 43
    • 47749116844 scopus 로고    scopus 로고
    • Cavity-creating mutations in Pseudomonas aeruginosa azurin: Effects on protein dynamics and stability
    • Gabellieri E, Balestreri E, Galli A, Cioni P (2008) Cavity-creating mutations in Pseudomonas aeruginosa azurin: effects on protein dynamics and stability. Biophys J 95:771-781.
    • (2008) Biophys J , vol.95 , pp. 771-781
    • Gabellieri, E.1    Balestreri, E.2    Galli, A.3    Cioni, P.4
  • 46
    • 49649083370 scopus 로고    scopus 로고
    • Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins
    • Cao Y, Yoo T, Li H (2008) Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins. Proc Natl Acad Sci USA 105:11152-11157.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11152-11157
    • Cao, Y.1    Yoo, T.2    Li, H.3
  • 47
    • 33748552058 scopus 로고    scopus 로고
    • Engineering proteins with novel mechanical properties by recombination of protein fragments
    • Sharma D, Cao Y, Li H (2006) Engineering proteins with novel mechanical properties by recombination of protein fragments. Angew Chem Int Ed Engl 45:5633-5638.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 5633-5638
    • Sharma, D.1    Cao, Y.2    Li, H.3
  • 49
    • 33746368361 scopus 로고    scopus 로고
    • Single molecule force spectroscopy reveals a weakly populated microstate of the FnIII domains of tenascin
    • Cao Y, Li H (2006) Single molecule force spectroscopy reveals a weakly populated microstate of the FnIII domains of tenascin. J Mol Biol 361:372-381.
    • (2006) J Mol Biol , vol.361 , pp. 372-381
    • Cao, Y.1    Li, H.2
  • 51
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems. J Chem Phys 98:10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 52
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert J, Ciccotti G, Berendsen H (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 23:327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.1    Ciccotti, G.2    Berendsen, H.3
  • 53


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.