메뉴 건너뛰기




Volumn 95, Issue 10, 2011, Pages 1457-1462

A novel mutation in transforming growth factor-beta induced protein (TGFβIp) reveals secondary structure perturbation in lattice corneal dystrophy

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; DOXYCYCLINE; GENOMIC DNA; MUTANT PROTEIN; SCLEROPROTEIN; TRANSFORMING GROWTH FACTOR BETA INDUCED PROTEIN; UNCLASSIFIED DRUG;

EID: 81155161831     PISSN: 00071161     EISSN: 14682079     Source Type: Journal    
DOI: 10.1136/bjophthalmol-2011-300651     Document Type: Article
Times cited : (24)

References (24)
  • 3
    • 0346670134 scopus 로고    scopus 로고
    • A model of FAS1 domain 4 of the corneal protein betaig-h3 gives a clearer view on corneal dystrophies
    • Clout NJ, Hohenester E. A model of FAS1 domain 4 of the corneal protein beta(ig)-h3 gives a clearer view on corneal dystrophies. Mol Vis 2003;9:440-8. (Pubitemid 38097612)
    • (2003) Molecular Vision , vol.9 , pp. 440-448
    • Clout, N.J.1    Hohenester, E.2
  • 4
    • 33745728355 scopus 로고    scopus 로고
    • TGFBI gene mutations in corneal dystrophies
    • Kannabiran C, Klintworth GK. TGFBI gene mutations in corneal dystrophies. Hum Mutat 2006;27:615-25.
    • (2006) Hum Mutat , vol.27 , pp. 615-625
    • Kannabiran, C.1    Klintworth, G.K.2
  • 5
    • 34748877706 scopus 로고    scopus 로고
    • TGFBIp/betaig-h3 protein: A versatile matrix molecule induced by TGF-beta
    • DOI 10.1016/j.biocel.2007.06.004, PII S1357272507002026
    • Thapa N, Lee BH, Kim IS. TGFBIp/betaig-h3 protein: a versatile matrix molecule induced by TGF-beta. Int J Biochem Cell Biol 2007;39:2183-94. (Pubitemid 47484277)
    • (2007) International Journal of Biochemistry and Cell Biology , vol.39 , Issue.12 , pp. 2183-2194
    • Thapa, N.1    Lee, B.-H.2    Kim, I.-S.3
  • 6
    • 0026783009 scopus 로고
    • CDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-beta
    • Skonier J, Neubauer M, Madisen L, et al. cDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-beta. DNA Cell Biol 1992;11:511-22.
    • (1992) DNA Cell Biol , vol.11 , pp. 511-522
    • Skonier, J.1    Neubauer, M.2    Madisen, L.3
  • 8
    • 0036184212 scopus 로고    scopus 로고
    • Molecular properties of wild-type and mutant betaIG-H3 proteins
    • Kim JE, Park RW, Choi JY, et al. Molecular properties of wild-type and mutant betaIG-H3 proteins. Invest Ophthalmol Vis Sci 2002;43:656-61.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 656-661
    • Kim, J.E.1    Park, R.W.2    Choi, J.Y.3
  • 9
    • 0034646599 scopus 로고    scopus 로고
    • Amyloid and non-amyloid forms of 5q31-linked corneal dystrophy resulting from kerato-epithelin mutations at Arg-124 are associated with abnormal turnover of the protein
    • DOI 10.1074/jbc.275.15.11465
    • Korvatska E, Henry H, Mashima Y, et al. Amyloid and non-amyloid forms of 5q31-linked corneal dystrophy resulting from kerato-epithelin mutations at Arg-124 are associated with abnormal turnover of the protein. J Biol Chem 2000;275:11465-9. (Pubitemid 30212801)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 11465-11469
    • Korvatska, E.1    Henry, H.2    Mashima, Y.3    Yamada, M.4    Bachmann, C.5    Munier, F.L.6    Schorderet, D.F.7
  • 10
    • 33644552779 scopus 로고    scopus 로고
    • Unilateral lattice corneal dystrophy associated with the novel His572del mutation in the TGFBI gene
    • Aldave AJ, Rayner SA, Kim BT, et al. Unilateral lattice corneal dystrophy associated with the novel His572del mutation in the TGFBI gene. Mol Vis 2006;12:142-6.
    • (2006) Mol Vis , vol.12 , pp. 142-146
    • Aldave, A.J.1    Rayner, S.A.2    Kim, B.T.3
  • 11
    • 0033852796 scopus 로고    scopus 로고
    • Linear extrapolation method of analyzing solvent denaturation curves
    • Pace CN, Shaw KL. Linear extrapolation method of analyzing solvent denaturation curves. Proteins 2000;9:1395-8.
    • (2000) Proteins , vol.9 , pp. 1395-1398
    • Pace, C.N.1    Shaw, K.L.2
  • 13
    • 0028175780 scopus 로고
    • A thermodynamic scale for the beta-sheet forming tendencies of the amino acids
    • Smith CK, Withka JM, Regan L. A thermodynamic scale for the beta-sheet forming tendencies of the amino acids. Biochemistry 1994;33:5510-17.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 17
    • 33749341780 scopus 로고    scopus 로고
    • A novel H572R mutation in the transforming growth factor-beta-induced gene in a Thai family with lattice corneal dystrophy type I
    • Atchaneeyasakul LO, Appukuttan B, Pingsuthiwong S, et al. A novel H572R mutation in the transforming growth factor-beta-induced gene in a Thai family with lattice corneal dystrophy type I. Jpn J Ophthalmol 2005;50:403-8.
    • (2005) Jpn J Ophthalmol , vol.50 , pp. 403-408
    • Atchaneeyasakul, L.O.1    Appukuttan, B.2    Pingsuthiwong, S.3
  • 18
    • 67650588816 scopus 로고    scopus 로고
    • Clinical and genetic features of TGFBI-linked corneal dystrophies in Mexican population: Description of novel mutations and novel genotype-phenotype correlations
    • Zenteno JC, Correa-Gomez V, Santacruz-Valdez C, et al. Clinical and genetic features of TGFBI-linked corneal dystrophies in Mexican population: description of novel mutations and novel genotype-phenotype correlations. Exp Eye Res 2009;89:172-7.
    • (2009) Exp Eye Res , vol.89 , pp. 172-177
    • Zenteno, J.C.1    Correa-Gomez, V.2    Santacruz-Valdez, C.3
  • 19
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006;75:333-66. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 20
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F, Dobson CM. Amyloid formation by globular proteins under native conditions. Nat Chem Biol 2009;5:15-22.
    • (2009) Nat Chem Biol , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 21
    • 77649259910 scopus 로고    scopus 로고
    • Denaturation and solvent effect on the conformation and fibril formation of TGFBIp
    • Grothe HL, Little MR, Cho AS, et al. Denaturation and solvent effect on the conformation and fibril formation of TGFBIp. Mol Vis 2009;15:2617-26.
    • (2009) Mol Vis , vol.15 , pp. 2617-2626
    • Grothe, H.L.1    Little, M.R.2    Cho, A.S.3
  • 23
    • 33846218303 scopus 로고    scopus 로고
    • Identification of an amyloidogenic region on keratoepithelin via synthetic peptides
    • DOI 10.1016/j.febslet.2006.12.019, PII S0014579306014566
    • Yuan C, Berscheit HL, Huang AJ. Identification of an amyloidogenic region on keratoepithelin via synthetic peptides. FEBS Lett 2007;581:241-7. (Pubitemid 46096466)
    • (2007) FEBS Letters , vol.581 , Issue.2 , pp. 241-247
    • Yuan, C.1    Berscheit, H.L.2    Huang, A.J.W.3
  • 24
    • 79953155808 scopus 로고    scopus 로고
    • Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1 domain of TGFBIp
    • Runager K, Basaiawmoit RV, Deva T, et al. Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1 domain of TGFBIp. J Biol Chem 2011;286:4951-8.
    • (2011) J Biol Chem , vol.286 , pp. 4951-4958
    • Runager, K.1    Basaiawmoit, R.V.2    Deva, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.