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Volumn 49, Issue 8, 2008, Pages 3483-3490

Visualization of in situ intracellular aggregation of two cataract-associated human γ-crystallin mutants: Lose a tail, lose transparency

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; ENHANCED GREEN FLUORESCENT PROTEIN; GAMMA CRYSTALLIN; GAMMA D CRYSTALLIN; MUTANT PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; CRYGC PROTEIN, HUMAN; CRYSTALLIN; CRYSTALLIN GAMMAD, HUMAN; GREEN FLUORESCENT PROTEIN;

EID: 49049106786     PISSN: 01460404     EISSN: 15525783     Source Type: Journal    
DOI: 10.1167/iovs.07-1114     Document Type: Article
Times cited : (20)

References (27)
  • 2
    • 0038071733 scopus 로고    scopus 로고
    • Crystallins, genes and cataract
    • Bhat SP. Crystallins, genes and cataract. Prog Drug Res. 2003;60:205-262.
    • (2003) Prog Drug Res , vol.60 , pp. 205-262
    • Bhat, S.P.1
  • 3
    • 0031979070 scopus 로고    scopus 로고
    • The genetics of cataract: Our vision becomes clearer
    • Hejtmancik JF. The genetics of cataract: our vision becomes clearer. Am J Hum Genet. 1998;62:520-525.
    • (1998) Am J Hum Genet , vol.62 , pp. 520-525
    • Hejtmancik, J.F.1
  • 4
    • 0033358423 scopus 로고    scopus 로고
    • The gamma crystallins and human cataracts: A puzzle made clearer
    • Heon L, Priston M, Schorderet DF, et al. The gamma crystallins and human cataracts: a puzzle made clearer. Am J Hum Genet. 1999;65:261-267.
    • (1999) Am J Hum Genet , vol.65 , pp. 261-267
    • Heon, L.1    Priston, M.2    Schorderet, D.F.3
  • 5
    • 0036093256 scopus 로고    scopus 로고
    • Novel mutations in the γ-crystallin genes cause autosomal dominant congenital cataracts
    • Santhiya ST, Shyam Manohar M, Rawlley D, et al. Novel mutations in the γ-crystallin genes cause autosomal dominant congenital cataracts. J Med Genet. 2002;39:352-358.
    • (2002) J Med Genet , vol.39 , pp. 352-358
    • Santhiya, S.T.1    Shyam Manohar, M.2    Rawlley, D.3
  • 6
    • 0034050880 scopus 로고    scopus 로고
    • Molecular basis of a progressive juvenile-onset hereditary cataract
    • Pande A, Pande J, Asherie N, et al. Molecular basis of a progressive juvenile-onset hereditary cataract. Proc Natl Acad Sci U S A. 2000;97:1993-1998.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1993-1998
    • Pande, A.1    Pande, J.2    Asherie, N.3
  • 7
    • 0035933113 scopus 로고    scopus 로고
    • Crystal cataracts: Human genetic cataract caused by protein crystallization
    • Pande A, Pande J, Asherie N, et al. Crystal cataracts: human genetic cataract caused by protein crystallization. Proc Natl Acad Sci U S A. 2001;98:6116-6120.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6116-6120
    • Pande, A.1    Pande, J.2    Asherie, N.3
  • 8
    • 0037449145 scopus 로고    scopus 로고
    • High-resolution X-ray crystal structures of human γD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract
    • Basak A, Bateman O, Slingsby C, et al. High-resolution X-ray crystal structures of human γD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract. J Mol Biol. 2003;328:1137-1147.
    • (2003) J Mol Biol , vol.328 , pp. 1137-1147
    • Basak, A.1    Bateman, O.2    Slingsby, C.3
  • 10
    • 14044262967 scopus 로고    scopus 로고
    • Pande A, Annunziata O, Asherie A, Ogun O, Benedek GB, Pande J. Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin. Biochemistry. 2005;44:2491-2500.
    • Pande A, Annunziata O, Asherie A, Ogun O, Benedek GB, Pande J. Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin. Biochemistry. 2005;44:2491-2500.
  • 11
    • 34248176794 scopus 로고    scopus 로고
    • Mutation causing self-aggregation in human γC-crystallin leading to congenital cataract
    • Talla V, Narayanan C, Srinivasan N, Balasubramanian D. Mutation causing self-aggregation in human γC-crystallin leading to congenital cataract. Invest Ophthalmol Vis Sci. 2006;47:5212-5217.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 5212-5217
    • Talla, V.1    Narayanan, C.2    Srinivasan, N.3    Balasubramanian, D.4
  • 12
    • 0037181130 scopus 로고    scopus 로고
    • Conformational change and destabilization of cataract γC-crystallin T5P mutant
    • Fu L, Liang JJ. Conformational change and destabilization of cataract γC-crystallin T5P mutant. FEBS Lett. 2002;513:213-216.
    • (2002) FEBS Lett , vol.513 , pp. 213-216
    • Fu, L.1    Liang, J.J.2
  • 13
    • 0033862351 scopus 로고    scopus 로고
    • Link between a novel human γD-crystallin allele and a unique cataract phenotype explained by protein crystallography
    • Kmoch S, Brynda J, Asfaw B, et al. Link between a novel human γD-crystallin allele and a unique cataract phenotype explained by protein crystallography. Hum Mol Genet. 2000;9:1779-1786.
    • (2000) Hum Mol Genet , vol.9 , pp. 1779-1786
    • Kmoch, S.1    Brynda, J.2    Asfaw, B.3
  • 15
  • 16
    • 0028777967 scopus 로고
    • Evidence for redox forms of the Aequorea green fluorescent protein
    • Inouye S, Tsuji FI. Evidence for redox forms of the Aequorea green fluorescent protein. FEBS Lett. 1994;341:277-280.
    • (1994) FEBS Lett , vol.341 , pp. 277-280
    • Inouye, S.1    Tsuji, F.I.2
  • 17
    • 0030933472 scopus 로고    scopus 로고
    • Conformational and functional differences between recombinant human lens αA-and αB-crystallin
    • Sun TX, Das BK, Liang JJ. Conformational and functional differences between recombinant human lens αA-and αB-crystallin. J Biol Chem. 1997;272:6220-6225.
    • (1997) J Biol Chem , vol.272 , pp. 6220-6225
    • Sun, T.X.1    Das, B.K.2    Liang, J.J.3
  • 19
    • 34248200380 scopus 로고
    • Comparative protein modeling by satisfaction of spatial constraints
    • Sali A, Blundell TL. Comparative protein modeling by satisfaction of spatial constraints. J Mol Biol. 1993;339:1103-1113.
    • (1993) J Mol Biol , vol.339 , pp. 1103-1113
    • Sali, A.1    Blundell, T.L.2
  • 20
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans SV. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J Mol Graphics. 1993;11:134-138.
    • (1993) J Mol Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 21
    • 34648813925 scopus 로고    scopus 로고
    • γD-crystallin-associated protein aggregation and lens fiber cell denucleation
    • Wang K, Cheng C, Li L, et al. γD-crystallin-associated protein aggregation and lens fiber cell denucleation. Invest Ophthalmol Vis Sci. 2007;48:3719-3728.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 3719-3728
    • Wang, K.1    Cheng, C.2    Li, L.3
  • 22
    • 27944468768 scopus 로고    scopus 로고
    • Lenticular chaperones suppress the aggregation of the cataract-causing mutant T5P γC-crystallin
    • Pigaga V, Quinlan RA. Lenticular chaperones suppress the aggregation of the cataract-causing mutant T5P γC-crystallin. Exp Cell Res. 2006;312:51-62.
    • (2006) Exp Cell Res , vol.312 , pp. 51-62
    • Pigaga, V.1    Quinlan, R.A.2
  • 23
    • 0032580087 scopus 로고    scopus 로고
    • Cloning and mapping of the mouse Crygc gene and non-lens expression of γS-crystallin
    • Sinha D, Esumi N, Jaworski C, Kozak CA, Pierce E, Wistow G. Cloning and mapping of the mouse Crygc gene and non-lens expression of γS-crystallin. Mol Vis. 1998;4:8.
    • (1998) Mol Vis , vol.4 , pp. 8
    • Sinha, D.1    Esumi, N.2    Jaworski, C.3    Kozak, C.A.4    Pierce, E.5    Wistow, G.6
  • 24
    • 23944461004 scopus 로고    scopus 로고
    • A potential role for β- and γ-crystallins in the vascular remodeling of the eye
    • Zhang C, Gehlbach P, Gongora C, et al. A potential role for β- and γ-crystallins in the vascular remodeling of the eye. Dev Dyn. 2005;234:36-47.
    • (2005) Dev Dyn , vol.234 , pp. 36-47
    • Zhang, C.1    Gehlbach, P.2    Gongora, C.3
  • 25
    • 0023988274 scopus 로고    scopus 로고
    • Mandal K, Kono M, Bose SK, Thomson J, Chakrabarti B. Structure and stability of gamma-crystallins, IV: aggregation and structural destabilization in photosensitized reactions. Photochem Photobiol. 1998;47:583-591.
    • Mandal K, Kono M, Bose SK, Thomson J, Chakrabarti B. Structure and stability of gamma-crystallins, IV: aggregation and structural destabilization in photosensitized reactions. Photochem Photobiol. 1998;47:583-591.
  • 26
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • Cardamone M, Puri NK. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem J. 1992;282:589-593.
    • (1992) Biochem J , vol.282 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 27
    • 0037372175 scopus 로고    scopus 로고
    • In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation
    • Kosinski-Collins MS, King J. In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation. Protein Sci. 2003;12:480-490.
    • (2003) Protein Sci , vol.12 , pp. 480-490
    • Kosinski-Collins, M.S.1    King, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.