메뉴 건너뛰기




Volumn 108, Issue 2, 2011, Pages 574-579

Cataract-associated mutant E107A of human γD-crystallin shows increased attraction to α-crystallin and enhanced light scattering

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALPHA CRYSTALLIN; GAMMA CRYSTALLIN; GLUTAMIC ACID; TRYPTOPHAN;

EID: 79551672297     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1014653107     Document Type: Article
Times cited : (55)

References (40)
  • 1
    • 39149086399 scopus 로고    scopus 로고
    • Congenital cataracts and their molecular genetics
    • Hejtmancik JF (2008) Congenital cataracts and their molecular genetics. Semin Cell Dev Biol 19:134-149.
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 134-149
    • Hejtmancik, J.F.1
  • 2
    • 0015022316 scopus 로고
    • Theory of transparency of the eye
    • Benedek GB (1971) Theory of transparency of the eye. Appl Opt 10:459-473.
    • (1971) Appl Opt , vol.10 , pp. 459-473
    • Benedek, G.B.1
  • 3
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins account for eye lens transparency
    • DOI 10.1038/302415a0
    • Delaye M, Tardieu A (1983) Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302:415-417. (Pubitemid 13164324)
    • (1983) Nature , vol.302 , Issue.5907 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 4
    • 33845425645 scopus 로고    scopus 로고
    • Crystallins in the eye: Function and pathology
    • Andley UP (2007) Crystallins in the eye: Function and pathology. Prog Retin Eye Res 26:78-98.
    • (2007) Prog Retin Eye Res , vol.26 , pp. 78-98
    • Andley, U.P.1
  • 6
    • 0030954844 scopus 로고    scopus 로고
    • Cataract as a protein condensation disease: The Proctor lecture
    • Benedek GB (1997) Cataract as a protein condensation disease: The Proctor lecture. Invest Ophth Vis Sci 38:1911-1921.
    • (1997) Invest Ophth Vis Sci , vol.38 , pp. 1911-1921
    • Benedek, G.B.1
  • 9
    • 13044250483 scopus 로고    scopus 로고
    • Progressive juvenile-onset punctate cataracts caused by mutation of the gammaD-crystallin gene
    • Stephan DA, et al. (1999) Progressive juvenile-onset punctate cataracts caused by mutation of the gammaD-crystallin gene. Proc Natl Acad Sci USA 96:1008-1012.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1008-1012
    • Stephan, D.A.1
  • 10
    • 66649096748 scopus 로고    scopus 로고
    • The cataract-associated R14C mutant of human gamma D-crystallin shows a variety of intermolecular disulfide cross-links: A Raman spectroscopic study
    • Pande A, Gillot D, Pande J (2009) The cataract-associated R14C mutant of human gamma D-crystallin shows a variety of intermolecular disulfide cross-links: A Raman spectroscopic study. Biochemistry 48:4937-4945.
    • (2009) Biochemistry , vol.48 , pp. 4937-4945
    • Pande, A.1    Gillot, D.2    Pande, J.3
  • 13
    • 14044262967 scopus 로고    scopus 로고
    • Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gammaD-crystallin
    • DOI 10.1021/bi0479611
    • Pande A, et al. (2005) Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin. Biochemistry 44:2491-2500. (Pubitemid 40279552)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2491-2500
    • Pande, A.1    Annunziata, O.2    Asherie, N.3    Ogun, O.4    Benedek, G.B.5    Pande, J.6
  • 14
    • 0037181130 scopus 로고    scopus 로고
    • Conformational change and destabilization of cataract gammaC-crystallin T5P mutant
    • Fu L, Liang JJ (2002) Conformational change and destabilization of cataract gammaC-crystallin T5P mutant. FEBS Lett 513:213-216.
    • (2002) FEBS Lett , vol.513 , pp. 213-216
    • Fu, L.1    Liang, J.J.2
  • 15
    • 27944468768 scopus 로고    scopus 로고
    • Lenticular chaperones suppress the aggregation of the cataract-causing mutant T5P gamma C-crystallin
    • Pigaga V, Quinlan RA (2006) Lenticular chaperones suppress the aggregation of the cataract-causing mutant T5P gamma C-crystallin. Exp Cell Res 312:51-62.
    • (2006) Exp Cell Res , vol.312 , pp. 51-62
    • Pigaga, V.1    Quinlan, R.A.2
  • 16
    • 33747832463 scopus 로고    scopus 로고
    • Two affected siblings with nuclear cataract associated with a novel missense mutation in the CRYGD gene
    • Messina-Baas OM, Gonzalez-Huerta LM, Cuevas-Covarrubias SA (2006) Two affected siblings with nuclear cataract associated with a novel missense mutation in the CRYGD gene. Mol Vis 12:995-1000.
    • (2006) Mol Vis , vol.12 , pp. 995-1000
    • Messina-Baas, O.M.1    Gonzalez-Huerta, L.M.2    Cuevas-Covarrubias, S.A.3
  • 17
    • 0032536563 scopus 로고    scopus 로고
    • +-ions with alpha-crystallin: Solvent accessibility of ionizable side chains and surface charge
    • DOI 10.1016/S0301-4622(97)00130-0, PII S0301462297001300
    • Bera S, Ghosh SK (1998) Interaction of H(+)-ions with alpha-crystallin: Solvent accessibility of ionizable side chains and surface charge. Biophys Chem 70:147-160. (Pubitemid 28138817)
    • (1998) Biophysical Chemistry , vol.70 , Issue.2 , pp. 147-160
    • Bera, S.1    Ghosh, S.K.2
  • 18
    • 0032077168 scopus 로고    scopus 로고
    • Thermodynamic stability of bovine alpha-crystallin in its interactions with other bovine crystallins
    • Bettelheim FA, Chen A (1998) Thermodynamic stability of bovine alpha-crystallin in its interactions with other bovine crystallins. Int J Biol Macromol 22:247-252.
    • (1998) Int J Biol Macromol , vol.22 , pp. 247-252
    • Bettelheim, F.A.1    Chen, A.2
  • 19
    • 56349133640 scopus 로고    scopus 로고
    • Protein-protein interactions and lens transparency
    • Takemoto L, Sorensen CM (2008) Protein-protein interactions and lens transparency. Exp Eye Res 87:496-501.
    • (2008) Exp Eye Res , vol.87 , pp. 496-501
    • Takemoto, L.1    Sorensen, C.M.2
  • 20
    • 36048973994 scopus 로고    scopus 로고
    • New insight into cataract formation: Enhanced stability through mutual attraction
    • Stradner A, Foffi G, Dorsaz N, Thurston G, Schurtenberger P (2007) New insight into cataract formation: Enhanced stability through mutual attraction. Phys Rev Lett 99:198103.
    • (2007) Phys Rev Lett , vol.99 , pp. 198103
    • Stradner, A.1    Foffi, G.2    Dorsaz, N.3    Thurston, G.4    Schurtenberger, P.5
  • 21
    • 34547649473 scopus 로고    scopus 로고
    • Liquid-liquid phase separation and static light scattering of concentrated ternary mixtures of bovine alpha and gammaB crystallins
    • Thurston GM (2006) Liquid-liquid phase separation and static light scattering of concentrated ternary mixtures of bovine alpha and gammaB crystallins. J Chem Phys 124:134909.
    • (2006) J Chem Phys , vol.124 , pp. 134909
    • Thurston, G.M.1
  • 22
    • 62149088915 scopus 로고    scopus 로고
    • Colloidal characterization and thermodynamic stability of binary eye lens protein mixtures
    • Dorsaz N, Thurston GM, Stradner A, Schurtenberger P, Foffi G (2009) Colloidal characterization and thermodynamic stability of binary eye lens protein mixtures. J Phys Chem B 113:1693-1709.
    • (2009) J Phys Chem B , vol.113 , pp. 1693-1709
    • Dorsaz, N.1    Thurston, G.M.2    Stradner, A.3    Schurtenberger, P.4    Foffi, G.5
  • 23
    • 0027342592 scopus 로고
    • Proctor Lecture. The function of alpha-crystallin
    • Horwitz J (1993) Proctor Lecture. The function of alpha-crystallin. Invest Ophth Vis Sci 34:10-22.
    • (1993) Invest Ophth Vis Sci , vol.34 , pp. 10-22
    • Horwitz, J.1
  • 24
    • 0024365241 scopus 로고
    • The protein concentration gradient within eye lens might originate from constant osmotic pressure coupled to differential interactive properties of crystallins
    • Veretout F, Tardieu A (1989) The protein concentration gradient within eye lens might originate from constant osmotic pressure coupled to differential interactive properties of crystallins. Eur Biophys J 17:61-68.
    • (1989) Eur Biophys J , vol.17 , pp. 61-68
    • Veretout, F.1    Tardieu, A.2
  • 26
    • 34247096110 scopus 로고    scopus 로고
    • A reference dataset for circular dichroism spectroscopy tailored for the betagamma-crystallin lens proteins
    • Evans P, Bateman OA, Slingsby C, Wallace BA (2007) A reference dataset for circular dichroism spectroscopy tailored for the betagamma-crystallin lens proteins. Exp Eye Res 84:1001-1008.
    • (2007) Exp Eye Res , vol.84 , pp. 1001-1008
    • Evans, P.1    Bateman, O.A.2    Slingsby, C.3    Wallace, B.A.4
  • 27
    • 0022352190 scopus 로고
    • Structure and stability of gammacrystallins. I. Spectroscopic evaluation of secondary and tertiary structure in solution
    • Mandal K, Bose SK, Chakrabarti B, Siezen RJ (1985) Structure and stability of gammacrystallins. I. Spectroscopic evaluation of secondary and tertiary structure in solution. Biochim Biophys Acta 832:156-164.
    • (1985) Biochim Biophys Acta , vol.832 , pp. 156-164
    • Mandal, K.1    Bose, S.K.2    Chakrabarti, B.3    Siezen, R.J.4
  • 28
    • 77954821049 scopus 로고    scopus 로고
    • Increase in surface hydrophobicity of the cataract-associated P23T mutant of human gammaD-crystallin is responsible for its dramatically lower, retrograde solubility
    • Pande A, Ghosh KS, Banerjee PR, Pande J (2010) Increase in surface hydrophobicity of the cataract-associated P23T mutant of human gammaD-crystallin is responsible for its dramatically lower, retrograde solubility. Biochemistry 49:6122-6129.
    • (2010) Biochemistry , vol.49 , pp. 6122-6129
    • Pande, A.1    Ghosh, K.S.2    Banerjee, P.R.3    Pande, J.4
  • 29
    • 49749093086 scopus 로고    scopus 로고
    • On a partial differential equation method for determining the free energies and coexisting phase compositions of ternary mixtures from light scattering data
    • Ross DS, Thurston GM, Lutzer CV (2008) On a partial differential equation method for determining the free energies and coexisting phase compositions of ternary mixtures from light scattering data. J Chem Phys 129:064106.
    • (2008) J Chem Phys , vol.129 , pp. 064106
    • Ross, D.S.1    Thurston, G.M.2    Lutzer, C.V.3
  • 30
    • 0008679116 scopus 로고
    • Opacification of gamma-crystallin solutions from calf lens in relation to cold cataract formation
    • Siezen RJ, Fisch MR, Slingsby C, Benedek GB (1985) Opacification of gamma-crystallin solutions from calf lens in relation to cold cataract formation. Proc Natl Acad Sci USA 82:1701-1705.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1701-1705
    • Siezen, R.J.1    Fisch, M.R.2    Slingsby, C.3    Benedek, G.B.4
  • 31
    • 0030040281 scopus 로고    scopus 로고
    • Phase separation in aqueous solutions of lens gamma-crystallins: Special role of gamma s
    • Liu C, et al. (1996) Phase separation in aqueous solutions of lens gamma-crystallins: Special role of gamma s. Proc Natl Acad Sci USA 93:377-382.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 377-382
    • Liu, C.1
  • 32
    • 0037449145 scopus 로고    scopus 로고
    • High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract
    • DOI 10.1016/S0022-2836(03)00375-9
    • Basak A, et al. (2003) High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract. J Mol Biol 328:1137-1147. (Pubitemid 36506879)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.5 , pp. 1137-1147
    • Basak, A.1    Bateman, O.2    Slingsby, C.3    Pande, A.4    Asherie, N.5    Ogun, O.6    Benedek, G.B.7    Pande, J.8
  • 33
    • 77957296137 scopus 로고    scopus 로고
    • Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function
    • Laganowsky A, et al. (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci 19:1031-1043.
    • (2010) Protein Sci , vol.19 , pp. 1031-1043
    • Laganowsky, A.1
  • 34
    • 0023271853 scopus 로고
    • The refractive increments of bovine alpha-, beta-, and gamma-crystallins
    • Pierscionek B, Smith G, Augusteyn RC (1987) The refractive increments of bovine alpha-, beta-, and gamma-crystallins. Vision Res 27:1539-1541.
    • (1987) Vision Res , vol.27 , pp. 1539-1541
    • Pierscionek, B.1    Smith, G.2    Augusteyn, R.C.3
  • 36
    • 0032562286 scopus 로고    scopus 로고
    • Inhibition of assembly of bacterial cell division protein FtsZ by the hydrophobic dye 5,5′-bis-(8-anilino-1-naphthalenesulfonate)
    • Yu XC, Margolin W (1998) Inhibition of assembly of bacterial cell division protein FtsZ by the hydrophobic dye 5,5′-bis-(8-anilino-1- naphthalenesulfonate). J Biol Chem 273:10216-10222.
    • (1998) J Biol Chem , vol.273 , pp. 10216-10222
    • Yu, X.C.1    Margolin, W.2
  • 37
    • 0028970270 scopus 로고
    • Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes
    • Ruvinov SB, et al. (1995) Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes. J Biol Chem 270:6357-6369.
    • (1995) J Biol Chem , vol.270 , pp. 6357-6369
    • Ruvinov, S.B.1
  • 38
    • 0026228560 scopus 로고
    • Structural properties of polydisperse biopolymer solutions: A light scattering study of bovine alpha-crystallin
    • Schurtenberger P, Augusteyn RC (1991) Structural properties of polydisperse biopolymer solutions: A light scattering study of bovine alpha-crystallin. Biopolymers 31:1229-1240.
    • (1991) Biopolymers , vol.31 , pp. 1229-1240
    • Schurtenberger, P.1    Augusteyn, R.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.