메뉴 건너뛰기




Volumn 13, Issue 3, 1999, Pages 395-402

Structure of the crystallins

Author keywords

Cataract; Crystallin; Domain fold; Evolution; Eye lens; Protein structure

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; CRYSTALLIN; GAMMA CRYSTALLIN; MUTANT PROTEIN;

EID: 0032789443     PISSN: 0950222X     EISSN: 14765454     Source Type: Journal    
DOI: 10.1038/eye.1999.113     Document Type: Article
Times cited : (88)

References (51)
  • 1
    • 84984776389 scopus 로고    scopus 로고
    • A searchlight through the fog
    • Wright AF. A searchlight through the fog. Nature Genet 1997;17:132-4.
    • (1997) Nature Genet , vol.17 , pp. 132-134
    • Wright, A.F.1
  • 3
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye M, Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 1983;302:415-7.
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 4
    • 0030954844 scopus 로고    scopus 로고
    • Cataract as a protein condensation disease. The proctor lecture
    • Benedek GB. Cataract as a protein condensation disease. The Proctor lecture. Invest Ophthalmol Vis Sci 1997;38:1911-21.
    • (1997) Invest Ophthalmol Vis Sci , vol.38 , pp. 1911-1921
    • Benedek, G.B.1
  • 6
    • 0028903455 scopus 로고
    • The expanding small heat shock protein family, and structure predictions of the conserved ‘α-crystallin domain’
    • Caspers G-J, Leunissen JAM, de Jong WW. The expanding small heat shock protein family, and structure predictions of the conserved ‘α-crystallin domain’. J Mol Evol 1995;40:238-48.
    • (1995) J Mol Evol , vol.40 , pp. 238-248
    • Caspers, G.-J.1    Leunissen, J.2    De Jong, W.W.3
  • 7
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heatshock protein
    • Kim KK, Kim R, Kim S-H. Crystal structure of a small heatshock protein. Nature 1998;394:595-9.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.-H.3
  • 8
    • 0024218965 scopus 로고    scopus 로고
    • The evolution of lenticular proteins: The β-and γ-crystallin super gene family
    • Lubsen NH, Aarts HJM, Schoenmakers JGG. The evolution of lenticular proteins: the β-and γ-crystallin super gene family. Prog Biophys Mol Bioi 1998;51:47-56.
    • (1998) Prog Biophys Mol Bioi , vol.51 , pp. 47-56
    • Lubsen, N.H.1    Aarts, H.2    Schoenmakers, J.G.G.3
  • 9
    • 0031555941 scopus 로고    scopus 로고
    • The domains in γb-crystallin: Identical fold-different stabilities
    • Mayr E-M, Jaenicke R, Glockshuber R. The domains in γB-crystallin: identical fold-different stabilities. J Mol Bioi 1997;269:260-9.
    • (1997) J Mol Bioi , vol.269 , pp. 260-269
    • Mayr, E.-M.1    Jaenicke, R.2    Glockshuber, R.3
  • 11
    • 0027984870 scopus 로고
    • Covalent modification at the c-terminal end of a 9 kda γd-crystallin fragment in human lenses
    • Strivastava OP, Strivastava K, Silney C. Covalent modification at the C-terminal end of a 9 kDa γD-crystallin fragment in human lenses. Exp Eye Res 1994;58:595-604.
    • (1994) Exp Eye Res , vol.58 , pp. 595-604
    • Strivastava, O.P.1    Strivastava, K.2    Silney, C.3
  • 12
    • 0023389564 scopus 로고
    • γ-crystallins of the human eye lens: Expression analysis of five members of the gene family
    • Meakin SO, Du RP, Tsui L-C, Breitman ML. γ-crystallins of the human eye lens: expression analysiS of five members of the gene family. Mol Cell Bioi 1987;7:2671-9.
    • (1987) Mol Cell Bioi , vol.7 , pp. 2671-2679
    • Meakin, S.O.1    Du, R.P.2    Tsui, L.-C.3    Breitman, M.L.4
  • 14
    • 0030710251 scopus 로고    scopus 로고
    • Towards a molecular understanding of phase separation in the lens: A comparison of the x-ray structures of two high tc γ-crystallins, γe and γf, with two low tc γ-crystallins, γb and γd
    • Norledge BV, Hay RE, Bateman OA, Slingsby C, Driessen HPC. Towards a molecular understanding of phase separation in the lens: a comparison of the X-ray structures of two high Tc γ-crystallins, γE and γF, with two low Tc γ-crystallins, γB and γD. Exp Eye Res 1997;65:609-30.
    • (1997) Exp Eye Res , vol.65 , pp. 609-630
    • Norledge, B.V.1    Hay, R.E.2    Bateman, O.A.3    Slingsby, C.4    Driessen, H.P.C.5
  • 16
    • 0032568962 scopus 로고    scopus 로고
    • Unusual domain pairing in a mutant of bovine lens γb-crystallin
    • Palme S, Jaenicke R, Slingsby C. Unusual domain pairing in a mutant of bovine lens γB-crystallin. J Mol Bioi 1998;279:1053-9.
    • (1998) J Mol Bioi , vol.279 , pp. 1053-1059
    • Palme, S.1    Jaenicke, R.2    Slingsby, C.3
  • 18
    • 0031952170 scopus 로고    scopus 로고
    • X-ray structures of three interface mutants of)lb-crystallin from bovine eye lens
    • Palme S, Jaenicke R, Slingsby C. X-ray structures of three interface mutants of γB-crystallin from bovine eye lens. Protein Sci 1998;7:611-8.
    • (1998) Protein Sci , vol.7 , pp. 611-618
    • Palme, S.1    Jaenicke, R.2    Slingsby, C.3
  • 19
    • 0025186133 scopus 로고
    • X-ray analysis of βb2-crystallin and evolution of oligomeric lens proteins
    • Bax B, Lapatto R, Nalini V, Driessen H, Lindley PF, Mahadevan D, et al. X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins. Nature 1990;347:776-80.
    • (1990) Nature , vol.347 , pp. 776-780
    • Bax, B.1    Lapatto, R.2    Nalini, V.3    Driessen, H.4    Lindley, P.F.5    Mahadevan, D.6
  • 20
    • 0028053274 scopus 로고
    • Domain interactions and connecting pep tides in lens crystallins
    • Mayr E-M, Jaenicke R, Glockshuber R. Domain interactions and connecting pep tides in lens crystallins. J Mol BioI 1994;235:84-8.
    • (1994) J Mol Bioi , vol.235 , pp. 84-88
    • Mayr, E.-M.1    Jaenicke, R.2    Glockshuber, R.3
  • 21
    • 0028171466 scopus 로고
    • Dimerization of βb2-crystallin: The role of the linker peptide and the n-and c-terminal extensions
    • Trinkl S, Glockshuber R, Jaenicke R. Dimerization of βB2-crystallin: the role of the linker peptide and the N-and C-terminal extensions. Protein Sci 1994;3:1392-400.
    • (1994) Protein Sci , vol.3 , pp. 1392-1400
    • Trinkl, S.1    Glockshuber, R.2    Jaenicke, R.3
  • 22
    • 0028169457 scopus 로고
    • Aggregation of βa3-crystallin is independent of the specific sequence of the domain connecting peptide
    • Hope IN, Chen H-C, Hejtmancik JF. Aggregation of βA3-crystallin is independent of the specific sequence of the domain connecting peptide. J BioI Chem 1994;269:21141-5.
    • (1994) J Bioi Chem , vol.269 , pp. 21141-21145
    • Hope, I.N.1    Chen, H.-C.2    Hejtmancik, J.F.3
  • 23
    • 0030847791 scopus 로고    scopus 로고
    • The x-ray structure of a mutant eye lens βb2-crystallin with truncated sequence extensions
    • Norledge BV, Trinkl S, Jaenicke R, Slingsby C. The X-ray structure of a mutant eye lens βB2-crystallin with truncated sequence extensions. Protein Sci 1997;6:1612-20.
    • (1997) Protein Sci , vol.6 , pp. 1612-1620
    • Norledge, B.V.1    Trinkl, S.2    Jaenicke, R.3    Slingsby, C.4
  • 24
    • 0032562996 scopus 로고    scopus 로고
    • Eye lens βb2-crystallin: Circular permutation does not influence the oligomerization state but enhances the conformational stability
    • Wieligmann K, Norledge B, Jaenicke R, Mayr E-M. Eye lens βB2-crystallin: circular permutation does not influence the oligomerization state but enhances the conformational stability. J Mol BioI 1998;280:721-9.
    • (1998) J Mol Bioi , vol.280 , pp. 721-729
    • Wieligmann, K.1    Norledge, B.2    Jaenicke, R.3    Mayr, E.-M.4
  • 26
    • 0025371285 scopus 로고
    • Quaternary interactions in eye lens β-crystallins: Basic and acidic subunits of [3-crystallins favour heterologous association
    • Slingsby C, Bateman OA. Quaternary interactions in eye lens β-crystallins: basic and acidic subunits of [3-crystallins favour heterologous association. Biochemistry 1990;29:6592-9.
    • (1990) Biochemistry , vol.29 , pp. 6592-6599
    • Slingsby, C.1    Bateman, O.A.2
  • 27
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by hplc and mass spectrometry
    • Ma Z, Hanson SRA, Lampi KJ, David LL, Smith DL, Smith JB. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp Eye Res 1998;67:21-30.
    • (1998) Exp Eye Res , vol.67 , pp. 21-30
    • Ma, Z.1    Hanson, S.2    Lampi, K.J.3    David, L.L.4    Smith, D.L.5    Smith, J.B.6
  • 28
    • 0032128377 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry
    • Lampi KJ, Ma Z, Hanson SRA, Azuma M, Shih M, Shearer TR, et al. Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry. Exp Eye Res 1998;67:31-43.
    • (1998) Exp Eye Res , vol.67 , pp. 31-43
    • Lampi, K.J.1    Ma, Z.2    Hanson, S.3    Azuma, M.4    Shih, M.5    Shearer, T.R.6
  • 29
    • 0030893023 scopus 로고    scopus 로고
    • Size of human lens β-crystallin aggregates are distinguished by n-terminal truncation of [3b1
    • Ajaz MS, Ma Z, Smith DL, Smith JB. Size of human lens β-crystallin aggregates are distinguished by N-terminal truncation of [3B1. J BioI Chem 1997;272:11250-5.
    • (1997) J Bioi Chem , vol.272 , pp. 11250-11255
    • Ajaz, M.S.1    Ma, Z.2    Smith, D.L.3    Smith, J.B.4
  • 30
    • 0028280702 scopus 로고
    • Close packing of an oligomeric eye lens β-crystallin induces loss of symmetry and ordering of sequence extensions
    • Nalini V, Bax B, Driessen H, Moss DS, Lindley PF, Slingsby C. Close packing of an oligomeric eye lens β-crystallin induces loss of symmetry and ordering of sequence extensions. J Mol BioI 1994;236:1250-8.
    • (1994) J Mol Bioi , vol.236 , pp. 1250-1258
    • Nalini, V.1    Bax, B.2    Driessen, H.3    Moss, D.S.4    Lindley, P.F.5    Slingsby, C.6
  • 31
    • 84984930927 scopus 로고
    • Molecular biology and evolution of crystallins: Gene recruitment and multifunctional proteins in the eye lens
    • Wistow G. Molecular biology and evolution of crystallins: gene recruitment and multifunctional proteins in the eye lens. Austin/New York: RG Landes/Springer, 1995.
    • (1995) Austin/New York: RG Landes/Springer
    • Wistow, G.1
  • 33
    • 0031006549 scopus 로고    scopus 로고
    • Aim1, a novel non-lens member of the βγ-crystallin superfamily, is associated with the control of tumorigenicity in human malignant melanoma
    • Ray ME, Wistow G, Su YA, Meltzer PS, Trent JM. AIM1, a novel non-lens member of the βγ-crystallin superfamily, is associated with the control of tumorigenicity in human malignant melanoma. Proc Natl Acad Sci USA 1997;94:3229-34.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3229-3234
    • Ray, M.E.1    Wistow, G.2    Su, Y.A.3    Meltzer, P.S.4    Trent, J.M.5
  • 34
    • 84984931496 scopus 로고    scopus 로고
    • Cloning and mapping the mouse Crygs gene and non-lens expression of γ S-crystallin
    • Sinha D, Esumi N, Jaworski C, Kozak CA, Pierce E, Wistow G. Cloning and mapping the mouse Crygs gene and non-lens expression of γ S-crystallin. 1998. http://www.molvis.org/molvis/v4/p8.
    • (1998)
    • Sinha, D.1    Esumi, N.2    Jaworski, C.3    Kozak, C.A.4    Pierce, E.5    Wistow, G.6
  • 35
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992;89:10449-53.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 37
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain substrate in a folding-competent state
    • Lee GJ, Roseman AM, Saibil HR, Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain substrate in a folding-competent state. EMBO J 1997;16:659-71.
    • (1997) EMBO J , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 38
    • 0031979070 scopus 로고    scopus 로고
    • The genetics of cataract: Our vision becomes clearer
    • Heljmancik JF. The genetics of cataract: our vision becomes clearer. Am J Genet 1998;62:520-5.
    • (1998) Am J Genet , vol.62 , pp. 520-525
    • Heljmancik, J.F.1
  • 41
    • 0026731884 scopus 로고
    • Structural studies on βh-crystallin from bovine eye lens
    • Bateman OA, Slingsby C. Structural studies on βH-crystallin from bovine eye lens. Exp Eye Res 1992;55:127-33.
    • (1992) Exp Eye Res , vol.55 , pp. 127-133
    • Bateman, O.A.1    Slingsby, C.2
  • 42
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene cryaa
    • Litt M, Kramer P, LaMorticella DM, Murphey W, Lovrien EW, Weleber RG. Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 1998;7:471-4.
    • (1998) Hum Mol Genet , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 43
    • 0025778685 scopus 로고
    • Deletion mutation in an eye lens β-crystallin
    • Chambers C, Russell P. Deletion mutation in an eye lens β-crystallin. J BioI Chem 1991;266:6742-6.
    • (1991) J Bioi Chem , vol.266 , pp. 6742-6746
    • Chambers, C.1    Russell, P.2
  • 44
    • 0025295355 scopus 로고
    • Interaction of an altered β-crystallin with other proteins in the philly mouse lens
    • Russell P, Chambers C. Interaction of an altered β-crystallin with other proteins in the Philly mouse lens. Exp Eye Res 1990;50:683-7.
    • (1990) Exp Eye Res , vol.50 , pp. 683-687
    • Russell, P.1    Chambers, C.2
  • 45
    • 0026921910 scopus 로고
    • A frameshift mutation in the γe-crystallin gene of the elo mouse
    • Cartier M, Breitman ML, Tsui LC. A frameshift mutation in the γE-crystallin gene of the Elo mouse. Nature Genet 1992;2:42-5.
    • (1992) Nature Genet , vol.2 , pp. 42-45
    • Cartier, M.1    Breitman, M.L.2    Tsui, L.C.3
  • 46
    • 0031283282 scopus 로고    scopus 로고
    • Disruption of 013 connexin gene leads to proteolysis and cataractogenesis in mice
    • Gong X, Li E, Klier G, Huang Q, Wu Y, Lei H, et al. Disruption of 013 connexin gene leads to proteolysis and cataractogenesis in mice. Cell 1997;91:833-43.
    • (1997) Cell , vol.91 , pp. 833-843
    • Gong, X.1    Li, E.2    Klier, G.3    Huang, Q.4    Wu, Y.5    Lei, H.6
  • 47
    • 0031959735 scopus 로고    scopus 로고
    • A missense mutation in the human connexin 50 gene (Gja8) underlines autosomal dominant ‘zonular pulverulent’ cataract, on chromosome 1q
    • Shiels A, Mackay D, Ionides A, Berry V, Moore A, Bhattacharya S. A missense mutation in the human connexin 50 gene (GJA8) underlines autosomal dominant ‘zonular pulverulent’ cataract, on chromosome 1q. Am J Hum Genet 1998;62:526-32.
    • (1998) Am J Hum Genet , vol.62 , pp. 526-532
    • Shiels, A.1    Mackay, D.2    Ionides, A.3    Berry, V.4    Moore, A.5    Bhattacharya, S.6
  • 48
    • 0029986488 scopus 로고    scopus 로고
    • The nucleus of the human lens: Demonstration of a highly characteristic protein pattern by 2d electrophoresis and introduction of new method of lens dissection
    • Garland DL, Duglas-Tabor Y, Jimenez-Asensio J, Datiles MB, Magno B. The nucleus of the human lens: demonstration of a highly characteristic protein pattern by 2D electrophoresis and introduction of new method of lens dissection. Exp Eye Res 1996;62:285-91.
    • (1996) Exp Eye Res , vol.62 , pp. 285-291
    • Garland, D.L.1    Duglas-Tabor, Y.2    Jimenez-Asensio, J.3    Datiles, M.B.4    Magno, B.5
  • 50
    • 0031126762 scopus 로고    scopus 로고
    • Disulphide bond formation of cysteine-37 and cysteine-66 of βb2 crystallin during cataractogenesis of the human lens
    • Takemoto LJ. Disulphide bond formation of cysteine-37 and cysteine-66 of βB2 crystallin during cataractogenesis of the human lens. Exp Eye Res 1997;64:609-14.
    • (1997) Exp Eye Res , vol.64 , pp. 609-614
    • Takemoto, L.J.1
  • 51
    • 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;11:134-8.
    • (1993) J Mol Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.