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Volumn 77, Issue 4, 2003, Pages 409-422

The stability of human acidic β-crystallin oligomers and hetero-oligomers

Author keywords

Age related cataract; CD and fluorescence spectroscopy; Crystallins; Denaturation; Eye lens; Sequence extensions; Stability

Indexed keywords

BETA CRYSTALLIN; OLIGOMER; PROTEIN SUBUNIT;

EID: 0041382747     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4835(03)00173-8     Document Type: Article
Times cited : (69)

References (34)
  • 1
    • 0030893023 scopus 로고    scopus 로고
    • Size of human lens βcrystallin aggregates are distinguished by N-terminal truncation of βB1
    • Ajaz M.S., Ma Z., Smith D.L., Smith J.B. Size of human lens βcrystallin aggregates are distinguished by N-terminal truncation of βB1. J. Biol. Chem. 272:1997;11250-11255.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11250-11255
    • Ajaz, M.S.1    Ma, Z.2    Smith, D.L.3    Smith, J.B.4
  • 2
    • 0034771090 scopus 로고    scopus 로고
    • Association behaviour of human βB1-crystallin and its truncated forms
    • Bateman O.A., Lubsen N.H., Slingsby C. Association behaviour of human βB1-crystallin and its truncated forms. Exp. Eye Res. 73:2001;321-331.
    • (2001) Exp. Eye Res. , vol.73 , pp. 321-331
    • Bateman, O.A.1    Lubsen, N.H.2    Slingsby, C.3
  • 4
    • 0037450579 scopus 로고    scopus 로고
    • Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone
    • Callis P.R., Vivian J.T. Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone. Chem. Phys. Lett. 369:2003;409-414.
    • (2003) Chem. Phys. Lett. , vol.369 , pp. 409-414
    • Callis, P.R.1    Vivian, J.T.2
  • 5
    • 0027339842 scopus 로고
    • 1NMR spectroscopy of βB2-crystallin from bovine eye lens: Conformation of the N- and C-terminal extensions
    • 1NMR spectroscopy of βB2-crystallin from bovine eye lens: conformation of the N- and C-terminal extensions. Eur. J. Biochem. 213:1993;313-320.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 313-320
    • Carver, J.A.1    Cooper, P.G.2    Truscott, R.J.W.3
  • 6
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen Y., Barkley M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry. 37:1998;9976-9982.
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 7
    • 0029664615 scopus 로고    scopus 로고
    • The sequence of human βB1-crystallin cDNA allows mass spectrometric detection of βB1 protein missing portions of its N-terminal extension
    • David L.L., Lampi K.J., Lund A.L., Smith J.B. The sequence of human βB1-crystallin cDNA allows mass spectrometric detection of βB1 protein missing portions of its N-terminal extension. J. Biol. Chem. 271:1996;4273-4279.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4273-4279
    • David, L.L.1    Lampi, K.J.2    Lund, A.L.3    Smith, J.B.4
  • 8
    • 0033829222 scopus 로고    scopus 로고
    • The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
    • Hanson S.R.A., Hasan A., Smith D.L., Smith J.B. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp. Eye Res. 71:2000;195-207.
    • (2000) Exp. Eye Res. , vol.71 , pp. 195-207
    • Hanson, S.R.A.1    Hasan, A.2    Smith, D.L.3    Smith, J.B.4
  • 9
    • 0036597985 scopus 로고    scopus 로고
    • Viewing molecular mechanisms of ageing through a lens
    • Harding J.J. Viewing molecular mechanisms of ageing through a lens. Ageing Res. Rev. 1:2002;465-479.
    • (2002) Ageing Res. Rev. , vol.1 , pp. 465-479
    • Harding, J.J.1
  • 10
    • 0034486034 scopus 로고    scopus 로고
    • The function of alpha-crystallin in vision
    • Horwitz J. The function of alpha-crystallin in vision. Semin. Cell Dev. Biol. 11:2000;53-60.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 53-60
    • Horwitz, J.1
  • 13
    • 0035167113 scopus 로고    scopus 로고
    • Lens crystallins and their microbial homologs: Structure, stability, and function
    • Jaenicke R., Slingsby C. Lens crystallins and their microbial homologs: structure, stability, and function. Crit. Rev. Biochem. Mol. Biol. 36:2001;435-499.
    • (2001) Crit. Rev. Biochem. Mol. Biol. , vol.36 , pp. 435-499
    • Jaenicke, R.1    Slingsby, C.2
  • 16
    • 0036841037 scopus 로고    scopus 로고
    • Incidence of age-related cataract over a 10-year interval: The Beaver Dam Eye Study
    • Klein B.E.K., Klein R., Lee K.E. Incidence of age-related cataract over a 10-year interval: The Beaver Dam Eye Study. Ophthalmology. 109:2002;2052-2057.
    • (2002) Ophthalmology , vol.109 , pp. 2052-2057
    • Klein, B.E.K.1    Klein, R.2    Lee, K.E.3
  • 17
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in peptide and protein analysis
    • R.A. Meyers. Chichester: Wiley
    • Ladokhin A.S. Fluorescence spectroscopy in peptide and protein analysis. Meyers R.A. Encyclopedia of Analytical Chemistry. 2000;5762-5779 Wiley, Chichester.
    • (2000) Encyclopedia of Analytical Chemistry , pp. 5762-5779
    • Ladokhin, A.S.1
  • 19
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by HPLC and mass spectrometry
    • Ma Z., Hanson S.R.A., Lampi K.J., David L.L., Smith D.L., Smith J.B. Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp. Eye Res. 67:1998;21-30.
    • (1998) Exp. Eye Res. , vol.67 , pp. 21-30
    • Ma, Z.1    Hanson, S.R.A.2    Lampi, K.J.3    David, L.L.4    Smith, D.L.5    Smith, J.B.6
  • 21
    • 0023777949 scopus 로고
    • Heat-induced changes in the conformation of α- and β-crystallins: Unique thermal stability of α-crystallin
    • Maiti M., Kono M., Chakrabarti B. Heat-induced changes in the conformation of α- and β-crystallins: unique thermal stability of α-crystallin. FEBS Lett. 236:1988;109-114.
    • (1988) FEBS Lett. , vol.236 , pp. 109-114
    • Maiti, M.1    Kono, M.2    Chakrabarti, B.3
  • 23
    • 0025339471 scopus 로고
    • Folding of an all-beta protein: Independent domain folding in gamma II-crystallin from calf eye lens
    • Rudolph R., Siebendritt R., Nesslauer G., Sharma A.K., Jaenicke R. Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens. Proc. Nat. Acad. Sci. USA. 87:1990;4625-4629.
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 4625-4629
    • Rudolph, R.1    Siebendritt, R.2    Nesslauer, G.3    Sharma, A.K.4    Jaenicke, R.5
  • 24
    • 0034719101 scopus 로고    scopus 로고
    • Monomer-dimer equilibrium of normal and modified βA3-crystallins: Experimental determination and molecular modeling
    • Sergeev Y.V., Wingfield P.T., Hejtmancik J.F. Monomer-dimer equilibrium of normal and modified βA3-crystallins: experimental determination and molecular modeling. Biochemistry. 39:2000;15799-15806.
    • (2000) Biochemistry , vol.39 , pp. 15799-15806
    • Sergeev, Y.V.1    Wingfield, P.T.2    Hejtmancik, J.F.3
  • 25
    • 0022443288 scopus 로고
    • Interactions of lens proteins. Concentration dependence of β-crystallin aggregation
    • Siezen R.J., Anello R.D., Thomson J.A. Interactions of lens proteins. Concentration dependence of β-crystallin aggregation. Exp. Eye Res. 43:1986;293-303.
    • (1986) Exp. Eye Res. , vol.43 , pp. 293-303
    • Siezen, R.J.1    Anello, R.D.2    Thomson, J.A.3
  • 26
    • 0025371285 scopus 로고
    • Quaternary interactions in eye lens β-crystallins: Basic and acidic subunits of β-crystallins favor heterologous association
    • Slingsby C., Bateman O.A. Quaternary interactions in eye lens β-crystallins: basic and acidic subunits of β-crystallins favor heterologous association. Biochemistry. 29:1990;6592-6599.
    • (1990) Biochemistry , vol.29 , pp. 6592-6599
    • Slingsby, C.1    Bateman, O.A.2
  • 27
    • 85031068474 scopus 로고
    • PhD Thesis, University of Regensburg
    • Trinkl, S., 1995. PhD Thesis, University of Regensburg.
    • (1995)
    • Trinkl, S.1
  • 28
    • 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. 3:1994;1392-1400.
    • (1994) Protein Sci. , vol.3 , pp. 1392-1400
    • Trinkl, S.1    Glockshuber, R.2    Jaenicke, R.3
  • 29
    • 0023652252 scopus 로고
    • Differential absorption flattening optical effects are significant in the circular-dichroism spectra of large membrane fragments
    • Wallace B.A., Teeters C.L. Differential absorption flattening optical effects are significant in the circular-dichroism spectra of large membrane fragments. Biochemistry. 26:1987;65-70.
    • (1987) Biochemistry , vol.26 , pp. 65-70
    • Wallace, B.A.1    Teeters, C.L.2
  • 30
    • 0034734298 scopus 로고    scopus 로고
    • Gamma S-crystallin of bovine and human eye lens: Solution structure, stability and folding of the intact two-domain protein and its separate domains
    • Wenk M., Herbst R., Hoeger D., Kretschmar M., Lubsen N.H., Jaenicke R. Gamma S-crystallin of bovine and human eye lens: solution structure, stability and folding of the intact two-domain protein and its separate domains. Biophys. Chem. 86:2000;95-108.
    • (2000) Biophys. Chem. , vol.86 , pp. 95-108
    • Wenk, M.1    Herbst, R.2    Hoeger, D.3    Kretschmar, M.4    Lubsen, N.H.5    Jaenicke, R.6
  • 31
    • 0029803592 scopus 로고    scopus 로고
    • The elusive role of the N-terminal extension of βA3 and βA1-crystallin
    • Werten P.J.L., Carver J.A., Jaenicke R., de Jong W.W. The elusive role of the N-terminal extension of βA3 and βA1-crystallin. Protein Engng. 9:1996;1021-1028.
    • (1996) Protein Engng , vol.9 , pp. 1021-1028
    • Werten, P.J.L.1    Carver, J.A.2    Jaenicke, R.3    De Jong, W.W.4
  • 32
    • 0033551420 scopus 로고    scopus 로고
    • Formation of βA3/βB2-crystallin mixed complexes: Involvement of N- and C-terminal extensions
    • Werten P.L.J., Lindner R.A., Carver J.A., de Jong W.W. Formation of βA3/βB2-crystallin mixed complexes: involvement of N- and C-terminal extensions. BBA-Protein Struct. M1432:1999;286-292.
    • (1999) BBA-Protein Struct. , vol.M1432 , pp. 286-292
    • Werten, P.L.J.1    Lindner, R.A.2    Carver, J.A.3    De Jong, W.W.4
  • 33
    • 0033525632 scopus 로고    scopus 로고
    • Folding and self-assembly of the domains of βB2-crystallin from the rat eye lens
    • Wieligmann K., Mayr E.-M., Jaenicke R. Folding and self-assembly of the domains of βB2-crystallin from the rat eye lens. J. Mol. Biol. 286:1999;989-994.
    • (1999) J. Mol. Biol. , vol.286 , pp. 989-994
    • Wieligmann, K.1    Mayr, E.-M.2    Jaenicke, R.3
  • 34
    • 0028102759 scopus 로고
    • Contributions of tryptophan side-chains to the far-ultraviolet circular dichroism of proteins
    • Woody R.W. Contributions of tryptophan side-chains to the far-ultraviolet circular dichroism of proteins. Eur. Biophys. J. Biophys. Lett. 23:1994;253-262.
    • (1994) Eur. Biophys. J. Biophys. Lett. , vol.23 , pp. 253-262
    • Woody, R.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.