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Volumn 581, Issue 10, 2007, Pages 1939-1943

Specificity of αA-crystallin binding to destabilized mutants of βB1-crystallin

Author keywords

Crystallin; Crystallin; Cataract; Chaperone; Small heat shock protein

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; BETAB1 CRYSTALLIN; DIMER; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34247580177     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.04.005     Document Type: Article
Times cited : (21)

References (22)
  • 3
    • 0030893023 scopus 로고    scopus 로고
    • Size of human lens beta-crystallin aggregates are distinguished by N-terminal truncation of betaB1
    • Ajaz M.S., Ma Z., Smith D.L., and Smith J.B. Size of human lens beta-crystallin aggregates are distinguished by N-terminal truncation of betaB1. Journal of Biological Chemistry 272 (1997) 11250-11255
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 11250-11255
    • Ajaz, M.S.1    Ma, Z.2    Smith, D.L.3    Smith, J.B.4
  • 4
    • 0032128377 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry
    • Lampi K.J., et al. Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry. Experimental Eye Research 67 (1998) 31-43
    • (1998) Experimental Eye Research , vol.67 , pp. 31-43
    • Lampi, K.J.1
  • 8
    • 0242582458 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-crystallin
    • Sathish H.A., Stein R.A., Yang G., and Mchaourab H.S. Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-crystallin. Journal of Biological Chemistry 278 (2003) 44214-44221
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 44214-44221
    • Sathish, H.A.1    Stein, R.A.2    Yang, G.3    Mchaourab, H.S.4
  • 9
    • 18044388716 scopus 로고    scopus 로고
    • Age-related nuclear cataract-oxidation is the key
    • Truscott R.J.W. Age-related nuclear cataract-oxidation is the key. Experimental Eye Research 80 (2005) 709-725
    • (2005) Experimental Eye Research , vol.80 , pp. 709-725
    • Truscott, R.J.W.1
  • 10
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study
    • Carver J.A., Lindner R.A., Lyon C., Canet D., Hernandez H., Dobson C.M., and Redfield C. The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study. Journal of Molecular Biology 318 (2002) 815-827
    • (2002) Journal of Molecular Biology , vol.318 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3    Canet, D.4    Hernandez, H.5    Dobson, C.M.6    Redfield, C.7
  • 11
    • 0037174851 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins.Two-mode binding of the excited states of T4 lysozyme mutants by aA-crystallin
    • Mchaourab H.S., Dodson E.K., and Koteiche H.A. Mechanism of chaperone function in small heat-shock proteins.Two-mode binding of the excited states of T4 lysozyme mutants by aA-crystallin. Journal of Biological Chemistry 277 (2002) 40557-40566
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 40557-40566
    • Mchaourab, H.S.1    Dodson, E.K.2    Koteiche, H.A.3
  • 12
    • 0027267599 scopus 로고
    • Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation
    • Rao P.V., Horwitz J., and Zigler Jr. J.S. Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation. Biochemical & Biophysical Research Communications 190 (1993) 786-793
    • (1993) Biochemical & Biophysical Research Communications , vol.190 , pp. 786-793
    • Rao, P.V.1    Horwitz, J.2    Zigler Jr., J.S.3
  • 14
    • 0033764457 scopus 로고    scopus 로고
    • In vitro filament-like formation upon interaction between lens alpha-crystallin and betaL-crystallin promoted by stress
    • Weinreb O., van Rijk A.F., Dovrat A., and Bloemendal H. In vitro filament-like formation upon interaction between lens alpha-crystallin and betaL-crystallin promoted by stress. Investigative Ophthalmology & Visual Science 41 (2000) 3893-3897
    • (2000) Investigative Ophthalmology & Visual Science , vol.41 , pp. 3893-3897
    • Weinreb, O.1    van Rijk, A.F.2    Dovrat, A.3    Bloemendal, H.4
  • 15
    • 1942437441 scopus 로고    scopus 로고
    • Binding of destabilized betaB2-crystallin mutants to alpha-crystallin: the role of a folding intermediate
    • Sathish H.A., Koteiche H.A., and McHaourab H.S. Binding of destabilized betaB2-crystallin mutants to alpha-crystallin: the role of a folding intermediate. Journal of Biological Chemistry 279 (2004) 16425-16432
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 16425-16432
    • Sathish, H.A.1    Koteiche, H.A.2    McHaourab, H.S.3
  • 16
    • 21644476499 scopus 로고    scopus 로고
    • Crystallin {gamma}B-I4F mutant protein binds to {alpha}-crystallin and affects lens transparency
    • Liu H., et al. Crystallin {gamma}B-I4F mutant protein binds to {alpha}-crystallin and affects lens transparency. Journal of Biological Chemistry 280 (2005) 25071-25078
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 25071-25078
    • Liu, H.1
  • 18
    • 34247644864 scopus 로고    scopus 로고
    • Koteiche, H.A., Kumar, M.S. and Machaourab, H.S. (2007) Analysis of βB1-crystallin unfolding equilibrium by spin and fluorescence labeling. Evidence of a dimeric intermediate. FEBS Letters, this issue, doi:10.1016/j.febslet.2007.04.004.
  • 19
    • 0037176909 scopus 로고    scopus 로고
    • Mapping proximity within proteins using fluorescence spectroscopy. A study of T4 lysozyme showing that tryptophan residues quench bimane fluorescence
    • Mansoor S.E., McHaourab H.S., and Farrens D.L. Mapping proximity within proteins using fluorescence spectroscopy. A study of T4 lysozyme showing that tryptophan residues quench bimane fluorescence. Biochemistry 41 (2002) 2475-2484
    • (2002) Biochemistry , vol.41 , pp. 2475-2484
    • Mansoor, S.E.1    McHaourab, H.S.2    Farrens, D.L.3
  • 20
    • 33744903422 scopus 로고    scopus 로고
    • Mechanism of a hereditary cataract phenotype: mutations in αA-crystallin activate substrate binding
    • Koteiche H.A., and McHaourab H.S. Mechanism of a hereditary cataract phenotype: mutations in αA-crystallin activate substrate binding. Journal of Biological Chemistry 281 (2006) 14273-14279
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 14273-14279
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 21
    • 0030711517 scopus 로고    scopus 로고
    • Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate
    • Grimsley J.K., Scholtz J.M., Pace C.N., and Wild J.R. Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate. Biochemistry 36 (1997) 14366-14374
    • (1997) Biochemistry , vol.36 , pp. 14366-14374
    • Grimsley, J.K.1    Scholtz, J.M.2    Pace, C.N.3    Wild, J.R.4
  • 22
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton A.P. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. Journal of Biological Chemistry 276 (2001) 10577-10580
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 10577-10580
    • Minton, A.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.