메뉴 건너뛰기




Volumn 16, Issue , 2010, Pages 2446-2456

The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: A light and X-ray scattering investigation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LACTALBUMIN; ALPHAB CRYSTALLIN; CHAPERONE; MALATE DEHYDROGENASE; OLIGOMER; UNCLASSIFIED DRUG;

EID: 78650782776     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (25)

References (64)
  • 2
    • 0037596678 scopus 로고    scopus 로고
    • Intracellular protein unfolding and aggregation: The role of small heat-shock chaperone proteins
    • Treweek TM, Morris AM, Carver JA. Intracellular protein unfolding and aggregation: The role of small heat-shock chaperone proteins. Aust J Chem 2003; 56:357-67.
    • (2003) Aust J Chem , vol.56 , pp. 357-367
    • Treweek, T.M.1    Morris, A.M.2    Carver, J.A.3
  • 3
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • [PMID: 12565801]
    • Horwitz J. Alpha-crystallin. Exp Eye Res 2003; 76:145-53. [PMID: 12565801]
    • (2003) Exp Eye Res , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 4
    • 0032986520 scopus 로고    scopus 로고
    • Alpha-crystallin as a molecular chaperone
    • [PMID: 10217480]
    • Derham BK, Harding JJ. Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res 1999; 18:463-509. [PMID: 10217480]
    • (1999) Prog Retin Eye Res , vol.18 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 5
    • 1642528843 scopus 로고    scopus 로고
    • Small heat-shock proteins and clusterin: Intra- and extracellular molecular chaperones with a common mechanism of action and function?
    • [PMID: 14769002]
    • Carver JA, Rekas A, Thorn DC, Wilson MR. Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function? IUBMB Life 2003; 55:661-8. [PMID: 14769002]
    • (2003) IUBMB Life , vol.55 , pp. 661-668
    • Carver, J.A.1    Rekas, A.2    Thorn, D.C.3    Wilson, M.R.4
  • 6
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • [PMID: 1438232]
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992; 89:10449-53. [PMID: 1438232]
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 7
    • 58149506229 scopus 로고    scopus 로고
    • Crystallin proteins and amyloid fibrils
    • [PMID: 18810322]
    • Ecroyd H, Carver JA. Crystallin proteins and amyloid fibrils. Cell Mol Life Sci 2009; 66:62-81. [PMID: 18810322]
    • (2009) Cell Mol Life Sci , vol.66 , pp. 62-81
    • Ecroyd, H.1    Carver, J.A.2
  • 10
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • [PMID: 6835373]
    • Delaye M, Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 1983; 302:415-7. [PMID: 6835373]
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 11
    • 15344341428 scopus 로고    scopus 로고
    • Alpha-crystallin: An ATP-independent complete molecular chaperone toward sorbitol dehydrogenase
    • [PMID: 15747064]
    • Marini I, Moschini R, Del Corso A, Mura U. Alpha-crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase. Cell Mol Life Sci 2005; 62:599-605. [PMID: 15747064]
    • (2005) Cell Mol Life Sci , vol.62 , pp. 599-605
    • Marini, I.1    Moschini, R.2    del Corso, A.3    Mura, U.4
  • 12
    • 0028293240 scopus 로고
    • Characterization of the alpha-gamma and alpha-beta complex: Evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone
    • [PMID: 8157104]
    • Boyle D, Takemoto L. Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone. Exp Eye Res 1994; 58:9-15. [PMID: 8157104]
    • (1994) Exp Eye Res , vol.58 , pp. 9-15
    • Boyle, D.1    Takemoto, L.2
  • 13
    • 0024578954 scopus 로고
    • Alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues
    • [PMID: 2912453]
    • Bhat SP, Nagineni CN. alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues. Biochem Biophys Res Commun 1989; 158:319-25. [PMID: 2912453]
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 15
    • 0027330972 scopus 로고
    • Alpha B crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease
    • [PMID: 8277336]
    • Shinohara H, Inaguma Y, Goto S, Inagaki T, Kato K. Alpha B crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease. J Neurol Sci 1993; 119:203-8. [PMID: 8277336]
    • (1993) J Neurol Sci , vol.119 , pp. 203-208
    • Shinohara, H.1    Inaguma, Y.2    Goto, S.3    Inagaki, T.4    Kato, K.5
  • 16
    • 0026541969 scopus 로고
    • Alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease
    • [PMID: 1311375]
    • Lowe J, McDermott H, Pike I, Spendlove I, Landon M, Mayer RJ. alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease. J Pathol 1992; 166:61-8. [PMID: 1311375]
    • (1992) J Pathol , vol.166 , pp. 61-68
    • Lowe, J.1    McDermott, H.2    Pike, I.3    Spendlove, I.4    Landon, M.5    Mayer, R.J.6
  • 17
    • 0031762949 scopus 로고    scopus 로고
    • Fatal attractions: Abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia
    • [PMID: 10203692]
    • Trojanowski JQ, Goedert M, Iwatsubo T, Lee VM. Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia. Cell Death Differ 1998; 5:832-7. [PMID: 10203692]
    • (1998) Cell Death Differ , vol.5 , pp. 832-837
    • Trojanowski, J.Q.1    Goedert, M.2    Iwatsubo, T.3    Lee, V.M.4
  • 18
    • 0029060142 scopus 로고
    • The small heat-shock protein alphaB-crystallin as candidate autoantigen in multiple sclerosis
    • vSAC, [PMID: 7596414]
    • van Noort JM. vSAC, Bajramovic JJ., el Ouagmiri M, Polman CH, Lassmann H, Ravid R, The small heat-shock protein alphaB-crystallin as candidate autoantigen in multiple sclerosis. Nature 1995; 375:798-801. [PMID: 7596414]
    • (1995) Nature , vol.375 , pp. 798-801
    • van Noort, J.M.1    Bajramovic, J.J.2    el Ouagmiri, M.3    Polman, C.H.4    Lassmann, H.5    Ravid, R.6
  • 20
    • 0025167955 scopus 로고
    • Cardiac alpha-crystallin. III. Involvement during heart ischemia
    • [PMID: 2280761]
    • Chiesi M, Longoni S, Limbruno U. Cardiac alpha-crystallin. III. Involvement during heart ischemia. Mol Cell Biochem 1990; 97:129-36. [PMID: 2280761]
    • (1990) Mol Cell Biochem , vol.97 , pp. 129-136
    • Chiesi, M.1    Longoni, S.2    Limbruno, U.3
  • 24
    • 0029025765 scopus 로고
    • Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase
    • [PMID: 7628468]
    • Ganea E, Harding JJ. Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase. Eur J Biochem 1995; 231:181-5. [PMID: 7628468]
    • (1995) Eur J Biochem , vol.231 , pp. 181-185
    • Ganea, E.1    Harding, J.J.2
  • 25
    • 0029932037 scopus 로고    scopus 로고
    • Prevention of the fructation-induced inactivation of glutathione reductase by bovine alphacrystallin acting as a molecular chaperone
    • [PMID: 8727959]
    • Blakytny R, Harding JJ. Prevention of the fructation-induced inactivation of glutathione reductase by bovine alphacrystallin acting as a molecular chaperone. Ophthalmic Res 1996; 28:19-22. [PMID: 8727959]
    • (1996) Ophthalmic Res , vol.28 , pp. 19-22
    • Blakytny, R.1    Harding, J.J.2
  • 26
    • 0029968456 scopus 로고    scopus 로고
    • Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, [alpha]-crystallin
    • [PMID: 8611656]
    • Heath MM, Rixon KC, Harding JJ. Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, [alpha]-crystallin. Biochim Biophys Acta 1996; 1315:176-84. [PMID: 8611656]
    • (1996) Biochim Biophys Acta , vol.1315 , pp. 176-184
    • Heath, M.M.1    Rixon, K.C.2    Harding, J.J.3
  • 27
    • 0033006872 scopus 로고    scopus 로고
    • Image restrained modeling of alphaB-crystallin
    • [PMID: 9986751]
    • Haley DA, Horwitz J, Stewart PL. Image restrained modeling of alphaB-crystallin. Exp Eye Res 1999; 68:133-6. [PMID: 9986751]
    • (1999) Exp Eye Res , vol.68 , pp. 133-136
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 28
    • 0026612249 scopus 로고
    • Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin
    • [PMID: 1397302]
    • Carver JA, Aquilina JA, Truscott RJ, Ralston GB. Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin. FEBS Lett 1992; 311:143-9. [PMID: 1397302]
    • (1992) FEBS Lett , vol.311 , pp. 143-149
    • Carver, J.A.1    Aquilina, J.A.2    Truscott, R.J.3    Ralston, G.B.4
  • 29
    • 0032983631 scopus 로고    scopus 로고
    • Probing the structure and interactions of crystallin proteins by NMR spectroscopy
    • [PMID: 10217479]
    • Carver JA. Probing the structure and interactions of crystallin proteins by NMR spectroscopy. Prog Retin Eye Res 1999; 18:431-62. [PMID: 10217479]
    • (1999) Prog Retin Eye Res , vol.18 , pp. 431-462
    • Carver, J.A.1
  • 30
    • 1242339668 scopus 로고    scopus 로고
    • Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle Xray diffraction
    • [PMID: 15037078]
    • Regini JW, Grossmann JG, Burgio MR, Malik NS, Koretz JF, Hodson SA, Elliott GF. Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle Xray diffraction. J Mol Biol 2004; 336:1185-94. [PMID: 15037078]
    • (2004) J Mol Biol , vol.336 , pp. 1185-1194
    • Regini, J.W.1    Grossmann, J.G.2    Burgio, M.R.3    Malik, N.S.4    Koretz, J.F.5    Hodson, S.A.6    Elliott, G.F.7
  • 31
    • 34347205682 scopus 로고    scopus 로고
    • X-ray- and neutron-scattering studies of alpha-crystallin and evidence that the target protein sits in the fenestrations of the alpha-crystallin shell
    • [PMID: 17525201]
    • Regini JW, Grossmann JG, Timmins P, Harding JJ, Quantock AJ, Hodson SA, Elliott GF. X-ray- and neutron-scattering studies of alpha-crystallin and evidence that the target protein sits in the fenestrations of the alpha-crystallin shell. Invest Ophthalmol Vis Sci 2007; 48:2695-700. [PMID: 17525201]
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 2695-2700
    • Regini, J.W.1    Grossmann, J.G.2    Timmins, P.3    Harding, J.J.4    Quantock, A.J.5    Hodson, S.A.6    Elliott, G.F.7
  • 32
    • 0034673329 scopus 로고    scopus 로고
    • Correlation between the chaperone-like activity and aggregate size of alphacrystallin with increasing temperature
    • [PMID: 10679221]
    • Burgio MR, Kim CJ, Dow CC, Koretz JF. Correlation between the chaperone-like activity and aggregate size of alphacrystallin with increasing temperature. Biochem Biophys Res Commun 2000; 268:426-32. [PMID: 10679221]
    • (2000) Biochem Biophys Res Commun , vol.268 , pp. 426-432
    • Burgio, M.R.1    Kim, C.J.2    Dow, C.C.3    Koretz, J.F.4
  • 34
    • 0030783517 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin
    • [PMID: 9346914]
    • Lindner RA, Kapur A, Carver JA. The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin. J Biol Chem 1997; 272:27722-9. [PMID: 9346914]
    • (1997) J Biol Chem , vol.272 , pp. 27722-27729
    • Lindner, R.A.1    Kapur, A.2    Carver, J.A.3
  • 35
    • 0035865589 scopus 로고    scopus 로고
    • The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alphalactalbumin
    • [PMID: 11171082]
    • Lindner RA, Treweek TM, Carver JA. The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alphalactalbumin. Biochem J 2001; 354:79-87. [PMID: 11171082]
    • (2001) Biochem J , vol.354 , pp. 79-87
    • Lindner, R.A.1    Treweek, T.M.2    Carver, J.A.3
  • 36
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: A structural and kinetic spectroscopic study
    • [PMID: 12054825]
    • Carver JA, Lindner RA, Lyon C, Canet D, Hernandez H, Dobson CM, Redfield C. The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study. J Mol Biol 2002; 318:815-27. [PMID: 12054825]
    • (2002) J Mol Biol , 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
  • 37
    • 0028113441 scopus 로고
    • Malate-dehydrogenase - a model for structure, evolution and catalysis
    • [PMID: 7849603]
    • Goward CR, Nicholls DJ. Malate-dehydrogenase - a model for structure, evolution and catalysis. Protein Sci 1994; 3:1883-8. [PMID: 7849603]
    • (1994) Protein Sci , vol.3 , pp. 1883-1888
    • Goward, C.R.1    Nicholls, D.J.2
  • 38
    • 11844274723 scopus 로고    scopus 로고
    • The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function?
    • [PMID: 15642318]
    • Horwitz J, Huang QL, Ding LL. The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function? Exp Eye Res 2004; 79:817-21. [PMID: 15642318]
    • (2004) Exp Eye Res , vol.79 , pp. 817-821
    • Horwitz, J.1    Huang, Q.L.2    Ding, L.L.3
  • 39
    • 0031918807 scopus 로고    scopus 로고
    • Lens alpha-crystallin: Chaperone-like properties
    • [PMID: 9534176]
    • Horwitz J, Huang QL, Ding L, Bova MP. Lens alpha-crystallin: chaperone-like properties. Methods Enzymol 1998; 290:365-83. [PMID: 9534176]
    • (1998) Methods Enzymol , vol.290 , pp. 365-383
    • Horwitz, J.1    Huang, Q.L.2    Ding, L.3    Bova, M.P.4
  • 42
    • 0002427553 scopus 로고
    • Static and dynamic light-scattering from branched polymers and bio-polymers
    • Burchard W. Static and dynamic light-scattering from branched polymers and bio-polymers. Adv Polym Sci 1983; 48:1-124.
    • (1983) Adv Polym Sci , vol.48 , pp. 1-124
    • Burchard, W.1
  • 43
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • [PMID: 10339554]
    • Bova MP, Yaron O, Huang Q, Ding L, Haley DA, Stewart PL, Horwitz J. Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc Natl Acad Sci USA 1999; 96:6137-42. [PMID: 10339554]
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7
  • 44
    • 0033517042 scopus 로고    scopus 로고
    • The mode of chaperoning of dithiothreitol-denatured alpha-lactalbumin by alpha-crystallin
    • [PMID: 10425180]
    • Bettelheim FA, Ansari R, Cheng QF, Zigler JS Jr. The mode of chaperoning of dithiothreitol-denatured alpha-lactalbumin by alpha-crystallin. Biochem Biophys Res Commun 1999; 261:292-7. [PMID: 10425180]
    • (1999) Biochem Biophys Res Commun , vol.261 , pp. 292-297
    • Bettelheim, F.A.1    Ansari, R.2    Cheng, Q.F.3    Zigler Jr., J.S.4
  • 46
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heatshock protein
    • [PMID: 9707123]
    • Kim KK, Kim R, Kim SH. Crystal structure of a small heatshock protein. Nature 1998; 394:595-9. [PMID: 9707123]
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 47
    • 25144461582 scopus 로고    scopus 로고
    • Wrapping the alpha-crystallin domain fold in a chaperone assembly
    • [PMID: 16165157]
    • Stamler R, Kappe G, Boelens W, Slingsby C. Wrapping the alpha-crystallin domain fold in a chaperone assembly. J Mol Biol 2005; 353:68-79. [PMID: 16165157]
    • (2005) J Mol Biol , vol.353 , pp. 68-79
    • Stamler, R.1    Kappe, G.2    Boelens, W.3    Slingsby, C.4
  • 49
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure
    • [PMID: 9514758]
    • Haley DA, Horwitz J, Stewart PL. The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure. J Mol Biol 1998; 277:27-35. [PMID: 9514758]
    • (1998) J Mol Biol , vol.277 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 51
    • 0027933712 scopus 로고
    • A possible chaperone-like quaternary structure for alpha-crystallin
    • [PMID: 7835412]
    • Carver JA, Aquilina JA, Truscott RJ. A possible chaperone-like quaternary structure for alpha-crystallin. Exp Eye Res 1994; 59:231-4. [PMID: 7835412]
    • (1994) Exp Eye Res , vol.59 , pp. 231-234
    • Carver, J.A.1    Aquilina, J.A.2    Truscott, R.J.3
  • 52
    • 0037129795 scopus 로고    scopus 로고
    • Kinetics of chaperoning of dithiothreitoldenatured alpha-lactalbumin by alpha-crystallin
    • [PMID: 12063118]
    • Bettelheim FA. Kinetics of chaperoning of dithiothreitoldenatured alpha-lactalbumin by alpha-crystallin. Int J Biol Macromol 2002; 30:161-9. [PMID: 12063118]
    • (2002) Int J Biol Macromol , vol.30 , pp. 161-169
    • Bettelheim, F.A.1
  • 53
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • [PMID: 10764595]
    • Haley DA, Bova MP, Huang QL, McHaourab HS, Stewart PL. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. J Mol Biol 2000; 298:261-72. [PMID: 10764595]
    • (2000) J Mol Biol , vol.298 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.L.3    McHaourab, H.S.4    Stewart, P.L.5
  • 54
    • 33646007016 scopus 로고    scopus 로고
    • sHSPs under temperature and pressure: The opposite behaviour of lens alpha-crystallins and yeast HSP26
    • [PMID: 16476575]
    • Skouri-Panet F, Quevillon-Cheruel S, Michiel M, Tardieu A, Finet S. sHSPs under temperature and pressure: the opposite behaviour of lens alpha-crystallins and yeast HSP26. Biochim Biophys Acta 2006; 1764:372-83. [PMID: 16476575]
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 372-383
    • Skouri-Panet, F.1    Quevillon-Cheruel, S.2    Michiel, M.3    Tardieu, A.4    Finet, S.5
  • 56
    • 0032078812 scopus 로고    scopus 로고
    • Alpha-Crystallin polymers and polymerization: The view from down under
    • [PMID: 9650080]
    • Augusteyn RC. alpha-Crystallin polymers and polymerization: the view from down under. Int J Biol Macromol 1998; 22:253-62. [PMID: 9650080]
    • (1998) Int J Biol Macromol , vol.22 , pp. 253-262
    • Augusteyn, R.C.1
  • 57
    • 0023439448 scopus 로고
    • Structure of Casein Micelles. 2. Alpha-S1-Casein
    • Thurn A, Burchard W, Niki R. Structure of Casein Micelles. 2. Alpha-S1-Casein. Colloid Polym Sci 1987; 265:897-902.
    • (1987) Colloid Polym Sci , vol.265 , pp. 897-902
    • Thurn, A.1    Burchard, W.2    Niki, R.3
  • 58
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • [PMID: 16205709]
    • Haslbeck M, Franzmann T, Weinfurtner D, Buchner J. Some like it hot: the structure and function of small heat-shock proteins. Nat Struct Mol Biol 2005; 12:842-6. [PMID: 16205709]
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 59
    • 38949124389 scopus 로고    scopus 로고
    • The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation
    • [PMID: 18218039]
    • Ecroyd H, Carver JA. The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation. FEBS J 2008; 275:935-47. [PMID: 18218039]
    • (2008) FEBS J , vol.275 , pp. 935-947
    • Ecroyd, H.1    Carver, J.A.2
  • 60
    • 78049506985 scopus 로고    scopus 로고
    • A quantitative NMR spectroscopic examination of the flexibility of the Cterminal extensions of the molecular chaperones, αA- and αB-crystallin
    • [PMID: 20732317]
    • Treweek TM, Rekas A, Walker MJ, Carver JA. A quantitative NMR spectroscopic examination of the flexibility of the Cterminal extensions of the molecular chaperones, αA- and αB-crystallin. Exp Eye Res 2010; 91:691-9. [PMID: 20732317]
    • (2010) Exp Eye Res , vol.91 , pp. 691-699
    • Treweek, T.M.1    Rekas, A.2    Walker, M.J.3    Carver, J.A.4
  • 63
    • 0032533361 scopus 로고    scopus 로고
    • Structural alterations of alpha-crystallin during its chaperone action
    • [PMID: 9851707]
    • Lindner RA, Kapur A, Mariani M, Titmuss SJ, Carver JA. Structural alterations of alpha-crystallin during its chaperone action. Eur J Biochem 1998; 258:170-83. [PMID: 9851707]
    • (1998) Eur J Biochem , vol.258 , pp. 170-183
    • Lindner, R.A.1    Kapur, A.2    Mariani, M.3    Titmuss, S.J.4    Carver, J.A.5
  • 64
    • 36749037242 scopus 로고    scopus 로고
    • Monitoring the prevention of amyloid fibril formation by alpha-crystallin
    • [PMID: 18005258]
    • Rekas A, Jankova L, Thorn DC, Cappai R, Carver JA. Monitoring the prevention of amyloid fibril formation by alpha-crystallin. FEBS J 2007; 274:6290-304. [PMID: 18005258]
    • (2007) FEBS J , vol.274 , pp. 6290-6304
    • Rekas, A.1    Jankova, L.2    Thorn, D.C.3    Cappai, R.4    Carver, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.