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Volumn 11, Issue 2, 2006, Pages 187-197

The function of the β3 interactive domain in the small heat shock protein and molecular chaperone, human αB crystallin

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; ALPHAB CRYSTALLIN; ASPARAGINE; CAENORHABDITIS ELEGANS PROTEIN; CHAPERONE; CHYMOTRYPSIN; CITRATE SYNTHASE; HEAT SHOCK PROTEIN; HISTIDINE; LYSINE; PROTEIN CE1; PROTEIN H83F; PROTEIN K82Q; PROTEIN N78G; PROTEIN S76E; SERINE; UNCLASSIFIED DRUG; ALPHA CRYSTALLIN; SMALL HEAT SHOCK PROTEIN;

EID: 33745467101     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1379/CSC-186.1     Document Type: Conference Paper
Times cited : (23)

References (35)
  • 1
    • 0026341897 scopus 로고
    • Alpha B-crystallin in skeletal muscle: Purification and localization
    • Atomi Y, Yamada S, Strohman R, Nonomura Y. 1991. Alpha B-crystallin in skeletal muscle: purification and localization. J Biochem (Tokyo) 110: 812-822.
    • (1991) J Biochem (Tokyo) , vol.110 , pp. 812-822
    • Atomi, Y.1    Yamada, S.2    Strohman, R.3    Nonomura, Y.4
  • 2
    • 0026325675 scopus 로고
    • Alpha B-crystallin exists as an independent protein in the heart and in the lens
    • Bhat SP, Horwitz J, Srinivasan A, Ding L. 1991. Alpha B-crystallin exists as an independent protein in the heart and in the lens. Eur J Biochem 202: 775-781.
    • (1991) Eur J Biochem , vol.202 , pp. 775-781
    • Bhat, S.P.1    Horwitz, J.2    Srinivasan, A.3    Ding, L.4
  • 3
    • 0033968166 scopus 로고    scopus 로고
    • Small heat-shock proteins and their potential role in human disease
    • Clark JI, Muchowski PJ. 2000. Small heat-shock proteins and their potential role in human disease. Curr Opin Struct Biol 10: 52-59.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 52-59
    • Clark, J.I.1    Muchowski, P.J.2
  • 4
    • 0021776417 scopus 로고
    • The heat shock response
    • Craig EA. 1985. The heat shock response. CRC Crit Rev Biochem 18: 239-280.
    • (1985) CRC Crit Rev Biochem , vol.18 , pp. 239-280
    • Craig, E.A.1
  • 6
    • 0024580908 scopus 로고
    • Expression of the murine alpha B-crystallin gene is not restricted to the lens
    • Dubin RA, Wawrousek EF, Piatigorsky J. 1989. Expression of the murine alpha B-crystallin gene is not restricted to the lens. Mol Cell Biol 9: 1083-1091.
    • (1989) Mol Cell Biol , vol.9 , pp. 1083-1091
    • Dubin, R.A.1    Wawrousek, E.F.2    Piatigorsky, J.3
  • 7
    • 14144255401 scopus 로고    scopus 로고
    • Insights into the domains required for dimerization and assembly of human alphaB crystallin
    • Ghosh JG, Clark JI. 2005. Insights into the domains required for dimerization and assembly of human alphaB crystallin. Protein Sci 14: 684-695.
    • (2005) Protein Sci , vol.14 , pp. 684-695
    • Ghosh, J.G.1    Clark, J.I.2
  • 8
    • 27744485379 scopus 로고    scopus 로고
    • Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin
    • Ghosh JG, Estrada MR, Clark JI. 2005. Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin. Biochemistry 44: 14854-14869.
    • (2005) Biochemistry , vol.44 , pp. 14854-14869
    • Ghosh, J.G.1    Estrada, M.R.2    Clark, J.I.3
  • 9
    • 0242352386 scopus 로고    scopus 로고
    • Three-dimensional models corresponding to the C-terminal domain of human alphaA- and alphaB-crystallins based on the crystal structure of the small heat-shock protein HSP16.9 from wheat
    • Guruprasad K, Kumari K. 2003. Three-dimensional models corresponding to the C-terminal domain of human alphaA- and alphaB-crystallins based on the crystal structure of the small heat-shock protein HSP16.9 from wheat. Int J Biol Macromol 33: 107-112.
    • (2003) Int J Biol Macromol , vol.33 , pp. 107-112
    • Guruprasad, K.1    Kumari, K.2
  • 10
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. 1992. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci U S A 89: 10449-10453.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 12
    • 0025101570 scopus 로고
    • Cellular distribution of alpha B-crystallin in non-lenticular tissues
    • Iwaki T, Kume-Iwaki A, Goldman JE. 1990. Cellular distribution of alpha B-crystallin in non-lenticular tissues. J Histochem Cytochem 38: 31-39.
    • (1990) J Histochem Cytochem , vol.38 , pp. 31-39
    • Iwaki, T.1    Kume-Iwaki, A.2    Goldman, J.E.3
  • 13
    • 0024521440 scopus 로고
    • Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki T, Kume-Iwaki A, Liem RK, Goldman JE. 1989. Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57: 71-78.
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.3    Goldman, J.E.4
  • 15
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heatshock protein
    • Kim KK, Kim R, Kim SH. 1998. Crystal structure of a small heatshock protein. Nature 394: 595-599.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 16
    • 0035195006 scopus 로고    scopus 로고
    • The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human alphaB-crystallin
    • Kokke BP, Boelens WC, de Jong WW. 2001. The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human alphaB-crystallin. Cell Stress Chaperones 6: 360-367.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 360-367
    • Kokke, B.P.1    Boelens, W.C.2    De Jong, W.W.3
  • 17
    • 0032555364 scopus 로고    scopus 로고
    • Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity
    • Kokke BP, Leroux MR, Candido EP, Boelens WC, de Jong WW. 1998. Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity. FEBS Lett 433: 228-232.
    • (1998) FEBS Lett , vol.433 , pp. 228-232
    • Kokke, B.P.1    Leroux, M.R.2    Candido, E.P.3    Boelens, W.C.4    De Jong, W.W.5
  • 18
    • 0033607618 scopus 로고    scopus 로고
    • Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling
    • Koteiche HA, McHaourab HS. 1999. Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling. J Mol Biol 294: 561-577.
    • (1999) J Mol Biol , vol.294 , pp. 561-577
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 19
    • 0030614502 scopus 로고    scopus 로고
    • Human alphaBcrystallin. Small heat shock protein and molecular chaperone
    • Muchowski PJ, Bassu JA, Lubsen NH, Clark JI. 1997. Human alphaBcrystallin. Small heat shock protein and molecular chaperone. J Biol Chem 272: 2578-2582.
    • (1997) J Biol Chem , vol.272 , pp. 2578-2582
    • Muchowski, P.J.1    Bassu, J.A.2    Lubsen, N.H.3    Clark, J.I.4
  • 20
    • 0033570053 scopus 로고    scopus 로고
    • ATP and the core "alpha-Crystallin" domain of the small heat-shock protein alphaB-crystallin
    • Muchowski PJ, Hays LG, Yates JR, 3rd, Clark JI. 1999a. ATP and the core "alpha-Crystallin" domain of the small heat-shock protein alphaB-crystallin. J Biol Chem 274: 30190-30195.
    • (1999) J Biol Chem , vol.274 , pp. 30190-30195
    • Muchowski, P.J.1    Hays, L.G.2    Yates III, J.R.3    Clark, J.I.4
  • 21
    • 0032587169 scopus 로고    scopus 로고
    • AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress
    • Muchowski PJ, Valdez MM, Clark JI. 1999b. AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress. Invest Ophthalmol Vis Sci 40: 951-958.
    • (1999) Invest Ophthalmol Vis Sci , vol.40 , pp. 951-958
    • Muchowski, P.J.1    Valdez, M.M.2    Clark, J.I.3
  • 22
    • 0033522885 scopus 로고    scopus 로고
    • Site-directed mutations within the core "alpha-crystallin" domain of the small heat-shock protein, human alphaB-crystallin, decrease molecular chaperone functions
    • Muchowski PJ, Wu GJ, Liang JJ, Adman ET, Clark JI. 1999c. Site-directed mutations within the core "alpha-crystallin" domain of the small heat-shock protein, human alphaB-crystallin, decrease molecular chaperone functions. J Mol Biol 289: 397-411.
    • (1999) J Mol Biol , vol.289 , pp. 397-411
    • Muchowski, P.J.1    Wu, G.J.2    Liang, J.J.3    Adman, E.T.4    Clark, J.I.5
  • 23
    • 0024359521 scopus 로고
    • Alpha B-crystallin is expressed in kidney epithelial cell lines and not in fibroblasts
    • Nagineni CN, Bhat SP. 1989. Alpha B-crystallin is expressed in kidney epithelial cell lines and not in fibroblasts. FEBS Lett 249: 89-94.
    • (1989) FEBS Lett , vol.249 , pp. 89-94
    • Nagineni, C.N.1    Bhat, S.P.2
  • 24
    • 0036195722 scopus 로고    scopus 로고
    • Alpha-crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • Narberhaus F. 2002. Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol Mol Biol Rev 66: 64-93.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 25
    • 0024349323 scopus 로고
    • Lens crystallins and their genes: Diversity and tissue-specific expression
    • Piatigorsky J. 1989. Lens crystallins and their genes: diversity and tissue-specific expression. FASEB J 3: 1933-1940.
    • (1989) FASEB J , vol.3 , pp. 1933-1940
    • Piatigorsky, J.1
  • 26
    • 0025340370 scopus 로고
    • Molecular biology: Recent studies on enzyme/ crystallins and alpha-crystallin gene expression
    • Piatigorsky J. 1990. Molecular biology: recent studies on enzyme/ crystallins and alpha-crystallin gene expression. Exp Eye Res 50: 725-728.
    • (1990) Exp Eye Res , vol.50 , pp. 725-728
    • Piatigorsky, J.1
  • 27
    • 0029956553 scopus 로고    scopus 로고
    • Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin
    • Plater ML, Goode D, Crabbe MJ. 1996. Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin. J Biol Chem 271: 28558-28566.
    • (1996) J Biol Chem , vol.271 , pp. 28558-28566
    • Plater, M.L.1    Goode, D.2    Crabbe, M.J.3
  • 28
    • 0035947181 scopus 로고    scopus 로고
    • Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation
    • Rajaraman K, Raman B, Ramakrishna T, Rao CM. 2001. Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation. FEBS Lett 497: 118-123.
    • (2001) FEBS Lett , vol.497 , pp. 118-123
    • Rajaraman, K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 29
    • 0025894777 scopus 로고
    • Study of crystallin expression in human lens epithelial cells during differentiation in culture and in non-lenticular tissues
    • Reddy VN, Katsura H, Arita T, Lin LR, Eguchi G, Agata K, Sawada K. 1991. Study of crystallin expression in human lens epithelial cells during differentiation in culture and in non-lenticular tissues. Exp Eye Res 53: 367-374.
    • (1991) Exp Eye Res , vol.53 , pp. 367-374
    • Reddy, V.N.1    Katsura, H.2    Arita, T.3    Lin, L.R.4    Eguchi, G.5    Agata, K.6    Sawada, K.7
  • 30
    • 0034635397 scopus 로고    scopus 로고
    • Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin
    • Sharma KK, Kumar RS, Kumar GS, Quinn PT. 2000. Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin. J Biol Chem 275: 3767-3771.
    • (2000) J Biol Chem , vol.275 , pp. 3767-3771
    • Sharma, K.K.1    Kumar, R.S.2    Kumar, G.S.3    Quinn, P.T.4
  • 31
    • 52549105587 scopus 로고    scopus 로고
    • Interaction of alpha-lactalbumin with mini-alphaA-crystallin
    • Sreelakshmi Y, Sharma KK. 2001. Interaction of alpha-lactalbumin with mini-alphaA-crystallin. J Protein Chem 20: 123-130.
    • (2001) J Protein Chem , vol.20 , pp. 123-130
    • Sreelakshmi, Y.1    Sharma, K.K.2
  • 32
    • 0035789880 scopus 로고    scopus 로고
    • Studies on the alpha-crystallin target protein binding sites: Sequential binding with two target proteins
    • Srinivas V, Datta SA, Ramakrishna T, Rao CM. 2001. Studies on the alpha-crystallin target protein binding sites: sequential binding with two target proteins. Mol Vis 7: 114-119.
    • (2001) Mol Vis , vol.7 , pp. 114-119
    • Srinivas, V.1    Datta, S.A.2    Ramakrishna, T.3    Rao, C.M.4
  • 33
    • 0036784934 scopus 로고    scopus 로고
    • Enhanced Cterminal truncation of alphaA- and alphaB-crystallins in diabetic lenses
    • Thampi P, Hassan A, Smith JB, Abraham EC. 2002. Enhanced Cterminal truncation of alphaA- and alphaB-crystallins in diabetic lenses. Invest Ophthalmol Vis Sci 43: 3265-3272.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 3265-3272
    • Thampi, P.1    Hassan, A.2    Smith, J.B.3    Abraham, E.C.4
  • 35
    • 0242637569 scopus 로고    scopus 로고
    • AlphaB-crystallin modulates protein aggregation of abnormal desmin
    • Wang X, Klevitsky R, Huang W, Glasford J, Li F, Robbins J. 2003. AlphaB-crystallin modulates protein aggregation of abnormal desmin. Circ Res 93: 998-1005.
    • (2003) Circ Res , vol.93 , pp. 998-1005
    • Wang, X.1    Klevitsky, R.2    Huang, W.3    Glasford, J.4    Li, F.5    Robbins, J.6


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