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1
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0032561319
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Negative charges in the C-terminal domain stabilize the αb-crystallin complex
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In a yeast two-hybrid system, the conserved C-terminal core α-crystallin domain of small heat-shock proteins (sHsps) was essential for interactions among subunits of sHsps. The N terminus was found to participate in the formation of larger multimeric complexes.
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Boelens W.C., Croes Y., de Ruwe M., de Reu L., de Jong W.W. Negative charges in the C-terminal domain stabilize the αB-crystallin complex. J Biol Chem. 273:1998;28085-28090. In a yeast two-hybrid system, the conserved C-terminal core α-crystallin domain of small heat-shock proteins (sHsps) was essential for interactions among subunits of sHsps. The N terminus was found to participate in the formation of larger multimeric complexes.
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J Biol Chem
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Boelens, W.C.1
Croes, Y.2
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Probing the structure and interactions of crystallin proteins by NMR spectroscopy
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Carver J.A. Probing the structure and interactions of crystallin proteins by NMR spectroscopy. Prog Retin Eye Res. 18:1999;431-462.
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Prog Retin Eye Res
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Carver, J.A.1
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0032986520
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Alpha-crystallin as a molecular chaperone
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A review of the current status of structural and functional studies of αB-crystallin in the lens.
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Derham B.K., Harding J.J. Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res. 18:1999;463-509. A review of the current status of structural and functional studies of αB-crystallin in the lens.
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Prog Retin Eye Res
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Derham, B.K.1
Harding, J.J.2
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4
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1342292267
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Crystal structure of a small heat-shock protein
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This report provided the first structure of the core α-crystallin domain, solved at 2.9 Å resolution.
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Kim K.K., Kim R., Kim S.H. Crystal structure of a small heat-shock protein. Nature. 394:1998;595-599. This report provided the first structure of the core α-crystallin domain, solved at 2.9 Å resolution.
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Nature
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, pp. 595-599
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Kim, K.K.1
Kim, R.2
Kim, S.H.3
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5
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0032549677
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The small heat-shock protein, αb crystallin, has a variable quaternary structure
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The structure of the αB-crystallin complex was determined using cryoelectron microscopy. The results indicate that the multimer is a metastable, dynamic complex.
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Haley D.A., Horwitz J., Stewart P.L. The small heat-shock protein, αB crystallin, has a variable quaternary structure. J Mol Biol. 277:1998;27-35. The structure of the αB-crystallin complex was determined using cryoelectron microscopy. The results indicate that the multimer is a metastable, dynamic complex.
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(1998)
J Mol Biol
, vol.277
, pp. 27-35
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Haley, D.A.1
Horwitz, J.2
Stewart, P.L.3
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6
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0033525723
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Site-directed spin labeling study of subunit interactions in the α-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in αa-crystallin, HSP 27, and HSP 16.3
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Electron paramagnetic resonance studies of site-mutated small heat-shock proteins identified a twofold symmetric interface between subunits that involves two β strands in the core α-crystallin domain interacting in antiparallel fashion. The results were consistent with a role for these sequences in dimer formation.
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Berengian A.R., Parfenova M., McHaourab H.S. Site-directed spin labeling study of subunit interactions in the α-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in αA-crystallin, HSP 27, and HSP 16.3. J Biol Chem. 274:1999;6305-6314. Electron paramagnetic resonance studies of site-mutated small heat-shock proteins identified a twofold symmetric interface between subunits that involves two β strands in the core α-crystallin domain interacting in antiparallel fashion. The results were consistent with a role for these sequences in dimer formation.
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(1999)
J Biol Chem
, vol.274
, pp. 6305-6314
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Berengian, A.R.1
Parfenova, M.2
McHaourab, H.S.3
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7
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0033573984
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Identification of a site of Hsp27 binding with Hsp27 and αb-crystallin as indicated by the yeast two-hybrid system
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Liu C., Welsh M.J. Identification of a site of Hsp27 binding with Hsp27 and αB-crystallin as indicated by the yeast two-hybrid system. Biochem Biophys Res Commun. 255:1999;256-261.
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(1999)
Biochem Biophys Res Commun
, vol.255
, pp. 256-261
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Liu, C.1
Welsh, M.J.2
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8
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0033516660
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Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation
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Large complexes of Hsp27 were found to be necessary for chaperone action and phosphorylation decreased its activity by dissociating small heat-shock protein complexes.
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Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem. 274:1999;18947-18956. Large complexes of Hsp27 were found to be necessary for chaperone action and phosphorylation decreased its activity by dissociating small heat-shock protein complexes.
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(1999)
J Biol Chem
, vol.274
, pp. 18947-18956
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Rogalla, T.1
Ehrnsperger, M.2
Preville, X.3
Kotlyarov, A.4
Lutsch, G.5
Ducasse, C.6
Paul, C.7
Wieske, M.8
Arrigo, A.P.9
Buchner, J.10
Gaestel, M.11
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9
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0033515597
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HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus
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A yeast two-hybrid system was used to determine that both the core α-crystallin domain and the phosphorylation-sensitive N-terminal domain are involved in complex assembly of Hsp27. Stable dimers may be formed through the core α-crystallin domain and multimerization is mediated by the phosphorylation-sensitive N-terminal domain.
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Lambert H., Charette S.J., Bernier A.F., Guimond A., Landry J. HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus. J Biol Chem. 274:1999;9378-9385. A yeast two-hybrid system was used to determine that both the core α-crystallin domain and the phosphorylation-sensitive N-terminal domain are involved in complex assembly of Hsp27. Stable dimers may be formed through the core α-crystallin domain and multimerization is mediated by the phosphorylation-sensitive N-terminal domain.
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(1999)
J Biol Chem
, vol.274
, pp. 9378-9385
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Lambert, H.1
Charette, S.J.2
Bernier, A.F.3
Guimond, A.4
Landry, J.5
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10
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0032617026
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Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27)
-
Microfilament reorganization and assembly were mediated in human vascular endothelial cells by phosphorylation of Hsp27, resulting from activation of the SAPK2 pathway.
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Landry J., Huot J. Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27). Biochem Soc Symp. 64:1999;79-89. Microfilament reorganization and assembly were mediated in human vascular endothelial cells by phosphorylation of Hsp27, resulting from activation of the SAPK2 pathway.
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(1999)
Biochem Soc Symp
, vol.64
, pp. 79-89
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Landry, J.1
Huot, J.2
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11
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0030724879
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αb-crystallin interacts with intermediate filaments in response to stress
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Djabali K., de Nechaud B., Landon F., Portier M-M. αB-crystallin interacts with intermediate filaments in response to stress. J Cell Sci. 110:1997;2759-2769.
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J Cell Sci
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Djabali, K.1
De Nechaud, B.2
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Portier, M.-M.4
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12
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0032586878
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Mutation R120G in αb-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
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The R120G point mutation in human αB-crystallin, which is genetically linked to desmin-related myopathy and cataracts, resulted in altered structure and function of the small heat-shock protein complex. The mutation is in the core α-crystallin domain of human αB-crystallin.
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Bova M.P., Yaron O., Huang Q., Ding L., Haley D.A., Stewart P.L., Horwitz J. Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc Natl Acad Sci USA. 96:1999;6137-6142. The R120G point mutation in human αB-crystallin, which is genetically linked to desmin-related myopathy and cataracts, resulted in altered structure and function of the small heat-shock protein complex. The mutation is in the core α-crystallin domain of human αB-crystallin.
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(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 6137-6142
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Bova, M.P.1
Yaron, O.2
Huang, Q.3
Ding, L.4
Haley, D.A.5
Stewart, P.L.6
Horwitz, J.7
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13
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0031849099
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Small heat-shock protein family: Function in health and disease
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This brief review of a research meeting summarizes studies on filaments, phosphorylation, binding regions, oxidative stress, novel binding proteins and multimerization of small heat-shock proteins.
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Welsh M.J., Gaestel M. Small heat-shock protein family: function in health and disease. Ann NY Acad Sci. 851:1998;28-35. This brief review of a research meeting summarizes studies on filaments, phosphorylation, binding regions, oxidative stress, novel binding proteins and multimerization of small heat-shock proteins.
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(1998)
Ann NY Acad Sci
, vol.851
, pp. 28-35
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Welsh, M.J.1
Gaestel, M.2
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14
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0032078108
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Mutations and modifications support a 'pitted-flexiball' model for α-crystallin
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Smulders R.H., van Boekel M.A., de Jong W.W. Mutations and modifications support a 'pitted-flexiball' model for α-crystallin. Int J Biol Macromol. 22:1998;187-196.
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(1998)
Int J Biol Macromol
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, pp. 187-196
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Smulders, R.H.1
Van Boekel, M.A.2
De Jong, W.W.3
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15
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0033522885
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Site-directed mutations within the core 'α-crystallin' domain of the small heat-shock protein, human αb-crystallin, decrease molecular chaperone functions
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Selected site-directed mutations that had no measurable effect on the secondary, tertiary and quaternary structure of human αB-crystallin were studied for their effects on chaperone activity. In the absence of structural modification, only the core domain mutants altered the function of αB-crystallin.
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Muchowski P.J., Wu G.J., Liang J.J., Adman E.T., Clark J.I. Site-directed mutations within the core 'α-crystallin' domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions. J Mol Biol. 289:1999;397-411. Selected site-directed mutations that had no measurable effect on the secondary, tertiary and quaternary structure of human αB-crystallin were studied for their effects on chaperone activity. In the absence of structural modification, only the core domain mutants altered the function of αB-crystallin.
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(1999)
J Mol Biol
, vol.289
, pp. 397-411
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Muchowski, P.J.1
Wu, G.J.2
Liang, J.J.3
Adman, E.T.4
Clark, J.I.5
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16
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0032477726
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ATP-enhanced molecular chaperone functions of the small heat shock protein human αb crystallin
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ATP was observed to enhance the chaperone activity of human αB-crystallin. This was the first experimental demonstration of an effect of ATP on the function of an sHsp.
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Muchowski P.J., Clark J.I. ATP-enhanced molecular chaperone functions of the small heat shock protein human αB crystallin. Proc Natl Acad Sci USA. 95:1998;1004-1009. ATP was observed to enhance the chaperone activity of human αB-crystallin. This was the first experimental demonstration of an effect of ATP on the function of an sHsp.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 1004-1009
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Muchowski, P.J.1
Clark, J.I.2
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17
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0033570053
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ATP and the core α crystallin domain of the small heat-shock protein αb-crystallin
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In the presence of ATP, the accessibility of trypsin and chymotrypsin cleavage sites within the core α-crystallin domain decreased. The results suggested that the effect of ATP on the function of αB-crystallin may involve interactions with the conserved core α-crystallin domain.
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Muchowski P.J., Hays L.G., Yates J.R., Clark J.I. ATP and the core α crystallin domain of the small heat-shock protein αB-crystallin. J Biol Chem. 274:1999;30190-30195. In the presence of ATP, the accessibility of trypsin and chymotrypsin cleavage sites within the core α-crystallin domain decreased. The results suggested that the effect of ATP on the function of αB-crystallin may involve interactions with the conserved core α-crystallin domain.
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(1999)
J Biol Chem
, vol.274
, pp. 30190-30195
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Muchowski, P.J.1
Hays, L.G.2
Yates, J.R.3
Clark, J.I.4
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19
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0033617266
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From computer simulations to human disease: Emerging themes in protein folding
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Radford S.E., Dobson C.M. From computer simulations to human disease: emerging themes in protein folding. Cell. 97:1999;291-298.
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Cell
, vol.97
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Radford, S.E.1
Dobson, C.M.2
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20
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Aggresomes: A cellular response to misfolded proteins
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Johnston J.A., Ward C.L., Kopito R.R. Aggresomes: a cellular response to misfolded proteins. J Cell Biol. 143:1998;1883-1898.
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J Cell Biol
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Johnston, J.A.1
Ward, C.L.2
Kopito, R.R.3
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21
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0032956263
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Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by αb-crystallin
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Recombinant adenovirus was used to increase the intracellular levels of αB-crystallin. The result demonstrated that αB-crystallin protected astrocytes from the formation of filamentous inclusions and reorganized the aggregated filament proteins into a normal filamentous network. The findings suggest the possible effectiveness of gene therapy using small heat-shock proteins.
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Koyama Y., Goldman J.E. Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by αB-crystallin. Am J Pathol. 154:1999;1563-1572. Recombinant adenovirus was used to increase the intracellular levels of αB-crystallin. The result demonstrated that αB-crystallin protected astrocytes from the formation of filamentous inclusions and reorganized the aggregated filament proteins into a normal filamentous network. The findings suggest the possible effectiveness of gene therapy using small heat-shock proteins.
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(1999)
Am J Pathol
, vol.154
, pp. 1563-1572
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Koyama, Y.1
Goldman, J.E.2
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22
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0033016166
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Fatal attraction: When chaperone turns harlot
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[news]
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Quinlan R., Van Den Ijssel P. Fatal attraction: when chaperone turns harlot. Nat Med. 5:1999;25-26. [news].
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Nat Med
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Quinlan, R.1
Van Den Ijssel, P.2
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23
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0031934121
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Autosomal dominant congenital cataract associated with a missense mutation in the human α-crystallin gene CRYAA
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This report demonstrates a genetic link between a mutation in a small heat-shock protein and autosomal dominant cataract in humans.
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Litt M., Kramer P., LaMorticella D.M., Murphey W., Lovrien E.W., Weleber R.G. Autosomal dominant congenital cataract associated with a missense mutation in the human α-crystallin gene CRYAA. Hum Mol Genet. 7:1998;471-474. This report demonstrates a genetic link between a mutation in a small heat-shock protein and autosomal dominant cataract in humans.
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(1998)
Hum Mol Genet
, vol.7
, pp. 471-474
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Litt, M.1
Kramer, P.2
Lamorticella, D.M.3
Murphey, W.4
Lovrien, E.W.5
Weleber, R.G.6
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24
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Recent advances in understanding the pathogenesis of Huntington's disease
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Reddy P.H., Williams M., Tagle D.A. Recent advances in understanding the pathogenesis of Huntington's disease. Trends Neurosci. 22:1999;248-255.
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Trends Neurosci
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Reddy, P.H.1
Williams, M.2
Tagle, D.A.3
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25
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Dementia, gliosis and expression of the small heat shock proteins hsp27 and αb-crystallin in Parkinson's disease
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Renkawek K., Stege G.J., Bosman G.J. Dementia, gliosis and expression of the small heat shock proteins hsp27 and αB-crystallin in Parkinson's disease. Neuroreport. 10:1999;2273-2276.
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Renkawek, K.1
Stege, G.J.2
Bosman, G.J.3
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26
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αb-crystallin is associated with intermediate filaments in astrocytoma cells
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Wisniewski T., Goldman J.E. αB-crystallin is associated with intermediate filaments in astrocytoma cells. Neurochem Res. 23:1998;385-392.
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Neurochem Res
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Wisniewski, T.1
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The fundamentals of protein folding: Bringing together theory and experiment
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Dobson C.M., Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Curr Opin Struct Biol. 9:1999;92-101.
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Curr Opin Struct Biol
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Dobson, C.M.1
Karplus, M.2
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Stress-response proteins in cardiovascular disease
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This comprehensive review summarizes the importance of small heat-shock proteins in cardiomyopathy.
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Xiao X., Benjamin I.J. Stress-response proteins in cardiovascular disease. Am J Hum Genet. 64:1999;685-690. This comprehensive review summarizes the importance of small heat-shock proteins in cardiomyopathy.
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(1999)
Am J Hum Genet
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Xiao, X.1
Benjamin, I.J.2
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30
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0031918807
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Lens α-crystallin: Chaperone-like properties
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A useful summary of the expression, purification and characterization of human αA-crystallin and αB-crystallin.
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Horwitz J., Huang Q.L., Ding L., Bova M.P. Lens α-crystallin: chaperone-like properties. Methods Enzymol. 290:1998;365-383. A useful summary of the expression, purification and characterization of human αA-crystallin and αB-crystallin.
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Methods Enzymol
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, pp. 365-383
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Horwitz, J.1
Huang, Q.L.2
Ding, L.3
Bova, M.P.4
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31
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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
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Ehrnsperger M., Graber S., Gaestel M., Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16:1997;221-229.
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Ehrnsperger, M.1
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Buchner, J.4
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32
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17344361902
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A missense mutation in the αb-crystallin chaperone gene causes a desmin-related myopathy
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This report makes a direct association between an R120G mutation in αB-crystallin and desmin-related myopathy in humans.
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Vicart P., Caron A., Guicheney P., Li Z., Prevost M.C., Faure A., Chateau D., Chapon F., Tomé F., Dupret J.M.et al. A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet. 20:1998;92-95. This report makes a direct association between an R120G mutation in αB-crystallin and desmin-related myopathy in humans.
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(1998)
Nat Genet
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Vicart, P.1
Caron, A.2
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Faure, A.6
Chateau, D.7
Chapon, F.8
Tomé, F.9
Dupret, J.M.10
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33
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0033545355
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Molecular chaperones: Small heat shock proteins in the limelight
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The importance of the interaction between intermediate filaments and small heat-shock proteins is summarized.
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van den Ijssel P., Norman D.G., Quinlan R.A. Molecular chaperones: small heat shock proteins in the limelight. Curr Biol. 9:1999;103-105. The importance of the interaction between intermediate filaments and small heat-shock proteins is summarized.
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Curr Biol
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, pp. 103-105
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Van Den Ijssel, P.1
Norman, D.G.2
Quinlan, R.A.3
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34
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0033588379
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Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins
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The effects of the R116C and R120G mutations on the structure and function of human αA-crystallin and αB-crystallin, respectively, were reported. Chaperone activity was reduced and both the secondary and tertiary structure were altered by the mutations.
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Kumar L.V., Ramakrishna T., Rao C.M. Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins. J Biol Chem. 274:1999;24137-24141. The effects of the R116C and R120G mutations on the structure and function of human αA-crystallin and αB-crystallin, respectively, were reported. Chaperone activity was reduced and both the secondary and tertiary structure were altered by the mutations.
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J Biol Chem
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, pp. 24137-24141
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Kumar, L.V.1
Ramakrishna, T.2
Rao, C.M.3
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35
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0032818827
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Intermediate filament interactions can be altered by HSP27 and αb-crystallin
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Small heat-shock proteins (sHsps) bind to and prevent network formation in solutions of intermediate filaments, suggesting that sHsps interact directly with intermediate filaments and regulate filament organization.
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Perng M.D., Cairns L., van den Ijssel P., Prescott A., Hutcheson A.M., Quinlan R.A. Intermediate filament interactions can be altered by HSP27 and αB-crystallin. J Cell Sci. 112:1999;2099-2112. Small heat-shock proteins (sHsps) bind to and prevent network formation in solutions of intermediate filaments, suggesting that sHsps interact directly with intermediate filaments and regulate filament organization.
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(1999)
J Cell Sci
, vol.112
, pp. 2099-2112
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Perng, M.D.1
Cairns, L.2
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Prescott, A.4
Hutcheson, A.M.5
Quinlan, R.A.6
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0027437510
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Expression of αb-crystallin in human brain tumors
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Aoyama A., Steiger R.H., Fröhli E., Schäfer R., von Deimling A., Wiestler O.D., Klemenz R. Expression of αB-crystallin in human brain tumors. Int J Cancer. 55:1993;760-764.
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Aoyama, A.1
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Von Deimling, A.5
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Klemenz, R.7
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0031774301
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The small heat shock protein αb-crystallin as key autoantigen in multiple sclerosis
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This review highlights the possible importance of small heat-shock proteins in autoimmune disease.
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Van Noort J.M., van Sechel A.C., van Stipdonk M.J., Bajramovic J.J. The small heat shock protein αB-crystallin as key autoantigen in multiple sclerosis. Prog Brain Res. 117:1998;435-452. This review highlights the possible importance of small heat-shock proteins in autoimmune disease.
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Prog Brain Res
, vol.117
, pp. 435-452
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Van Noort, J.M.1
Van Sechel, A.C.2
Van Stipdonk, M.J.3
Bajramovic, J.J.4
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0032790422
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High prevalence of anti-α-crystallin antibodies in multiple sclerosis: Correlation with severity and activity of disease
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Agius M.A., Kirvan C.A., Schafer A.L., Gudipati E., Zhu S. High prevalence of anti-α-crystallin antibodies in multiple sclerosis: correlation with severity and activity of disease. Acta Neurol Scand. 100:1999;139-147.
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Acta Neurol Scand
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Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection
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Brenner B.G., Wainberg M.A. Heat shock protein-based therapeutic strategies against human immunodeficiency virus type 1 infection. Infect Dis Obstet Gynecol. 7:1999;80-90.
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