-
2
-
-
0041822089
-
Cell biology: Join the crowd
-
Ellis R. J. and Minton A. P. (2003) Cell biology: join the crowd. Nature 425: 27-28
-
(2003)
Nature
, vol.425
, pp. 27-28
-
-
Ellis, R.J.1
Minton, A.P.2
-
3
-
-
0035478585
-
Macromolecular crowding: Obvious but underappreciated
-
Ellis R. J. (2001) Macromolecular crowding: obvious but underappreciated. Trends iochem. Sci. 26: 597-604
-
(2001)
Trends Iochem. Sci.
, vol.26
, pp. 597-604
-
-
Ellis, R.J.1
-
4
-
-
0035815743
-
The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
-
Minton A. P. (2001) The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276: 10577-10580
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 10577-10580
-
-
Minton, A.P.1
-
5
-
-
0347357617
-
Protein folding and misfolding
-
Dobson C. M. (2003) Protein folding and misfolding. Nature 426: 884-890
-
(2003)
Nature
, vol.426
, pp. 884-890
-
-
Dobson, C.M.1
-
6
-
-
0034924812
-
Folding of newly translated proteins in vivo: The role of molecular chaperones
-
Frydman J. (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70: 603-647
-
(2001)
Annu. Rev. Biochem.
, vol.70
, pp. 603-647
-
-
Frydman, J.1
-
7
-
-
17044387386
-
Hsp70 chaperones: Cellular functions and molecular mechanism
-
Mayer M. P. and Bukau B. (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62: 670-6840
-
(2005)
Cell. Mol. Life Sci.
, vol.62
, pp. 670-6840
-
-
Mayer, M.P.1
Bukau, B.2
-
11
-
-
1142302227
-
Molecular chaperones: Structure of a protein disaggregase
-
Mogk A. and Bukau B. (2004) Molecular chaperones: structure of a protein disaggregase. Curr. Biol. 14: R78-R80
-
(2004)
Curr. Biol.
, vol.14
-
-
Mogk, A.1
Bukau, B.2
-
12
-
-
11144356089
-
CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
-
Petrucelli L., Dickson D., Kehoe K., Taylor J., Snyder H., Grove A. et al. (2004) CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum. Mol. Genet. 13: 703-714
-
(2004)
Hum. Mol. Genet.
, vol.13
, pp. 703-714
-
-
Petrucelli, L.1
Dickson, D.2
Kehoe, K.3
Taylor, J.4
Snyder, H.5
Grove, A.6
-
13
-
-
0036809333
-
sHSPs and their role in the chaperone network
-
Haslbeck M. (2002) sHSPs and their role in the chaperone network. Cell. Mol. Life Sci. 59: 1649-1657
-
(2002)
Cell. Mol. Life Sci.
, vol.59
, pp. 1649-1657
-
-
Haslbeck, M.1
-
14
-
-
0033927557
-
Structure and function of small heat shock/α-crystallin proteins: Established concepts and emerging ideas
-
MacRae T. H. (2000) Structure and function of small heat shock/α-crystallin proteins: established concepts and emerging ideas. Cell. Mol. Life Sci. 57 899-913
-
(2000)
Cell. Mol. Life Sci.
, vol.57
, pp. 899-913
-
-
MacRae, T.H.1
-
15
-
-
16844368450
-
The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state
-
Matuszewska M., Kuczy ska-Wi nik D., Laskowska E. and Liberek K. (2005) The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state. J. Biol. Chem. 280: 12292-12298
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 12292-12298
-
-
Matuszewska, M.1
Kuczyska-Winik, D.2
Laskowska, E.3
Liberek, K.4
-
16
-
-
14744291911
-
Small heat shock proteins: A new classification scheme in mammals
-
Taylor R. P. and Benjamin I. V. (2005) Small heat shock proteins: a new classification scheme in mammals. J. Mol. Cell Cardiol. 38: 433-444
-
(2005)
J. Mol. Cell Cardiol.
, vol.38
, pp. 433-444
-
-
Taylor, R.P.1
Benjamin, I.V.2
-
17
-
-
11944259586
-
Evolutionary diversity of vertebrate small heat shock proteins
-
Frank E., Madsen O., van Rheede T., Ricard G., Huynen M. A. and de Jong W. W. (2004) Evolutionary diversity of vertebrate small heat shock proteins. J. Mol. Evol. 59: 792-805
-
(2004)
J. Mol. Evol.
, vol.59
, pp. 792-805
-
-
Frank, E.1
Madsen, O.2
Van Rheede, T.3
Ricard, G.4
Huynen, M.A.5
De Jong, W.W.6
-
18
-
-
16644382368
-
α-crystallin: A review of its structure and function
-
Augusteyn R. C. (2004) α-crystallin: a review of its structure and function. Clin. Exp. Optom. 87: 356-366
-
(2004)
Clin. Exp. Optom.
, vol.87
, pp. 356-366
-
-
Augusteyn, R.C.1
-
19
-
-
3442885854
-
Small heat shock proteins from extremophiles: A review
-
Laksanalamai P. and Robb F. T. (2004) Small heat shock proteins from extremophiles: a review. Extremophiles 8: 1-11
-
(2004)
Extremophiles
, vol.8
, pp. 1-11
-
-
Laksanalamai, P.1
Robb, F.T.2
-
20
-
-
0036195722
-
α-crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
-
Narberhaus F. (2002) α-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
-
22
-
-
13144276278
-
Small heat shock protein of Methanococcus jannaschii, a hyperthermophile
-
USA
-
Kim R., Kim K. K., Yokota H. and Kim S.-H. (1998) Small heat shock protein of Methanococcus jannaschii, a hyperthermophile. Proc. Natl. Acad. Sci. USA 95: 9129-9133
-
(1998)
Proc. Natl. Acad. Sci.
, vol.95
, pp. 9129-9133
-
-
Kim, R.1
Kim, K.K.2
Yokota, H.3
Kim, S.-H.4
-
23
-
-
1342292267
-
Crystal structure of a small heat-shock protein
-
Kim K. K., Kim R. and Kim S.-H. (1998) Ciystal structure of a small heat-shock protein. Nature 394: 595-599
-
(1998)
Nature
, vol.394
, pp. 595-599
-
-
Kim, K.K.1
Kim, R.2
Kim, S.-H.3
-
24
-
-
0035191639
-
Crystal structure and assembly of a eukaryotic small heat shock protein
-
van Montfort R. L. M., Basha E., Friedrich K. L., Slingsby C. and Vierling E. (2001) Crystal structure and assembly of a eukaryotic small heat shock protein. Nat. Struct. Biol. 8: 1025-1030
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 1025-1030
-
-
Van Montfort, R.L.M.1
Basha, E.2
Friedrich, K.L.3
Slingsby, C.4
Vierling, E.5
-
25
-
-
20444478694
-
The small heat shock proteins and their role in human disease
-
Sun Y. and MacRae T. H. (2005) The small heat shock proteins and their role in human disease. FEBS J. 272: 2613-2627
-
(2005)
FEBS J.
, vol.272
, pp. 2613-2627
-
-
Sun, Y.1
MacRae, T.H.2
-
26
-
-
27144449614
-
Diapause: Diverse states of developmental and metabolic arrest
-
MacRae T. H. (2005) Diapause: diverse states of developmental and metabolic arrest. J. Biol. Res. 3: 3-14
-
(2005)
J. Biol. Res.
, vol.3
, pp. 3-14
-
-
MacRae, T.H.1
-
27
-
-
1442289304
-
Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae
-
Haslbeck M., Braun N., Stromer T., Richter B., Model N., Weinkauf S. et al. (2004) Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J. 23: 1-12
-
(2004)
EMBO J.
, vol.23
, pp. 1-12
-
-
Haslbeck, M.1
Braun, N.2
Stromer, T.3
Richter, B.4
Model, N.5
Weinkauf, S.6
-
28
-
-
0346463052
-
Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes
-
Friedrich K. L., Giese K. C., Buan N. R. and Vierling E. (2004) Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes. J. Biol. Chem. 279: 1080-1089
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 1080-1089
-
-
Friedrich, K.L.1
Giese, K.C.2
Buan, N.R.3
Vierling, E.4
-
29
-
-
1542320089
-
The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions
-
Basha E., Lee G. J., Breci L. A., Hausrath A. C., Buan N. R., Giese K. C. et al. (2004) The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions. J. Biol. Chem. 279: 7566-7575
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 7566-7575
-
-
Basha, E.1
Lee, G.J.2
Breci, L.A.3
Hausrath, A.C.4
Buan, N.R.5
Giese, K.C.6
-
30
-
-
0036306093
-
The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin: A structural and kinetic spectroscopic study
-
Carver J. A., Lindner R. A., Lyon C., Canet D., Hernandez H. Dobson C. M. et al. (2002) The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin: a structural and kinetic spectroscopic study. J. Mol. Biol. 318: 815-827
-
(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
-
31
-
-
0035865589
-
The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin
-
Lindner R.A., Treweek T.M. and Carver J.A. (2001) The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin. Biochem. J. 354: 79-87
-
(2001)
Biochem. J.
, vol.354
, pp. 79-87
-
-
Lindner, R.A.1
Treweek, T.M.2
Carver, J.A.3
-
32
-
-
0034739275
-
The small heat-shock chaperone protein, α-crystallin, does not recognize stable molten globule states of cytosolic proteins
-
Treweek T. M., Lindner R. A., Mariani M. and Carver J. A. (2000) The small heat-shock chaperone protein, α-crystallin, does not recognize stable molten globule states of cytosolic proteins. Biochim. Biophys. Acta 1481: 175-188
-
(2000)
Biochim. Biophys. Acta
, vol.1481
, pp. 175-188
-
-
Treweek, T.M.1
Lindner, R.A.2
Mariani, M.3
Carver, J.A.4
-
33
-
-
0033485868
-
Hsp26: A temperature-regulated chaperone
-
Haslbeck M., Walke S., Stromer T., Ehrnsperger M., White H. E., Chen S. et al. (1999) Hsp26: a temperature-regulated chaperone. EMBO J. 18: 6744-6751
-
(1999)
EMBO J.
, vol.18
, pp. 6744-6751
-
-
Haslbeck, M.1
Walke, S.2
Stromer, T.3
Ehrnsperger, M.4
White, H.E.5
Chen, S.6
-
34
-
-
0031024691
-
A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
-
Lee G. J., Roseman A .M., Saibil H. R. and Vierling, E. (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16: 659-671
-
(1997)
EMBO J.
, vol.16
, pp. 659-671
-
-
Lee, G.J.1
Roseman, A.M.2
Saibil, H.R.3
Vierling, E.4
-
36
-
-
0038043235
-
Analysis of the interaction of small heat shock proteins with unfolding proteins
-
Stromer T, Ehrnsperher M., Gaestel M. and Buchner J. (2003) Analysis of the interaction of small heat shock proteins with unfolding proteins. J. Biol. Chem. 278: 18015-18021
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 18015-18021
-
-
Stromer, T.1
Ehrnsperher, M.2
Gaestel, M.3
Buchner, J.4
-
37
-
-
0242582458
-
Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to αB-crystallin
-
Sathish H. A., Stein R. A., Yang G. and Mchaourab H. S. (2003) Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to αB-crystallin. J. Biol. Chem. 278: 44214-44221
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 44214-44221
-
-
Sathish, H.A.1
Stein, R.A.2
Yang, G.3
Mchaourab, H.S.4
-
38
-
-
0035947181
-
Interaction of human recombinant αA- And αB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation
-
Rajaraman K., Raman B., Ramakrishna T. and Rao Ch. M. (2001) Interaction of human recombinant αA- and αB-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, Ch.M.4
-
39
-
-
5644275139
-
Role of ATP on the interaction of α-crystallin with its substrates and its implications for the molecular chaperone function
-
Biswas A. and Das K. P. (2004) Role of ATP on the interaction of α-crystallin with its substrates and its implications for the molecular chaperone function. J. Biol. Chem. 279: 42648-42657
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 42648-42657
-
-
Biswas, A.1
Das, K.P.2
-
40
-
-
0035853131
-
Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding
-
USA
-
Török Z., Goloubinoff P., Horváth I., Tsvetkova N. M., Glatz A., Balogh G. et al. (2001) Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding. Proc. Natl. Acad. Sci. USA 98: 3098-3103
-
(2001)
Proc. Natl. Acad. Sci.
, vol.98
, pp. 3098-3103
-
-
Török, Z.1
Goloubinoff, P.2
Horváth, I.3
Tsvetkova, N.M.4
Glatz, A.5
Balogh, G.6
-
41
-
-
0343742639
-
Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
-
Ehrnsperger M., Gräber S., Gaestel M. and Buchner J. (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16: 221-229
-
(1997)
EMBO J.
, vol.16
, pp. 221-229
-
-
Ehrnsperger, M.1
Gräber, S.2
Gaestel, M.3
Buchner, J.4
-
42
-
-
0037636275
-
The molecular chaperone α-crystallin incorporated into red cell ghosts protects membrane Na/K-ATPase against glycation and oxidative stress
-
Derham B. K., Ellory J. C., Bron A. J. and Harding, J.J. (2003) The molecular chaperone α-crystallin incorporated into red cell ghosts protects membrane Na/K-ATPase against glycation and oxidative stress. Eur. J. Biochem. 270: 2605-2611
-
(2003)
Eur. J. Biochem.
, vol.270
, pp. 2605-2611
-
-
Derham, B.K.1
Ellory, J.C.2
Bron, A.J.3
Harding, J.J.4
-
43
-
-
2142768810
-
Chaperone activity of cytosolic small heat shock proteins from wheat
-
Basha E., Lee G. J., Demeler B. and Vierling E. (2004) Chaperone activity of cytosolic small heat shock proteins from wheat. Eur. J. Biochem. 271: 1426-1436
-
(2004)
Eur. J. Biochem.
, vol.271
, pp. 1426-1436
-
-
Basha, E.1
Lee, G.J.2
Demeler, B.3
Vierling, E.4
-
44
-
-
11844257596
-
Cytoxic effects induced by oxidative stress in cultured mammalian cells and protection provided by Hsp27 expression
-
Arrigo A.-P., Firdaus W. J. J., Mellier G., Moulin M., Paul C., Diaz-latoud C. et al. (2005) Cytoxic effects induced by oxidative stress in cultured mammalian cells and protection provided by Hsp27 expression. Methods 35: 126-138
-
(2005)
Methods
, vol.35
, pp. 126-138
-
-
Arrigo, A.-P.1
Firdaus, W.J.J.2
Mellier, G.3
Moulin, M.4
Paul, C.5
Diaz-latoud, C.6
-
45
-
-
20144374696
-
The small heat shock protein αB-crystallin is a novel inhibitor of TRAIL-induced apoptosis that suppresses the activation of caspase-3
-
Kamradt M. C., Lu M., Werner M. E., Kwan T., Chen F., Strohecker A. et al. (2005) The small heat shock protein αB-crystallin is a novel inhibitor of TRAIL-induced apoptosis that suppresses the activation of caspase-3. J. Biol. Chem. 280: 11059-11066
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 11059-11066
-
-
Kamradt, M.C.1
Lu, M.2
Werner, M.E.3
Kwan, T.4
Chen, F.5
Strohecker, A.6
-
46
-
-
1642354104
-
HSP25 is involved in two steps of the differentiation of PAM212 keratinocytes
-
Duverger O., Paslaru L. and Morange M. (2004) HSP25 is involved in two steps of the differentiation of PAM212 keratinocytes. J. Biol. Chem. 279: 10252-10260
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 10252-10260
-
-
Duverger, O.1
Paslaru, L.2
Morange, M.3
-
47
-
-
0041525250
-
A small heat shock/α-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation
-
Day R. M., Gupta J. S. and MacRae T. H. (2003) A small heat shock/α-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation. Cell Stress Chaperones 8: 183-193
-
(2003)
Cell Stress Chaperones
, vol.8
, pp. 183-193
-
-
Day, R.M.1
Gupta, J.S.2
MacRae, T.H.3
-
48
-
-
0242637569
-
αB-crystallin modulates protein aggregation of abnormal desmin
-
Wang X., Klevitsky R., Huang W., Glasford J., Li F. and Robbins J. (2003) αB-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
-
49
-
-
0037338308
-
Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin
-
Panasenko O. O., Kim M. V., Marston S. B. and Gusev N. B. (2003) Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin. Eur. J. Biochem. 270: 892-901
-
(2003)
Eur. J. Biochem.
, vol.270
, pp. 892-901
-
-
Panasenko, O.O.1
Kim, M.V.2
Marston, S.B.3
Gusev, N.B.4
-
50
-
-
0036556697
-
Actin cytoskeleton and small heat shock proteins: How do they interact?
-
Mounier N. and Arrigo A.-P. (2002) Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones 7: 167-176
-
(2002)
Cell Stress Chaperones
, vol.7
, pp. 167-176
-
-
Mounier, N.1
Arrigo, A.-P.2
-
51
-
-
0000843475
-
The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
-
Perng M. D., Muchowski P. J., van den IJssel P., Wu G. J. S, Hutcheson A. M., Clark J. I. et al. (1999) The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem. 274: 33235-33243
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 33235-33243
-
-
Perng, M.D.1
Muchowski, P.J.2
Van Den Ijssel, P.3
Wu, G.J.S.4
Hutcheson, A.M.5
Clark, J.I.6
-
52
-
-
0032818827
-
Intermediate filament interactions can be altered by HSP27 and αB-crystallin
-
Perng M. D., Cairns L., van den IJssel P., Prescott A., Hutcheson A. M. and Quinlan R. A. (1999) Intermediate filament interactions can be altered by HSP27 and αB-crystallin. J. Cell Sci. 112: 2099-2112
-
(1999)
J. Cell Sci.
, vol.112
, pp. 2099-2112
-
-
Perng, M.D.1
Cairns, L.2
Van Den Ijssel, P.3
Prescott, A.4
Hutcheson, A.M.5
Quinlan, R.A.6
-
53
-
-
0032586878
-
Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
-
USA
-
Bova M. P., Yaron O., Huang Q., Ding L., Haley D. A., Stewart P. L. et al. (1999) 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: 6137-6142
-
(1999)
Proc. Natl. Acad. Sci.
, 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
-
54
-
-
0742322606
-
Molecular chaperones, stress resistance and development in Artemia franciscana
-
MacRae T. H. (2003) Molecular chaperones, stress resistance and development in Artemia franciscana. Semin. Cell Dev. Biol. 14: 251-258
-
(2003)
Semin. Cell Dev. Biol.
, vol.14
, pp. 251-258
-
-
MacRae, T.H.1
-
55
-
-
2342439076
-
αB-crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly
-
Fujita Y., Ohto E., Katayama E. and Atomi, Y. (2004) αB-crystallin- coated MAP microtubule resists nocodazole and calcium-induced disassembly. J. Cell Sci. 117: 1719-1726
-
(2004)
J. Cell Sci.
, vol.117
, pp. 1719-1726
-
-
Fujita, Y.1
Ohto, E.2
Katayama, E.3
Atomi, Y.4
-
56
-
-
0035544297
-
αB-crystallin phosphorylated at Ser-59 is localized in centrosomes and midbodies during mitosis
-
Inaguma Y., Ito H., Iwamoto I., Saga S. and Kato K. (2001) αB-crystallin phosphorylated at Ser-59 is localized in centrosomes and midbodies during mitosis. Eur. J. Cell Biol. 80: 741-748
-
(2001)
Eur. J. Cell Biol.
, vol.80
, pp. 741-748
-
-
Inaguma, Y.1
Ito, H.2
Iwamoto, I.3
Saga, S.4
Kato, K.5
-
57
-
-
0028071812
-
Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
-
Benndorf R., Hayeß K., Ryazantsev S., Wieske M., Behlke J. and Lutsch G. (1994) Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J. Biol. Chem. 269: 20780-20784
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 20780-20784
-
-
Benndorf, R.1
Hayeß, K.2
Ryazantsev, S.3
Wieske, M.4
Behlke, J.5
Lutsch, G.6
-
58
-
-
0034843626
-
Defined sequence segments of the small heat shock proteins HSP25 and αB-crystallin inhibit actin polymerization
-
Wieske M., Benndorf R., Behlke J., Dölling R., Grelle G., Bielka H. et al. (2001) Defined sequence segments of the small heat shock proteins HSP25 and αB-crystallin inhibit actin polymerization. Eur. J. Biochem. 268: 2083-2090
-
(2001)
Eur. J. Biochem.
, vol.268
, pp. 2083-2090
-
-
Wieske, M.1
Benndorf, R.2
Behlke, J.3
Dölling, R.4
Grelle, G.5
Bielka, H.6
-
60
-
-
0031056783
-
Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27
-
Guay J., Lambert H., Gingras-Breton G., Lavoie J. N., Huot J. and Landry J. (1997) Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. J. Cell Sci. 110: 357-368
-
(1997)
J. Cell Sci.
, vol.110
, pp. 357-368
-
-
Guay, J.1
Lambert, H.2
Gingras-Breton, G.3
Lavoie, J.N.4
Huot, J.5
Landry, J.6
-
61
-
-
0030069517
-
HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
-
Huot J., Houle F., Spitz D. R. and Landry J. (1996) HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Can. Res. 56: 273-279
-
(1996)
Can. Res.
, vol.56
, pp. 273-279
-
-
Huot, J.1
Houle, F.2
Spitz, D.R.3
Landry, J.4
-
62
-
-
0036556789
-
Distribution, phosphorylation and activities of Hsp25 in heat-stressed H9c2 myoblasts: A functinal link to cytoprotection
-
Bryantsev A. L., Loktionova S. A., Ilyinskaya O. P., Tararak E. M., Kampinga H. H. and Kabakov A. E. (2002) Distribution, phosphorylation and activities of Hsp25 in heat-stressed H9c2 myoblasts: a functinal link to cytoprotection. Cell Stress Chaperones 7: 146-155
-
(2002)
Cell Stress Chaperones
, vol.7
, pp. 146-155
-
-
Bryantsev, A.L.1
Loktionova, S.A.2
Ilyinskaya, O.P.3
Tararak, E.M.4
Kampinga, H.H.5
Kabakov, A.E.6
-
63
-
-
0037709152
-
The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin
-
Tessier D. J., Komalavilas P., Panitch A., Joshi L. and Brophy C. M. (2003) The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin. J. Surg. Res. 111: 152-157
-
(2003)
J. Surg. Res.
, vol.111
, pp. 152-157
-
-
Tessier, D.J.1
Komalavilas, P.2
Panitch, A.3
Joshi, L.4
Brophy, C.M.5
-
64
-
-
17044438616
-
The association of small heat shock protein 16.3 with the plasma membrane of Mycobacterium tuberculosis: Dissociation of oligomers is a prerequisite
-
Zhang H., Fu X., Jiao W., Zhang X., Liu C. and Chang Z. (2005) The association of small heat shock protein 16.3 with the plasma membrane of Mycobacterium tuberculosis: Dissociation of oligomers is a prerequisite. Biochem. Biophys. Res. Commun. 330: 1055-1061
-
(2005)
Biochem. Biophys. Res. Commun.
, vol.330
, pp. 1055-1061
-
-
Zhang, H.1
Fu, X.2
Jiao, W.3
Zhang, X.4
Liu, C.5
Chang, Z.6
-
65
-
-
0141459044
-
Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer
-
Chen Y., Lu Y.-J., Wang H.-W., Quan S., Chang Z. and Sui S.-F. (2003) Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer. Biochem. Biophys. Res. Commun. 310: 360-366
-
(2003)
Biochem. Biophys. Res. Commun.
, vol.310
, pp. 360-366
-
-
Chen, Y.1
Lu, Y.-J.2
Wang, H.-W.3
Quan, S.4
Chang, Z.5
Sui, S.-F.6
-
66
-
-
0038745648
-
Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants
-
Abulimiti A., Qiu X., Chen J., Liu Y. and Chang Z. (2003) Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants. Biochem. Biophys. Res. Commun. 305: 87-93
-
(2003)
Biochem. Biophys. Res. Commun.
, vol.305
, pp. 87-93
-
-
Abulimiti, A.1
Qiu, X.2
Chen, J.3
Liu, Y.4
Chang, Z.5
-
67
-
-
0034009392
-
Characterization of α-crystallin-plasma membrane binding
-
Cobb B. A. and Petrash J. M. (2000) Characterization of α-crystallin-plasma membrane binding. J. Biol. Chem. 275: 6664-6672
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 6664-6672
-
-
Cobb, B.A.1
Petrash, J.M.2
-
68
-
-
0037108910
-
Small heat-shock proteins regulate membrane lipid polymorphism
-
USA
-
Tsvetkova N. M., Horváth I., Török Z., Wolkers W. F., Balogi Z., Shigapova N. et al. (2002) Small heat-shock proteins regulate membrane lipid polymorphism. Proc. Natl. Acad. Sci. USA 99: 13504-13509
-
(2002)
Proc. Natl. Acad. Sci.
, vol.99
, pp. 13504-13509
-
-
Tsvetkova, N.M.1
Horváth, I.2
Török, Z.3
Wolkers, W.F.4
Balogi, Z.5
Shigapova, N.6
-
69
-
-
0034099317
-
HSP16.6 is involved in the development of thermotolerance and thylakoid stability in the unicellular Cyanobacterium, Synechocystis sp. PCC 6803
-
Lee S., Owen H. A., Prochaska D. J. and Barnum S. R. (2000) HSP16.6 is involved in the development of thermotolerance and thylakoid stability in the unicellular Cyanobacterium, Synechocystis sp. PCC 6803. Curr. Microbiol. 40: 283-287
-
(2000)
Curr. Microbiol.
, vol.40
, pp. 283-287
-
-
Lee, S.1
Owen, H.A.2
Prochaska, D.J.3
Barnum, S.R.4
-
70
-
-
0032584147
-
Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: Identification of hsp17 as a fluidity gene
-
USA
-
Horváth I., Glatz A., Varvasovszki V., Török Z., Páli T., Balogh G. et al. (1998) Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: identification of hsp17 as a fluidity gene. Proc. Natl. Acad. Sci. USA 95: 3513-3518
-
(1998)
Proc. Natl. Acad. Sci.
, vol.95
, pp. 3513-3518
-
-
Horváth, I.1
Glatz, A.2
Varvasovszki, V.3
Török, Z.4
Páli, T.5
Balogh, G.6
-
71
-
-
1242291781
-
Tomato heat stress protein Hsp16.1-CIII represents a member of a new class of nucleocytoplasmic small heat stress proteins in plants
-
Siddique M., Port M., Tripp J., Weber C., Zielinski D., Calligaris R. et al. (2003) Tomato heat stress protein Hsp16.1-CIII represents a member of a new class of nucleocytoplasmic small heat stress proteins in plants. Cell Stress Chaperones 8: 381-394
-
(2003)
Cell Stress Chaperones
, vol.8
, pp. 381-394
-
-
Siddique, M.1
Port, M.2
Tripp, J.3
Weber, C.4
Zielinski, D.5
Calligaris, R.6
-
72
-
-
0036665915
-
Stress protection by a fluorescent Hsp27 chimera that is independent of nuclear translocation or multimeric dissociation
-
Borrelli M. J., Bernock L. J., Landry J., Spitz D. R., Weber L. A., Hickey E. et al. (2002) Stress protection by a fluorescent Hsp27 chimera that is independent of nuclear translocation or multimeric dissociation. Cell Stress Chaperones 7: 281-296
-
(2002)
Cell Stress Chaperones
, vol.7
, pp. 281-296
-
-
Borrelli, M.J.1
Bernock, L.J.2
Landry, J.3
Spitz, D.R.4
Weber, L.A.5
Hickey, E.6
-
73
-
-
0032879383
-
The small heat shock proteins Hsp20 and αB-crystallin in cultured cardiac myocytes: Differences in cellular localization and solubilization after heat stress
-
van de Klundert F. A. J. M. and de Jong W. W. (1999) The small heat shock proteins Hsp20 and αB-crystallin in cultured cardiac myocytes: differences in cellular localization and solubilization after heat stress. Eur. J. Cell Biol. 78: 567-572
-
(1999)
Eur. J. Cell Biol.
, vol.78
, pp. 567-572
-
-
Van De Klundert, F.A.J.M.1
De Jong, W.W.2
-
74
-
-
4744353967
-
Testis-specific human small heat shock protein HSPB9 is a cancer/testis antigen, and potentially interacts with the dynein subunit TCTEL1
-
de Wit N. J. W., Verschuure P., Kappé G., King S. M., de Jong W. W., van Muijen G. N. P. et al. (2004) Testis-specific human small heat shock protein HSPB9 is a cancer/testis antigen, and potentially interacts with the dynein subunit TCTEL1. Eur. J. Cell Biol. 83: 337-345
-
(2004)
Eur. J. Cell Biol.
, vol.83
, pp. 337-345
-
-
De Wit, N.J.W.1
Verschuure, P.2
Kappé, G.3
King, S.M.4
De Jong, W.W.5
Van Muijen, G.N.P.6
-
75
-
-
0033559203
-
The synthesis of a small heat shock/α-crystallin protein in Artemia and its relationship to stress tolerance during development
-
Liang P. and MacRae T.H. (1999) The synthesis of a small heat shock/α-crystallin protein in Artemia and its relationship to stress tolerance during development. Dev. Biol. 207: 445-456
-
(1999)
Dev. Biol.
, vol.207
, pp. 445-456
-
-
Liang, P.1
MacRae, T.H.2
-
76
-
-
0035698491
-
Small heat shock protein p26 associates with nuclear matrix and HSP70 in nuclei and nuclear matrix fractions form stressed cells
-
Willsie J. K. and Clegg J. S. (2002) Small heat shock protein p26 associates with nuclear matrix and HSP70 in nuclei and nuclear matrix fractions form stressed cells. J. Cell. Biochem. 84: 601-614
-
(2002)
J. Cell. Biochem.
, vol.84
, pp. 601-614
-
-
Willsie, J.K.1
Clegg, J.S.2
-
77
-
-
8644246567
-
Mimicking phosphorylation of the small heat-shock protein αB-crystallin recruits the F-box protein FBX4 to nuclear SC35 speckles
-
den Engelsman J., Bennink E. J., Doerwald L., Onnekink C., Wunderink L., Andley U. P. et al. (2004) Mimicking phosphorylation of the small heat-shock protein αB-crystallin recruits the F-box protein FBX4 to nuclear SC35 speckles. Eur. J. Biochem. 271: 4195-4203
-
(2004)
Eur. J. Biochem.
, vol.271
, pp. 4195-4203
-
-
Den Engelsman, J.1
Bennink, E.J.2
Doerwald, L.3
Onnekink, C.4
Wunderink, L.5
Andley, U.P.6
-
78
-
-
4444246913
-
Heat stress-induced localization of small heat shock proteins in mouse myoblasts: Intranuclear lamin A/C speckles as target for αB-crystallin and Hsp25
-
Adhikari A. S., Rao K. S. Rangaraj N., Parnaik, V. K. and Rao Ch. M. (2004) Heat stress-induced localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for αB-crystallin and Hsp25. Exp. Cell Res. 299: 393-403
-
(2004)
Exp. Cell Res.
, vol.299
, pp. 393-403
-
-
Adhikari, A.S.1
Rao, K.S.2
Rangaraj, N.3
Parnaik, V.K.4
Rao, Ch.M.5
-
79
-
-
0043205911
-
Nuclear speckle localisation of the small heat shock protein αB-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation
-
van den IJssel P., Wheelock R., Prescott A., Russell P. and Quinlan R. A. (2003) Nuclear speckle localisation of the small heat shock protein αB-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation. Exp. Cell Res. 287: 249-261
-
(2003)
Exp. Cell Res.
, vol.287
, pp. 249-261
-
-
Van Den Ijssel, P.1
Wheelock, R.2
Prescott, A.3
Russell, P.4
Quinlan, R.A.5
-
80
-
-
0043132253
-
Nuclear staining for the small heat shock protein αB-crystallin colocalizes with splicing factor SC35
-
van Rijk A. F., Stege G. J. J., Bennink E. J., May A. and Bloemendal H. (2003) Nuclear staining for the small heat shock protein αB-crystallin colocalizes with splicing factor SC35. Eur. J. Cell Biol. 82: 361-368
-
(2003)
Eur. J. Cell Biol.
, vol.82
, pp. 361-368
-
-
Van Rijk, A.F.1
Stege, G.J.J.2
Bennink, E.J.3
May, A.4
Bloemendal, H.5
-
81
-
-
0028168805
-
α-crystallins are involved in specific interactions with the murine γD/E/F-crystallin-encoding gene
-
Pietrowski D., Durante M. J., Liebstein A., Schmitt-John T., Werner T. and Graw J. (1994) α-crystallins are involved in specific interactions with the murine γD/E/F-crystallin-encoding gene. Gene 144: 171-178
-
(1994)
Gene
, vol.144
, pp. 171-178
-
-
Pietrowski, D.1
Durante, M.J.2
Liebstein, A.3
Schmitt-John, T.4
Werner, T.5
Graw, J.6
-
82
-
-
0033012051
-
Bovine lens crystallins do contain helical structure: A circular dichroism study
-
Bloemendal M., Toumadje A. and Johnson W. C. Jr (1999) Bovine lens crystallins do contain helical structure: a circular dichroism study. Biochim. Biophys. Acta 1432: 234-238
-
(1999)
Biochim. Biophys. Acta
, vol.1432
, pp. 234-238
-
-
Bloemendal, M.1
Toumadje, A.2
Johnson Jr., W.C.3
-
83
-
-
0032077184
-
Interaction of DNA with bovine lens α-crystallin: Its functional implications
-
Singh K., Groth-Vasselli B. and Farnsworth P. N. (1998) Interaction of DNA with bovine lens α-crystallin: its functional implications. Int. J. Biol. Macromol. 22: 315-320
-
(1998)
Int. J. Biol. Macromol.
, vol.22
, pp. 315-320
-
-
Singh, K.1
Groth-Vasselli, B.2
Farnsworth, P.N.3
-
84
-
-
0033611157
-
RNA-binding proteins TIA-1 and TIAR link the phophorylation of eIF-2α to the assembly of mammalian stress granules
-
Kedersha N .L., Gupta M., Li W., Miller I. and Anderson P. (1999) RNA-binding proteins TIA-1 and TIAR link the phophorylation of eIF-2α to the assembly of mammalian stress granules. J. Cell Biol. 147: 1431-1442
-
(1999)
J. Cell Biol.
, vol.147
, pp. 1431-1442
-
-
Kedersha, N.L.1
Gupta, M.2
Li, W.3
Miller, I.4
Anderson, P.5
-
85
-
-
0031948387
-
The tomato Hsf system: HsfA2 needs interaction with HsfA1 for efficient nuclear import and may be localized in cytoplasmic heat stress granules
-
Scharf K.-D., Heider H., Höhfeld I., Lyck R., Schmidt E. and Nover L. (1998) The tomato Hsf system: HsfA2 needs interaction with HsfA1 for efficient nuclear import and may be localized in cytoplasmic heat stress granules. Mol. Cell. Biol. 18: 2240-2251
-
(1998)
Mol. Cell. Biol.
, vol.18
, pp. 2240-2251
-
-
Scharf, K.-D.1
Heider, H.2
Höhfeld, I.3
Lyck, R.4
Schmidt, E.5
Nover, L.6
-
86
-
-
0042318880
-
Solution structure and dynamics of a heat shock protein assembly probed by hydrogen exchange and mass spectrometry
-
Wintrode P. L., Friedrich K. L., Vierling E., Smith J. B. and Smith D. L. (2003) Solution structure and dynamics of a heat shock protein assembly probed by hydrogen exchange and mass spectrometry. Biochemistry 42: 10667-10673
-
(2003)
Biochemistry
, vol.42
, pp. 10667-10673
-
-
Wintrode, P.L.1
Friedrich, K.L.2
Vierling, E.3
Smith, J.B.4
Smith, D.L.5
-
87
-
-
0037039153
-
The αA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with αB-crystallin
-
Bera S. and Abraham E. C. (2002) The αA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with αB-crystallin. Biochemistry 41: 297-305
-
(2002)
Biochemistry
, vol.41
, pp. 297-305
-
-
Bera, S.1
Abraham, E.C.2
-
88
-
-
0037155819
-
The R116C mutation in αA-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis
-
Andley, U. P., Patel H. C. and Xi J.-H. (2002) The R116C mutation in αA-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis. J. Biol. Chem. 277: 10178-10186
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 10178-10186
-
-
Andley, U.P.1
Patel, H.C.2
Xi, J.-H.3
-
89
-
-
0034719154
-
Structural and functional changes in the αA-crystallin R116C mutant in hereditary cataracts
-
Cobb B. A. and Petrash J. M. (2000) Structural and functional changes in the αA-crystallin R116C mutant in hereditary cataracts. Biochemistry 39: 15791-15798
-
(2000)
Biochemistry
, vol.39
, pp. 15791-15798
-
-
Cobb, B.A.1
Petrash, J.M.2
-
90
-
-
0037427451
-
Structural and functional defects caused by point mutations in the a-crystallin domain of a bacterial a-heat shock protein
-
Lentze N., Studer S. and Narberhaus F. (2003) Structural and functional defects caused by point mutations in the a-crystallin domain of a bacterial a-heat shock protein. J. Mol. Biol. 328: 927-937
-
(2003)
J. Mol. Biol.
, vol.328
, pp. 927-937
-
-
Lentze, N.1
Studer, S.2
Narberhaus, F.3
-
91
-
-
0033607618
-
Folding pattern of the α-crystallin domain in αA-crystallin determined by site-directed spin labeling
-
Koteiche H. A. and Mchaourab H. S. (1999) Folding pattern of the α-crystallin domain in αA-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
-
92
-
-
0034724559
-
Small heat-shock protein structures reveal a continum from symmetric to variable assemblies
-
Haley D. A., Bova M. P., Huang Q. L., Mchaourab H. S. and Stewart P. L. (2000) Small heat-shock protein structures reveal a continum from symmetric to variable assemblies. J. Mol. Biol. 298: 261-272
-
(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
-
93
-
-
0242352386
-
Three-dimensional models corresponding to the C-terminal domain of human αA- And αB-crystallins based on the crystal structure of the small heat-shock protein HSP16.9 from wheat
-
Guruprasad K. and Kumari K. (2003) Three-dimensional models corresponding to the C-terminal domain of human αA- and αB-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
-
94
-
-
0033522885
-
Site-directed mutations within the core α-crystallin domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions
-
Muchowski P. J., Wu G. J. S., Liang J. J. N., Adman E. T. and Clark J. I. (1999) 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: 397-111
-
(1999)
J. Mol. Biol.
, vol.289
, pp. 397-1111
-
-
Muchowski, P.J.1
Wu, G.J.S.2
Liang, J.J.N.3
Adman, E.T.4
Clark, J.I.5
-
95
-
-
0034809339
-
Preheat treatment for Mycobacterium tuberculosis Hsp16.3: Correlation between a structural phase change at 60°C and a dramatic increase in chaperone-like activity
-
Mao Q., Ke D., Feng X. and Chang Z. (2001) Preheat treatment for Mycobacterium tuberculosis Hsp16.3: correlation between a structural phase change at 60°C and a dramatic increase in chaperone-like activity. Biochem. Biophys. Res. Commun. 284: 942-947
-
(2001)
Biochem. Biophys. Res. Commun.
, vol.284
, pp. 942-947
-
-
Mao, Q.1
Ke, D.2
Feng, X.3
Chang, Z.4
-
96
-
-
0034822088
-
Chaperone function of mutant versions of αA- And αB-crystallin prepared to pinpoint chaperone binding sites
-
Derham B. K., van Boekel M. A. M., Muchowski P. J., Clark J. I., Horwitz J., Hepburne-Scott H. W. et al. (2001) Chaperone function of mutant versions of αA- and αB-crystallin prepared to pinpoint chaperone binding sites. Eur. J. Biochem. 268: 713-721
-
(2001)
Eur. J. Biochem.
, vol.268
, pp. 713-721
-
-
Derham, B.K.1
Van Boekel, M.A.M.2
Muchowski, P.J.3
Clark, J.I.4
Horwitz, J.5
Hepburne-Scott, H.W.6
-
97
-
-
0035861759
-
71 is essential for chaperone-like function in αA-crystallin
-
71 is essential for chaperone-like function in αA-crystallin. J. Biol. Chem. 276: 47094-17099
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 47094-117099
-
-
Santhoshkumar, P.1
Sharma, K.K.2
-
98
-
-
0031934121
-
Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
-
Litt M., Kramer P., LaMorticella D. M., Murphey W., Lovrien E. W. and Weleber R. G. (1998) Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum. Mol. Genet. 7: 471-174
-
(1998)
Hum. Mol. Genet.
, vol.7
, pp. 471-1174
-
-
Litt, M.1
Kramer, P.2
LaMorticella, D.M.3
Murphey, W.4
Lovrien, E.W.5
Weleber, R.G.6
-
99
-
-
17344361902
-
A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy
-
Vicart P., Caron A., Guicheney P., Li Z., Prévost M.-C., Faure A. et al. (1998) A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy. Nat. Genet. 20: 92-95
-
(1998)
Nat. Genet.
, vol.20
, pp. 92-95
-
-
Vicart, P.1
Caron, A.2
Guicheney, P.3
Li, Z.4
Prévost, M.-C.5
Faure, A.6
-
100
-
-
14844355848
-
The essential role of the flexible termini in the temperature- responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli
-
Jiao W., Qian M., Li P., Zhao L. and Chang, Z. (2005) The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli. J. Mol. Biol. 347: 871-884
-
(2005)
J. Mol. Biol.
, vol.347
, pp. 871-884
-
-
Jiao, W.1
Qian, M.2
Li, P.3
Zhao, L.4
Chang, Z.5
-
101
-
-
14844340165
-
N-terminal control of small heat shock protein oligomerization: Changes in aggregate size and chaperone-like function
-
Eifert C., Burgio M. R., Bennett P. M., Salerno J. C. and Koretz J. F. (2005) N-terminal control of small heat shock protein oligomerization: Changes in aggregate size and chaperone-like function. Biochim. Biophys. Acta 1748: 146-156
-
(2005)
Biochim. Biophys. Acta
, vol.1748
, pp. 146-156
-
-
Eifert, C.1
Burgio, M.R.2
Bennett, P.M.3
Salerno, J.C.4
Koretz, J.F.5
-
102
-
-
9644260484
-
Self-association of a small heat shock protein
-
Lelj-Garolla B. and Mauk A. G. (2004) Self-association of a small heat shock protein. J. Mol. Biol. 345: 631-642104
-
(2004)
J. Mol. Biol.
, vol.345
, pp. 631-642104
-
-
Lelj-Garolla, B.1
Mauk, A.G.2
-
103
-
-
4544356426
-
Oligomerization, chaperone activity and nuclear localization of p26, a small heat shock protein from Artemia franciscana
-
Sun Y., Mansour M., Crack J. A., Gass G. L. and MacRae T. H. (2004) Oligomerization, chaperone activity and nuclear localization of p26, a small heat shock protein from Artemia franciscana. J. Biol. Chem. 279: 39999-40006
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 39999-40006
-
-
Sun, Y.1
Mansour, M.2
Crack, J.A.3
Gass, G.L.4
MacRae, T.H.5
-
104
-
-
1642524277
-
Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation. the N-terminal domain is important for oligomer assembly and the binding of unfolding proteins
-
Stromer T. Fischer E., Richter K., Haslbeck M. and Buchner J. (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation. The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins. J. Biol. Chem. 279: 11222-11228
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 11222-11228
-
-
Stromer, T.1
Fischer, E.2
Richter, K.3
Haslbeck, M.4
Buchner, J.5
-
105
-
-
0344737954
-
Structural diversity in the small heat shock protein superfamily: Control of aggregation by the N-terminal region
-
Salerno J. C., Eifert C. L., Salerno K. M. and Koretz J. F. (2003) Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region. Prot. Eng. 16: 847-851
-
(2003)
Prot. Eng.
, vol.16
, pp. 847-851
-
-
Salerno, J.C.1
Eifert, C.L.2
Salerno, K.M.3
Koretz, J.F.4
-
106
-
-
0036375506
-
A critical motif for oligomerization and chaperone activity of bacterial α-heat shock proteins
-
Studer S., Obrist M., Lentre N. and Narberhaus F. (2002) A critical motif for oligomerization and chaperone activity of bacterial α-heat shock proteins. Eur. J. Biochem. 269: 3578-3586
-
(2002)
Eur. J. Biochem.
, vol.269
, pp. 3578-3586
-
-
Studer, S.1
Obrist, M.2
Lentre, N.3
Narberhaus, F.4
-
107
-
-
0037157161
-
The determinants of the oligomeric structure in Hsp16.5 are encoded in the α-crystallin domain
-
Koteiche H. A. and Mchaourab H. S. (2002) The determinants of the oligomeric structure in Hsp16.5 are encoded in the α-crystallin domain. FEBS Lett. 519: 16-22
-
(2002)
FEBS Lett.
, vol.519
, pp. 16-22
-
-
Koteiche, H.A.1
Mchaourab, H.S.2
-
108
-
-
0033972325
-
Subunit exchange of small heat shock proteins. Analysis of oligomer formation of αA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
-
Bova M. P., Mchaourab H. S., Han Y. and Fung B. K.-K. (2000) Subunit exchange of small heat shock proteins. Analysis of oligomer formation of αA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations. J. Biol. Chem. 275: 1035-1042
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 1035-1042
-
-
Bova, M.P.1
Mchaourab, H.S.2
Han, Y.3
Fung, B.K.-K.4
-
109
-
-
0033515597
-
HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus
-
Lambert H., Charette S. J., Bernier A. F., Guimond A. and Landry J. (1999) HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus. J. Biol. Chem. 274: 9378-9385
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 9378-9385
-
-
Lambert, H.1
Charette, S.J.2
Bernier, A.F.3
Guimond, A.4
Landry, J.5
-
110
-
-
0038109739
-
On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii
-
USA
-
Kim R., Lai L., Lee H.-H., Cheong G.-W., Kim K. K., Wu Z. et al. (2003) On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii. Proc. Natl. Acad. Sci. USA 100: 8151-8155
-
(2003)
Proc. Natl. Acad. Sci.
, vol.100
, pp. 8151-8155
-
-
Kim, R.1
Lai, L.2
Lee, H.-H.3
Cheong, G.-W.4
Kim, K.K.5
Wu, Z.6
-
111
-
-
0033571009
-
Molecular characterization of Oryza sativa 16.9 kDa heat shock protein
-
Young L.-S., Yeh C.-H., Chen Y.-M. and Lin C.-Y. (1999) Molecular characterization of Oryza sativa 16.9 kDa heat shock protein. Biochem. J. 344: 31-38161
-
(1999)
Biochem. J.
, vol.344
, pp. 31-38161
-
-
Young, L.-S.1
Yeh, C.-H.2
Chen, Y.-M.3
Lin, C.-Y.4
-
112
-
-
16644389981
-
Probing α-crystallin structure using chemical cross-linkers and mass spectrometry
-
Peterson J. J., Young M. M. and Takemoto L. J. (2004) Probing α-crystallin structure using chemical cross-linkers and mass spectrometry. Mol. Vis. 10: 857-866
-
(2004)
Mol. Vis.
, vol.10
, pp. 857-866
-
-
Peterson, J.J.1
Young, M.M.2
Takemoto, L.J.3
-
113
-
-
1642452930
-
Thermal stability of human α-crystallins sensed by amide hydrogen exchange
-
Hasan A., Yu J., Smith D. L. and Smith J. B. (2004) Thermal stability of human α-crystallins sensed by amide hydrogen exchange. Prot. Sci. 13: 332-341
-
(2004)
Prot. Sci.
, vol.13
, pp. 332-341
-
-
Hasan, A.1
Yu, J.2
Smith, D.L.3
Smith, J.B.4
-
114
-
-
0030826325
-
Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides
-
Leroux M. R., Melki R., Gordon B., Batelier G. and Candido E. P. M. (1997) Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides. J. Biol. Chem. 272: 24646-24656
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 24646-24656
-
-
Leroux, M.R.1
Melki, R.2
Gordon, B.3
Batelier, G.4
Candido, E.P.M.5
-
115
-
-
0027673091
-
Comparison of the homologous carboxy-terminal domain and tail of α-crystallin and small heat shock protein
-
Merck KB., Horwitz J., Kersten M., Overkamp P., Gaestel M., Bloemendal H. et al. (1993) Comparison of the homologous carboxy-terminal domain and tail of α-crystallin and small heat shock protein. Mol. Biol. Rep. 18: 209-215
-
(1993)
Mol. Biol. Rep.
, vol.18
, pp. 209-215
-
-
Merck, K.B.1
Horwitz, J.2
Kersten, M.3
Overkamp, P.4
Gaestel, M.5
Bloemendal, H.6
-
116
-
-
0026576648
-
Expression and aggregation of recombinant αA-crystallin and its two domains. Biochim
-
Merck K. B., De Haard-Hoekman W. A., Essink B. B. O., Bloemendal H. and De Jong W. W. (1992) Expression and aggregation of recombinant αA-crystallin and its two domains. Biochim. Biophys. Acta 1130: 267-276
-
(1992)
Biophys. Acta
, vol.1130
, pp. 267-276
-
-
Merck, K.B.1
De Haard-Hoekman, W.A.2
Essink, B.B.O.3
Bloemendal, H.4
De Jong, W.W.5
-
117
-
-
0035853671
-
A novel quaternary structure of the dimeric α-crystallin domain with chaperone-like activity
-
Feil I. K., Malfois M., Hendle J., van der Zandt, H. and Svergun D. I. (2001) A novel quaternary structure of the dimeric α-crystallin domain with chaperone-like activity. J. Biol. Chem. 276: 12024-12029
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 12024-12029
-
-
Feil, I.K.1
Malfois, M.2
Hendle, J.3
Van Der Zandt, H.4
Svergun, D.I.5
-
118
-
-
0038193547
-
Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in αB-crystallin
-
Koteiche H. A. and Mchaourab H. S. (2003) Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in αB-crystallin. J. Biol. Chem. 278: 10361-10367
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 10361-10367
-
-
Koteiche, H.A.1
Mchaourab, H.S.2
-
120
-
-
0346435099
-
Role of the conserved SRLFDQFFG region of α-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity
-
Pasta S. Y., Raman B., Ramakrishna T. and Rao, Ch. M. (2003) Role of the conserved SRLFDQFFG region of α-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity. J. Biol. Chem. 278: 51159-51166
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 51159-51166
-
-
Pasta, S.Y.1
Raman, B.2
Ramakrishna, T.3
Rao, Ch.M.4
-
121
-
-
0029956553
-
Effects of site-directed mutations on the chaperone-like activity of αB-crystallin
-
Plater M. L., Goode D. and Crabbe M. J. C. (1996) Effects of site-directed mutations on the chaperone-like activity of αB-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.C.3
-
122
-
-
0032582722
-
Effect of mutations of murine lens αB crystallin on transfected neural cell viability and cellular translocation in response to stress
-
Wiesmann K. E. H., Coop A., Goode D., Hepburne-Scott H. W. and Crabbe M. J. C. (1998) Effect of mutations of murine lens αB crystallin on transfected neural cell viability and cellular translocation in response to stress. FEBS Lett. 438: 25-31
-
(1998)
FEBS Lett.
, vol.438
, pp. 25-31
-
-
Wiesmann, K.E.H.1
Coop, A.2
Goode, D.3
Hepburne-Scott, H.W.4
Crabbe, M.J.C.5
-
123
-
-
0032078066
-
Mutation of αB-crystallin: Effects on chaperone-like activity
-
Horwitz J., Bova M., Huang Q.-L., Ding L., Yaron O. and Lowman S. (1998) Mutation of αB-crystallin: effects on chaperone-like activity. Int. J. Biol. Macromol. 22: 263-269
-
(1998)
Int. J. Biol. Macromol.
, vol.22
, pp. 263-269
-
-
Horwitz, J.1
Bova, M.2
Huang, Q.-L.3
Ding, L.4
Yaron, O.5
Lowman, S.6
-
124
-
-
0141839780
-
Thermally induced disintegration of the oligomeric structure of αB-crystallin mutant F28S is associated with diminished chaperone activity
-
Kelley P. B. and Abraham E. C. (2003) Thermally induced disintegration of the oligomeric structure of αB-crystallin mutant F28S is associated with diminished chaperone activity. Mol. Cell. Biochem. 252: 273-278
-
(2003)
Mol. Cell. Biochem.
, vol.252
, pp. 273-278
-
-
Kelley, P.B.1
Abraham, E.C.2
-
125
-
-
17644408766
-
Subunit exchange of polydisperse proteins. Mass spectrometry reveals consequences of αA-crystallin truncation
-
Aquilina J. A., Benesch J. L. P., Ding L. L., Yaron O., Horwitz J. and Robinson C. V. (2005) Subunit exchange of polydisperse proteins. Mass spectrometry reveals consequences of αA-crystallin truncation. J. Biol. Chem. 280: 14485-14491
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 14485-14491
-
-
Aquilina, J.A.1
Benesch, J.L.P.2
Ding, L.L.3
Yaron, O.4
Horwitz, J.5
Robinson, C.V.6
-
126
-
-
0032533361
-
Structural alterations of α-crystallin during its chaperone activity
-
Lindner R. A., Kapur A., Mariana M., Titmuss S. J. and Carver J. A. (1998) Structural alterations of α-crystallin during its chaperone activity. Eur. J. Biochem. 258: 170-183
-
(1998)
Eur. J. Biochem.
, vol.258
, pp. 170-183
-
-
Lindner, R.A.1
Kapur, A.2
Mariana, M.3
Titmuss, S.J.4
Carver, J.A.5
-
127
-
-
0029842722
-
Immobilization of the C-terminal extension of bovine αA-crystallin reduces chaperone-like activity
-
Smulders R. H. P. H., Carver J. A., Lindner R. A., van Boekel M. A. M., Bloemendal H. and de Jong W. W. (1996) Immobilization of the C-terminal extension of bovine αA-crystallin reduces chaperone-like activity. J. Biol. Chem. 271: 29060-29066
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 29060-29066
-
-
Smulders, R.H.P.H.1
Carver, J.A.2
Lindner, R.A.3
Van Boekel, M.A.M.4
Bloemendal, H.5
De Jong, W.W.6
-
128
-
-
0028984175
-
1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids
-
1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids. FEBS Lett. 369: 305-310
-
(1995)
FEBS Lett.
, vol.369
, pp. 305-310
-
-
Carver, J.A.1
Esposito, G.2
Schwedersky, G.3
Gaestel, M.4
-
129
-
-
0141988870
-
Influence of the C-terminal residues on oligomerization of αA-crystallin
-
Thampi P. and Abraham E. C. (2003) Influence of the C-terminal residues on oligomerization of αA-crystallin. Biochemistry 42: 11857-11863
-
(2003)
Biochemistry
, vol.42
, pp. 11857-11863
-
-
Thampi, P.1
Abraham, E.C.2
-
130
-
-
0027316992
-
The C-terminal region of α-crystallin: Involvement in protection against heat-induced denaturation
-
Takemoto L., Emmons T. and Horwitz I. (1993) The C-terminal region of α-crystallin: involvement in protection against heat-induced denaturation. Biochem. J. 294: 435-138
-
(1993)
Biochem. J.
, vol.294
, pp. 435-1138
-
-
Takemoto, L.1
Emmons, T.2
Horwitz, I.3
-
131
-
-
0029770039
-
Cloning, expression and chaperone-like activity of human αA-crystallin
-
Andley U. P., Mathur S., Griest T. A. and Petrash J. M. (1996) Cloning, expression and chaperone-like activity of human αA-crystallin. J. Biol. Chem. 271: 31973-31980
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 31973-31980
-
-
Andley, U.P.1
Mathur, S.2
Griest, T.A.3
Petrash, J.M.4
-
132
-
-
0034067386
-
Mouse Hsp25, a small heat shock protein: The role of its C-terminal extension in oligomerization and chaperone action
-
Lindner R.A., Carver J.A., Ehrnsperger M., Buchner J., Esposito G., Behlke J. et al. (2000) Mouse Hsp25, a small heat shock protein: the role of its C-terminal extension in oligomerization and chaperone action. Eur. J. Biochem. 267: 1923-1932
-
(2000)
Eur. J. Biochem.
, vol.267
, pp. 1923-1932
-
-
Lindner, R.A.1
Carver, J.A.2
Ehrnsperger, M.3
Buchner, J.4
Esposito, G.5
Behlke, J.6
-
133
-
-
0036402632
-
C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine αB-crystallin
-
Liao J.-H., Lee J.-S. and Chiou, S.-H. (2002) C-terminal lysine truncation increases thermostability and enhances chaperone-like function of porcine αB-crystallin. Biochem. Biophys. Res. Commun. 297: 309-316
-
(2002)
Biochem. Biophys. Res. Commun.
, vol.297
, pp. 309-316
-
-
Liao, J.-H.1
Lee, J.-S.2
Chiou, S.-H.3
-
134
-
-
3242776825
-
Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
-
Chowdary T. K., Raman B., Ramakrishna T. and Rao, C. H. (2004) Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity. Biochem. J. 381: 379-387
-
(2004)
Biochem. J.
, vol.381
, pp. 379-387
-
-
Chowdary, T.K.1
Raman, B.2
Ramakrishna, T.3
Rao, C.H.4
-
135
-
-
3543039976
-
Mutants in a small heat shock protein that affect the oligomeric state: Analysis and allele-specific suppression
-
Giese K.C. and Vierling E. (2004) Mutants in a small heat shock protein that affect the oligomeric state: Analysis and allele-specific suppression. J. Biol. Chem. 279: 32674-32683
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 32674-32683
-
-
Giese, K.C.1
Vierling, E.2
-
136
-
-
16544382615
-
The IXI/V motif in the C-terminal extension of α-crystallins: Alternative interactions and oligomeric assemblies
-
Pasta S. Y., Raman B., Ramakrishna T. and Rao Ch. M. (2004) The IXI/V motif in the C-terminal extension of α-crystallins: alternative interactions and oligomeric assemblies. Mol. Vis. 10: 655-662
-
(2004)
Mol. Vis.
, vol.10
, pp. 655-662
-
-
Pasta, S.Y.1
Raman, B.2
Ramakrishna, T.3
Rao, Ch.M.4
-
137
-
-
0036366373
-
The small heat shock proteins of the nematode Caenorhabditis elegans: Structure, regulation and biology
-
Arrigo, A.-P. and Müller, W. E. G. (eds), Springer, Berlin
-
Candido E. P. M. (2002) The small heat shock proteins of the nematode Caenorhabditis elegans: structure, regulation and biology. In. Arrigo, A.-P. and Müller, W. E. G. (eds), Small Stress Proteins, pp. 61-67. Springer, Berlin
-
(2002)
Small Stress Proteins
, pp. 61-67
-
-
Candido, E.P.M.1
-
138
-
-
0030973550
-
Unique structural features of a novel class of small heat shock proteins
-
Leroux M. R., Ma B.J., Batelier G., Melki R. and Candido E. P. M. (1997) Unique structural features of a novel class of small heat shock proteins. J. Biol. Chem. 272: 12847-12853
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 12847-12853
-
-
Leroux, M.R.1
Ma, B.J.2
Batelier, G.3
Melki, R.4
Candido, E.P.M.5
-
139
-
-
0032555364
-
Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity
-
Kokke B. P. A., Leroux M. R., Candido E. P. M., Boelens W. C. and de Jong W. W. (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.A.1
Leroux, M.R.2
Candido, E.P.M.3
Boelens, W.C.4
De Jong, W.W.5
-
140
-
-
0035195006
-
The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human αB-crystallin
-
Kokke B. P. A., Boelens W. C. and de Jong W. W. (2001) The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human αB-crystallin. Cell Stress Chaperones 6: 360-367
-
(2001)
Cell Stress Chaperones
, vol.6
, pp. 360-367
-
-
Kokke, B.P.A.1
Boelens, W.C.2
De Jong, W.W.3
-
141
-
-
0034737774
-
HSP25, a small heat shock protein associated with dense bodies and M-lines of body wall muscle in Caenorhabditis elegans
-
Ding L. and Candido E. P. M. (2000) HSP25, a small heat shock protein associated with dense bodies and M-lines of body wall muscle in Caenorhabditis elegans. I. Biol. Chem. 275: 9510-9517
-
(2000)
I. Biol. Chem.
, vol.275
, pp. 9510-9517
-
-
Ding, L.1
Candido, E.P.M.2
-
142
-
-
0033516660
-
Regulation of HSP27 oligomerization, chaperone function and protective activity against oxidative stress/tumor necrosis factor α by phosphorylation
-
Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C. et al. (1999) Regulation of HSP27 oligomerization, chaperone function and protective activity against oxidative stress/tumor necrosis factor α by phosphorylation. J. Biol. Chem. 274: 18947-18956
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 18947-18956
-
-
Rogalla, T.1
Ehrnsperger, M.2
Preville, X.3
Kotlyarov, A.4
Lutsch, G.5
Ducasse, C.6
-
143
-
-
0033591453
-
The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species
-
Ehrnsperger M., Lilie H., Gaestel M. and Buchner J. (1999) The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species. J. Biol. Chem. 274: 14867-14874
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 14867-14874
-
-
Ehrnsperger, M.1
Lilie, H.2
Gaestel, M.3
Buchner, J.4
-
144
-
-
0030002946
-
Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
-
Chang Z., Primm T. P., Jakana J., Lee I. H., Serysheva I., Chiu W. et al. (1996) Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J. Biol. Chem. 271: 7218-7223
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 7218-7223
-
-
Chang, Z.1
Primm, T.P.2
Jakana, J.3
Lee, I.H.4
Serysheva, I.5
Chiu, W.6
-
145
-
-
0033525723
-
Site-directed spin labeling study of subunit interactions in the α-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in αB-crystallin. HSP 27 and HSP 16.3
-
Berengian A. R., Parfenova M. and Mchaourab H. S. (1999) Site-directed spin labeling study of subunit interactions in the α-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in αB-crystallin. HSP 27 and HSP 16.3. J. Biol. Chem. 274: 6305-6314
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 6305-6314
-
-
Berengian, A.R.1
Parfenova, M.2
Mchaourab, H.S.3
-
146
-
-
0033573984
-
Identification of a site of Hsp27 binding with Hsp27 and αB-crystallin as indicated by the yeast two-hybrid system
-
Liu C. and Welsh M. J. (1999) 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: 256-261
-
(1999)
Biochem. Biophys. Res. Commun.
, vol.255
, pp. 256-261
-
-
Liu, C.1
Welsh, M.J.2
-
147
-
-
0032561319
-
Negative charges in the C-terminal domain stabilize the αB-crystallin complex
-
Boelens W. C., Croes Y., de Ruwe M., de Reu L. and de Jong W.W. (1998) Negative charges in the C-terminal domain stabilize the αB-crystallin complex. J. Biol. Chem. 273: 28085-28090
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 28085-28090
-
-
Boelens, W.C.1
Croes, Y.2
De Ruwe, M.3
De Reu, L.4
De Jong, W.W.5
-
148
-
-
1542788736
-
Quaternary structure of α-crystallin is necessary for the binding of unfolded proteins: A surface plasmon resonance study
-
Avilov S. V. Aleksandrova N. A. and Demchenko A. P. (2004) Quaternary structure of α-crystallin is necessary for the binding of unfolded proteins: a surface plasmon resonance study. Prot. Pept. Lett. 11: 41-48
-
(2004)
Prot. Pept. Lett.
, vol.11
, pp. 41-48
-
-
Avilov, S.V.1
Aleksandrova, N.A.2
Demchenko, A.P.3
-
149
-
-
1342345255
-
Some properties of human small heat shock protein Hsp22 (H11 or HspB8)
-
Kim M. V., Seit-Nebi A. S., Marston S. B. and Gusev N. B. (2004) Some properties of human small heat shock protein Hsp22 (H11 or HspB8). Biochem. Biophys, Res. Commun. 315: 796-801
-
(2004)
Biochem. Biophys, Res. Commun.
, vol.315
, pp. 796-801
-
-
Kim, M.V.1
Seit-Nebi, A.S.2
Marston, S.B.3
Gusev, N.B.4
-
151
-
-
4444370076
-
Tsp36, a tapeworm small heat-shock protein with a duplicated α-crystallin domain, forms dimers and tetramers with good chaperone-like activity
-
Kappé G., Aquilina J. A., Wunderink L., Kamps B., Robinson C. V., Garate T. et al. (2004). Tsp36, a tapeworm small heat-shock protein with a duplicated α-crystallin domain, forms dimers and tetramers with good chaperone-like activity. Proteins Struct. Funct. Bioinform. 57: 109-117
-
(2004)
Proteins Struct. Funct. Bioinform.
, vol.57
, pp. 109-117
-
-
Kappé, G.1
Aquilina, J.A.2
Wunderink, L.3
Kamps, B.4
Robinson, C.V.5
Garate, T.6
-
152
-
-
1542617030
-
Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis
-
Fu X. and Chang Z. (2004) Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis. Biochem. Biophys. Res. Commun. 316: 291-299
-
(2004)
Biochem. Biophys. Res. Commun.
, vol.316
, pp. 291-299
-
-
Fu, X.1
Chang, Z.2
-
153
-
-
1242339668
-
Structural changes in α-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction
-
Regini J. W., Grossmann J. G., Burgio M. R., Malik N. S., Koretz J. F., Hudson S. A. et al. (2004) Structural changes in α-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction. J. Mol. Biol. 336: 1185-1194
-
(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
Hudson, S.A.6
-
154
-
-
0037954045
-
Thermal dissociation of multimeric protein complexes by using nanoelectrospray mass spectrometry
-
Benesch J. L. P., Sobott F. and Robinson C. V. (2003) Thermal dissociation of multimeric protein complexes by using nanoelectrospray mass spectrometry. Anal. Chem. 75: 2208-2214
-
(2003)
Anal. Chem.
, vol.75
, pp. 2208-2214
-
-
Benesch, J.L.P.1
Sobott, F.2
Robinson, C.V.3
-
155
-
-
0037064096
-
Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
-
Sobott F., Benesch J. L. P., Vierling E. and Robinson C. V. (2002) Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry. J. Biol. Chem. 277: 38921-38929
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 38921-38929
-
-
Sobott, F.1
Benesch, J.L.P.2
Vierling, E.3
Robinson, C.V.4
-
156
-
-
0036306310
-
Monodisperse HSP16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity
-
Gu L., Abulimiti A., Li W. and Chang Z. (2002) Monodisperse HSP16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity. J. Mol. Biol. 319: 517-526
-
(2002)
J. Mol. Biol.
, vol.319
, pp. 517-526
-
-
Gu, L.1
Abulimiti, A.2
Li, W.3
Chang, Z.4
-
157
-
-
0037064015
-
Subunit exchange, conformational stability and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii
-
Bova M. P., Huang Q., Ding L. and Horwitz J. (2002) Subunit exchange, conformational stability and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii. J. Biol. Chem. 277: 38468-38475
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 38468-38475
-
-
Bova, M.P.1
Huang, Q.2
Ding, L.3
Horwitz, J.4
-
160
-
-
0034711315
-
Chaperone activity and homo- And hetero-oligomer formation of bacterial small heat shock proteins
-
Studer S. and Narberhaus F. (2000) Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins. J. Biol. Chem. 275: 37212-37218
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 37212-37218
-
-
Studer, S.1
Narberhaus, F.2
-
161
-
-
0037470554
-
Mycobacterium tuberculosis Hsp16.3 nonamers are assembled and re-assembled via trimer and hexamer intermediates
-
Abulimiti A., Fu X., Gu L., Feng X. and Chang Z. (2003) Mycobacterium tuberculosis Hsp16.3 nonamers are assembled and re-assembled via trimer and hexamer intermediates. J. Mol. Biol. 326: 1013-1023
-
(2003)
J. Mol. Biol.
, vol.326
, pp. 1013-1023
-
-
Abulimiti, A.1
Fu, X.2
Gu, L.3
Feng, X.4
Chang, Z.5
-
162
-
-
0141682090
-
Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation
-
Fu X., Liu C., Liu Y., Feng X., Gu L., Chen X. et al. (2003) Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation. Biochem. Biophys. Res. Commun. 310: 412-420
-
(2003)
Biochem. Biophys. Res. Commun.
, vol.310
, pp. 412-420
-
-
Fu, X.1
Liu, C.2
Liu, Y.3
Feng, X.4
Gu, L.5
Chen, X.6
-
163
-
-
0037459183
-
Enhanced stability of αB-crystallin in the presence of small heat shock protein Hsp27
-
Fu L. and Liang J. J.-N. (2003) Enhanced stability of αB-crystallin in the presence of small heat shock protein Hsp27. Biochem. Biophys. Res. Commun. 302: 710-714
-
(2003)
Biochem. Biophys. Res. Commun.
, vol.302
, pp. 710-714
-
-
Fu, L.1
Liang, J.J.-N.2
-
164
-
-
0031962334
-
Intermolecular exchange and stabilization of recombinant human αA- And αB-crystallin
-
Sun T.-X. and Liang, J. J.-N. (1998) Intermolecular exchange and stabilization of recombinant human αA- and αB-crystallin. J. Biol. Chem. 273: 286-290
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 286-290
-
-
Sun, T.-X.1
Liang, J.J.-N.2
-
165
-
-
0034681446
-
Temperature-dependent chaperone activity and structural properties of human αA- And αB-crystallins
-
Reddy G. B., Das K. P., Petrash J. M. and Surewicz W. K. (2000) Temperature-dependent chaperone activity and structural properties of human αA- and αB-crystallins. J. Biol. Chem. 275: 4565-1570
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 4565-11570
-
-
Reddy, G.B.1
Das, K.P.2
Petrash, J.M.3
Surewicz, W.K.4
-
166
-
-
0033521012
-
Differential temperature-dependent chaperone-like activity of αA- And αB-crystallin homoaggregates
-
Datta S. A. and Rao Ch. M. (1999) Differential temperature-dependent chaperone-like activity of αA- and αB-crystallin homoaggregates. J. Biol. Chem. 274: 34773-34778
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 34773-34778
-
-
Datta, S.A.1
Rao, Ch.M.2
-
167
-
-
0032078099
-
Structural perturbation of α-crystallin and its chaperone-like activity
-
Rao Ch. M., Raman B., Ramakrishna T., Rajaraman K., Ghosh D., Datta S. et al. (1998) Structural perturbation of α-crystallin and its chaperone-like activity. Int. J. Biol. Macromol. 22: 271-281
-
(1998)
Int. J. Biol. Macromol.
, vol.22
, pp. 271-281
-
-
Rao, Ch.M.1
Raman, B.2
Ramakrishna, T.3
Rajaraman, K.4
Ghosh, D.5
Datta, S.6
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