-
1
-
-
20444478694
-
The small heat shock proteins and their role in human disease
-
DOI 10.1111/j.1742-4658.2005.04708.x
-
Sun, Y., and Macrae, T. H. (2005) The small heat shock proteins and their role in human disease. FEBS J. 272, 2613-2627. (Pubitemid 40825410)
-
(2005)
FEBS Journal
, vol.272
, Issue.11
, pp. 2613-2627
-
-
Sun, Y.1
MacRae, T.H.2
-
4
-
-
0025797337
-
αB-Crystallin is a small heat-shock protein
-
Klemenz, R., Frohli, E., Steiger, R. H., Schafer, R., and Aoyama, A. (1991) αB-Crystallin is a small heat-shock protein. Proc. Natl. Acad. Sci. U.S.A. 88, 3652-3656.
-
(1991)
Proc. Natl. Acad. Sci. U.S.A.
, vol.88
, pp. 3652-3656
-
-
Klemenz, R.1
Frohli, E.2
Steiger, R.H.3
Schafer, R.4
Aoyama, A.5
-
5
-
-
0026534772
-
Hypertonic stress induces αB-crystallin expression
-
Dasgupta, S., Hohman, T. C., and Carper, D. (1992) Hypertonic stress induces αB-crystallin expression. Exp. Eye Res. 54, 461-470.
-
(1992)
Exp. Eye Res.
, vol.54
, pp. 461-470
-
-
Dasgupta, S.1
Hohman, T.C.2
Carper, D.3
-
6
-
-
0026483279
-
α-Crystallin can function as a molecular chaperone
-
Horwitz, J. (1992) α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U.S.A. 89, 10449-10453.
-
(1992)
Proc. Natl. Acad. Sci. U.S.A.
, vol.89
, pp. 10449-10453
-
-
Horwitz, J.1
-
7
-
-
0028282965
-
The chaperone activity of bovine α-crystallin. Interaction with other lens crystallins in native and denatured states
-
Wang, K., and Spector, A. (1994) The chaperone activity of bovine α-crystallin. Interaction with other lens crystallins in native and denatured states. J. Biol. Chem. 269, 13601-13608.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 13601-13608
-
-
Wang, K.1
Spector, A.2
-
8
-
-
0031577451
-
Effect of heat-induced structural perturbation of secondary and tertiary structures on the chaperone activity of α-crystallin
-
Lee, J. S., Satoh, T., Shinoda, H., Samejima, T., Wu, S. H., and Chiou, S. H. (1997) Effect of heat-induced structural perturbation of secondary and tertiary structures on the chaperone activity of α-crystallin. Biochem. Biophys. Res. Commun. 237, 277-282.
-
(1997)
Biochem. Biophys. Res. Commun.
, vol.237
, pp. 277-282
-
-
Lee, J.S.1
Satoh, T.2
Shinoda, H.3
Samejima, T.4
Wu, S.H.5
Chiou, S.H.6
-
9
-
-
0029910017
-
Molten-globule state of carbonic anhydrase binds to the chaperone-like α-crystallin
-
Rajaraman, K., Raman, B., and Rao, C. M. (1996) Molten-globule state of carbonic anhydrase binds to the chaperone-like α-crystallin. J. Biol. Chem. 271, 27595-27600.
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 27595-27600
-
-
Rajaraman, K.1
Raman, B.2
Rao, C.M.3
-
10
-
-
0037174851
-
Mechanism of chaperone function in small heat shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by αA-crystallin
-
Mchaourab, H. S., Dodson, E. K., and Koteiche, H. A. (2002) Mechanism of chaperone function in small heat shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by αA-crystallin. J. Biol. Chem. 277, 40557-40566.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 40557-40566
-
-
Mchaourab, H.S.1
Dodson, E.K.2
Koteiche, H.A.3
-
11
-
-
0032575656
-
The chaperone-like α-crystallin forms a complex only with the aggregation-prone molten globule state of α-lactalbumin
-
Rajaraman, K., Raman, B., Ramakrishna, T., and Rao, C. M. (1998) The chaperone-like α-crystallin forms a complex only with the aggregation-prone molten globule state of α-lactalbumin. Biochem. Biophys. Res. Commun. 249, 917-921.
-
(1998)
Biochem. Biophys. Res. Commun.
, vol.249
, pp. 917-921
-
-
Rajaraman, K.1
Raman, B.2
Ramakrishna, T.3
Rao, C.M.4
-
12
-
-
0027973129
-
Chaperone-like activity and quaternary structure of α-crystallin
-
Raman, B., and Rao, C. M. (1994) Chaperone-like activity and quaternary structure of α-crystallin. J. Biol. Chem. 269, 27264-27268.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 27264-27268
-
-
Raman, B.1
Rao, C.M.2
-
13
-
-
0029124685
-
Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin
-
Das, K. P., and Surewicz, W. K. (1995) Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin. FEBS Lett. 369, 321-325.
-
(1995)
FEBS Lett.
, vol.369
, pp. 321-325
-
-
Das, K.P.1
Surewicz, W.K.2
-
14
-
-
0030590541
-
The conformational stability of α-crystallin is rather low: Calorimetric results
-
DOI 10.1016/0014-5793(96)00867-8
-
Gesierich, U., and Pfeil, W. (1996) The conformational stability of α-crystallin is rather low: Calorimetric results. FEBS Lett. 393, 151-154. (Pubitemid 26298086)
-
(1996)
FEBS Letters
, vol.393
, Issue.2-3
, pp. 151-154
-
-
Gesierich, U.1
Pfeil, W.2
-
15
-
-
0028984242
-
On the thermal-stability of α-crystallin: A new insight from infrared-spectroscopy
-
Surewicz, W. K., and Olesen, P. R. (1995) On the thermal-stability of α-crystallin: A new insight from infrared-spectroscopy. Biochemistry 34, 9655-9660.
-
(1995)
Biochemistry
, vol.34
, pp. 9655-9660
-
-
Surewicz, W.K.1
Olesen, P.R.2
-
16
-
-
0030798628
-
Chaperone-like activity and temperature structural changes of α-crystallin
-
Raman, B., and Rao, C. M. (1997) Chaperone-like activity and temperature structural changes of α-crystallin. J. Biol. Chem. 272, 23559-23564.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 23559-23564
-
-
Raman, B.1
Rao, C.M.2
-
17
-
-
0032078099
-
Structural perturbation of α-crystallin and its chaperone-like activity
-
Rao, C. M., Raman, B., Ramakrishna, T., Rajaraman, K., Ghosh, D., Datta, S., Trivedi, V. D., and Sukhaswami, M. B. (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, C.M.1
Raman, B.2
Ramakrishna, T.3
Rajaraman, K.4
Ghosh, D.5
Datta, S.6
Trivedi, V.D.7
Sukhaswami, M.B.8
-
18
-
-
33750631597
-
Chaperone-like activity and hydrophobicity of α-crystallin
-
Reddy, G. B., Kumar, P. A., and Kumar, M. S. (2006) Chaperone-like activity and hydrophobicity of α-crystallin. IUBMB Life 58, 632-641.
-
(2006)
IUBMB Life
, vol.58
, pp. 632-641
-
-
Reddy, G.B.1
Kumar, P.A.2
Kumar, M.S.3
-
19
-
-
33846298505
-
Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
-
Khanova, H. A., Markossian, K. A., Kleimenov, S. Y., Levitsky, D. I., Chebotareva, N. A., Golub, N. V., Asryants, R. A., Muronetz, V. I., Saso, L., Yudin, I. K., Muranov, K. O., Ostrovsky, M. A., and Kurganov, B. I. (2007) Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. Biophys. Chem. 125, 521-531.
-
(2007)
Biophys. Chem.
, vol.125
, pp. 521-531
-
-
Khanova, H.A.1
Markossian, K.A.2
Kleimenov, S.Y.3
Levitsky, D.I.4
Chebotareva, N.A.5
Golub, N.V.6
Asryants, R.A.7
Muronetz, V.I.8
Saso, L.9
Yudin, I.K.10
Muranov, K.O.11
Ostrovsky, M.A.12
Kurganov, B.I.13
-
20
-
-
0026059486
-
The self-association of zinc-free human insulin and insulin analog B13-glutamine
-
Hansen, J. F. (1991) The self-association of zinc-free human insulin and insulin analog B13-glutamine. Biophys. Chem. 39, 107-110.
-
(1991)
Biophys. Chem.
, vol.39
, pp. 107-110
-
-
Hansen, J.F.1
-
21
-
-
0027863980
-
Insulin structure and stability
-
Brange, J., and Langkjoer, L. (1993) Insulin structure and stability. Pharm. Biotechnol. 5, 315-350.
-
(1993)
Pharm. Biotechnol.
, vol.5
, pp. 315-350
-
-
Brange, J.1
Langkjoer, L.2
-
22
-
-
0024280106
-
The structure of 2Zn pig insulin crystals at 1.5-Å resolution
-
Baker, E. N., Blundell, T. L., Cutfield, J. F., Cutfield, S. M., Dodson, E. J., Dodson, G. G., Hodgkin, D. M. C., Hubbard, R. E., Isaacs, N. W., Reynolds, C. D., Sakabe, K., Sakabe, N., and Vijayan, N. M. (1988) The structure of 2Zn pig insulin crystals at 1.5-Å resolution. Philos. Trans. R. Soc. London, Ser. B 319, 369-456.
-
(1988)
Philos. Trans. R. Soc. London, Ser. B
, vol.319
, pp. 369-456
-
-
Baker, E.N.1
Blundell, T.L.2
Cutfield, J.F.3
Cutfield, S.M.4
Dodson, E.J.5
Dodson, G.G.6
Hodgkin, D.M.C.7
Hubbard, R.E.8
Isaacs, N.W.9
Reynolds, C.D.10
Sakabe, K.11
Sakabe, N.12
Vijayan, N.M.13
-
23
-
-
23944504732
-
Thermal dissociation and unfolding of insulin
-
Huus, K., Havelund, S., Olsen, H. B., van de Weert, M., and Frokjaer, S. (2005) Thermal dissociation and unfolding of insulin. Biochemistry 44, 11171-11177.
-
(2005)
Biochemistry
, vol.44
, pp. 11171-11177
-
-
Huus, K.1
Havelund, S.2
Olsen, H.B.3
Van De Weert, M.4
Frokjaer, S.5
-
24
-
-
2442468092
-
Stimulation of insulin fibrillation by urea-induced intermediates
-
Ahmad, A., Millett, I. S., Doniach, S., Uversky, V. N., and Fink, A. L. (2004) Stimulation of insulin fibrillation by urea-induced intermediates. J. Biol. Chem. 279, 14999-15013.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 14999-15013
-
-
Ahmad, A.1
Millett, I.S.2
Doniach, S.3
Uversky, V.N.4
Fink, A.L.5
-
25
-
-
0141483330
-
Partially folded intermediates in insulin fibrillation
-
DOI 10.1021/bi034868o
-
Ahmad, A., Millett, I. S., Doniach, S., Uversky, V. N., and Fink, A. L. (2003) Partially folded intermediates in insulin fibrillation. Biochemistry 42, 11404-11416. (Pubitemid 37205734)
-
(2003)
Biochemistry
, vol.42
, Issue.39
, pp. 11404-11416
-
-
Ahmad, A.1
Millett, I.S.2
Doniach, S.3
Uversky, V.N.4
Fink, A.L.5
-
26
-
-
0035902492
-
Probing the mechanism of insulin fibril formation with insulin mutants
-
DOI 10.1021/bi0105983
-
Nielsen, L., Frokjaer, S., Brange, J., Uversky, V. N., and Fink, A. L. (2001) Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 40, 8397-8409. (Pubitemid 32661900)
-
(2001)
Biochemistry
, vol.40
, Issue.28
, pp. 8397-8409
-
-
Nielsen, L.1
Frokjaer, S.2
Brange, J.3
Uversky, V.N.4
Fink, A.L.5
-
27
-
-
0028871804
-
How to measure and predict the molar absorption coefficient of a protein
-
Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
-
(1995)
Protein Sci.
, vol.4
, pp. 2411-2423
-
-
Pace, C.N.1
Vajdos, F.2
Fee, L.3
Grimsley, G.4
Gray, T.5
-
28
-
-
0031214756
-
A new ultrasensitive scanning calorimeter
-
Plotnikov, V. V., Brandts, J. M., Lin, L. N., and Brandts, J. F. (1997)A new ultrasensitive scanning calorimeter. Anal. Biochem. 250, 237-244.
-
(1997)
Anal. Biochem.
, vol.250
, pp. 237-244
-
-
Plotnikov, V.V.1
Brandts, J.M.2
Lin, L.N.3
Brandts, J.F.4
-
29
-
-
0002343673
-
Measuring the conformational stability of a protein
-
(Creighton, T. E., Ed.) IRL Press Ltd., Oxford, U.K.
-
Pace, C. N., Shirley, B. A., and Thomson, J. A. (1989) Measuring the conformational stability of a protein. In Protein Structure: A practical approach (Creighton, T. E., Ed.) pp 311-330, IRL Press Ltd., Oxford, U.K.
-
(1989)
Protein Structure: a Practical Approach
, pp. 311-330
-
-
Pace, C.N.1
Shirley, B.A.2
Thomson, J.A.3
-
30
-
-
0017101409
-
Near-ultraviolet tyrosyl circular-dichroism of pig insulin monomers, dimers, and hexamers: Dipole-dipole coupling calculations in monopole approximation
-
Strickland, E. H., and Mercola, D. (1976) Near-ultraviolet tyrosyl circular-dichroism of pig insulin monomers, dimers, and hexamers: Dipole-dipole coupling calculations in monopole approximation. Biochemistry 15, 3875-3884.
-
(1976)
Biochemistry
, vol.15
, pp. 3875-3884
-
-
Strickland, E.H.1
Mercola, D.2
-
32
-
-
0035718677
-
Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones
-
Van, M. R., Slingsby, C., and Vierling, E. (2001) Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones. Adv. Protein Chem. 59, 105-156.
-
(2001)
Adv. Protein Chem.
, vol.59
, pp. 105-156
-
-
Van, M.R.1
Slingsby, C.2
Vierling, E.3
-
33
-
-
0029000171
-
Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of P53 tumor-suppressor
-
Johnson, C. R., Morin, P. E., Arrowsmith, C. H., and Freire, E. (1995) Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of P53 tumor-suppressor. Biochemistry 34, 5309-5316.
-
(1995)
Biochemistry
, vol.34
, pp. 5309-5316
-
-
Johnson, C.R.1
Morin, P.E.2
Arrowsmith, C.H.3
Freire, E.4
-
34
-
-
2442453433
-
Effects of divalent metal ions on the αβ-crystallin chaperone-like activity: Spectroscopic evidence for a complex between copper(II) and protein
-
Ganadu, M. L., Aru, M., Mura, G. M., Coi, A., Mlynarz, P., and Kozlowski, H. (2004) Effects of divalent metal ions on the αβ-crystallin chaperone-like activity: Spectroscopic evidence for a complex between copper(II) and protein. J. Inorg. Biochem. 98, 1103-1109.
-
(2004)
J. Inorg. Biochem.
, vol.98
, pp. 1103-1109
-
-
Ganadu, M.L.1
Aru, M.2
Mura, G.M.3
Coi, A.4
Mlynarz, P.5
Kozlowski, H.6
-
35
-
-
38849139632
-
2+ enhances the molecular chaperone function and stability of α-crystallin
-
DOI 10.1021/bi7011965
-
Biswas, A., and Das, K. P. (2008) Zn2+ enhances the molecular chaperone function and stability of α-crystallin. Biochemistry 47, 804-816. (Pubitemid 351195452)
-
(2008)
Biochemistry
, vol.47
, Issue.2
, pp. 804-816
-
-
Biswas, A.1
Das, K.P.2
-
36
-
-
0015250472
-
Differences in Nature of Interaction of Insulin and Proinsulin with Zinc
-
Grant, P. T., Frank, B. H., and Coombs, T. L. (1972) Differences in Nature of Interaction of Insulin and Proinsulin with Zinc. Biochem. J. 126, 433-440.
-
(1972)
Biochem. J.
, vol.126
, pp. 433-440
-
-
Grant, P.T.1
Frank, B.H.2
Coombs, T.L.3
-
37
-
-
0016167531
-
Zinc binding, circular dichroism, and equilibrium sedimentation studies on insulin (bovine) and several of its derivatives
-
Goldman, J., and Carpenter, F. H. (1974) Zinc binding, circular dichroism, and equilibrium sedimentation studies on insulin (bovine) and several of its derivatives. Biochemistry 13, 4566-4574.
-
(1974)
Biochemistry
, vol.13
, pp. 4566-4574
-
-
Goldman, J.1
Carpenter, F.H.2
-
38
-
-
0028972769
-
On the Interaction of α-crystallin with unfolded proteins
-
Carver, J. A., Guerreiro, N., Nicholls, K. A., and Truscott, R. J. W. (1995) On the Interaction of α-crystallin with unfolded proteins. Biochim. Biophys. Acta 1252, 251-260.
-
(1995)
Biochim. Biophys. Acta
, vol.1252
, pp. 251-260
-
-
Carver, J.A.1
Guerreiro, N.2
Nicholls, K.A.3
Truscott, R.J.W.4
-
39
-
-
0015239642
-
Atomic positions in rhombohedral 2-zinc insulin crystals
-
Blundell, T. L., Cutfield, J. F., Cutfield, S. M., Dodson, E. J., Dodson, G. G., Hodgkin, D. C., Mercola, D. A., and Vijayan, M. (1971) Atomic positions in rhombohedral 2-zinc insulin crystals. Nature 231, 506-511.
-
(1971)
Nature
, vol.231
, pp. 506-511
-
-
Blundell, T.L.1
Cutfield, J.F.2
Cutfield, S.M.3
Dodson, E.J.4
Dodson, G.G.5
Hodgkin, D.C.6
Mercola, D.A.7
Vijayan, M.8
-
40
-
-
0019860250
-
Self-association of insulin and the role of hydrophobic bonding: A thermodynamic model of insulin dimerization
-
DOI 10.1021/bi00518a019
-
Pocker, Y., and Biswas, S. B. (1981) Self-association of insulin and the role of hydrophobic bonding: A thermodynamic model of insulin dimerization. Biochemistry 20, 4354-4361. (Pubitemid 11013592)
-
(1981)
Biochemistry
, vol.20
, Issue.15
, pp. 4354-4361
-
-
Pocker, Y.1
Biswas, S.B.2
-
41
-
-
0024583245
-
Thermodynamic problems of protein structure
-
Privalov, P. L. (1989) Thermodynamic problems of protein structure. Annu. Rev. Biophys. Biophys. Chem. 18, 47-69.
-
(1989)
Annu. Rev. Biophys. Biophys. Chem.
, vol.18
, pp. 47-69
-
-
Privalov, P.L.1
-
42
-
-
0029783312
-
Energetics of cyclodextrin-induced dissociation of insulin
-
Lovatt, A., Cooper, A., and Camilleri, P. (1996) Energetics of cyclodextrin-induced dissociation of insulin. Eur. Biophys. J. 24, 354-357.
-
(1996)
Eur. Biophys. J.
, vol.24
, pp. 354-357
-
-
Lovatt, A.1
Cooper, A.2
Camilleri, P.3
-
43
-
-
1442359491
-
Structural background of cyclodextrin-protein interactions
-
Aachmann, F. L., Otzen, D. E., Larsen, K. L., and Wimmer, R. (2003) Structural background of cyclodextrin-protein interactions. Protein Eng. 16, 905-912.
-
(2003)
Protein Eng.
, vol.16
, pp. 905-912
-
-
Aachmann, F.L.1
Otzen, D.E.2
Larsen, K.L.3
Wimmer, R.4
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