Protein aggregation: Folding aggregates, inclusion bodies and amyloid

Folding and Design

Volumn 3, Issue 1, 1998, Pages

  Fink, Anthony L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID;

CELL INCLUSION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; REVIEW;

EID: 0031932169     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(98)00002-9     Document Type: Article

References (159)

1. Sipe, J.D. (1992). Amyloidosis. Annu. Rev. Biochem. 61, 947-975.
2. Carrell, R.W. & Lomas, D.A. (1997). Conformational disease. Lancet 350, 134-138.
3. Silow, M. & Oliveberg, M. (1997). Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc. Natl Acad. Sci. USA 94, 6084-6086.
4. Mitraki, A. & King, J. (1989). Protein folding intermediates and inclusion body formation. Biotechnology (N.Y.) 7, 690-697.
5. Schein, C.H. (1990). Solubility as a function of protein structure and solvent components Biotechnology (N.Y.) 8, 308-315.
6. Wetzel, R. (1992). Protein aggregation in vivo: bacterial inclusion bodies and mammalian amyloid. In Stability of Protein Pharmaceuticals, Part B; In Vivo Pathways of Degradation and Strategies for Protein Stabilization. Vol. 3 (Ahern, T.J. and Manning, M.C., eds), pp. 43-88, Plenum Press, New York.
7. Deyoung, L.R., Fink, A.L. & Dill, K.A. (1993). Aggregation of globular proteins Acc. Chem. Res. 26, 614-620.
8. Wetzel, R. (1994). Mutations and off-pathway aggregation of proteins. Trends Biotechnol. 12, 193-198.
9. Jaenicke, R. (1995). Folding and association versus misfolding and aggregation of proteins. Phil. Trans. R. Soc. Lond. B 348, 97-105.
10. Wetzel, R. (1996). For protein misassembly, it's the "I" decade. Cell 86, 699-702.
11. Eliezer, D., Chiba, K., Tsuruta, H., Doniach, S., Hodgson, K.O. & Kihara, H. (1993). Evidence of an associative intermediate on the myoglobin refolding pathway. Biophys. J. 65, 912-917.
12. Eliezer, D., Jennings, P.A., Wright, P.E., Doniach, S., Hodgson, K.O. & Tsuruta, H. (1995). The radius of gyration of an apomyoglobin folding intermediate. Science 270, 487-488.
13. Semisotnov, G.V., et al., & Kuwajima, K. (1996). Protein globularization during folding - a study by synchrotron small-angle X-ray scattering J. Mol. Biol. 262, 559-574.
14. Thomas, P.J., Qu, B.H. & Pedersen, P.L. (1995). Defective protein folding as a basis of human disease. Trends Biochem. Sci. 20, 456-459.
15. Scherzinger, E., et al., & Wanker, E.E. (1997). Huntingtin-encoded polyglutamine expansions form amyloid-like protein Cell 90, 549-558.
16. Stempfer, G. & Rudolph R. (1996). Improved refolding of a matrix-bound fusion protein. Ann. N.Y. Acad. Sci. 782, 506-512.
17. Townsend, M.W. & DeLuca, P.P. (1990). Stability of ribonuclease X in solution and the freeze-dried state. J. Pharm. Sci. 79, 1083-1086.
18. Dong, A.C., Prestrelski, S.J., Allison, S.D. & Carpenter, J.F. (1995). Infrared spectroscopic studies of lyophilization - and temperature induced protein aggregation J. Pharm. Sci. 84, 415-424.
19. Costantino, H.R., Schwendeman, S.P., Griebenow, K., Klibanov, A.M. & Langer, R. (1996). The secondary structure and aggregation of lyophilized tetanus toxoid. J. Pharm. Sci. 85, 1290-1293.
20. Chan, H.K., Ongpipattanakul, B. & Auyeung, J. (1996). Aggregation of rhodanese occurred during the compression of KBr pellets used for FTIR spectroscopy. Pharm. Res. 13, 238-242.
21. Jordan, G.M., Yoshioka, S. & Terao, T. (1994). The aggregation of bovine serum albumin in solution and in the solid state. J Pharm. Pharmacol. 46, 182-185.
22. Prestrelski, S.J., Pikal, K.A. & Arakawa, T. (1995). Optimization of lyophilization conditions for recombinant human interleukin-2 by dried-state conformational analysis using fourier-transform infrared spectroscopy. Pharm. Res. 12, 1250-1259.
23. Prestrelski, S.J., Tedeschi, N., Arakawa, T. & Carpenter, J.F. (1993). Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys. J. 65, 661-671.
24. Costantino, H.R., Griebenow, K., Mishra, P., Langer, R. & Klibanov, A.M. (1995). Fourier-transform infrared spectroscopic investigation of protein stability in the lyophilized form. Biochim. Biophys. Acta 1253, 69-74.
25. London, J., Skrzynia, C. & Goldberg, M.E. (1974). Renaturation of Escherichla coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers. Eur. J. Biochem. 47, 409-415.
26. King, J., Haase-Pettingell, C., Robinson, A.S., Speed, M. & Mitraki, A. (1996). Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates FASEB J. 10, 57-66.
27. Speed, M.A., Wang, D.I. & King, J. (1995). Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains. Protein Sci. 4, 900-908.
28. Wetzel, R. (1992). Principles of protein stability. Part 2. Enhanced folding and stabilization of proteins by suppression of aggregation in vitro and in vivo. In Protein Engineering. A Practical Approach (Rees, A.R. and Sternberg, M.J., eds) pp. 191 -219, IRL Press at Oxford University Press, Oxford.
29. Hurle, M.R., Helms, L.R., Li, L., Chan, W. & Wetzel, R. (1994). A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl Acad. Sci. USA 91, 5446-5450.
30. Oberg, K., Chrunyk, B.A., Wetzel, R. & Fink, A.L. (1994). Nativelike secondary structure in interleukin-1-beta inclusion bodies by attenuated total reflectance FT-IR. Biochemistry 33, 2628-2634.
31. Kim, D. & Yu, M.H. (1996). Folding pathway of human alpha 1-antitrypsin: characterization of an intermediate that is active but prone to aggregation. Biochem. Biophys. Res. Commun. 226, 378-384.
32. Fink, A.L. (1995). Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24, 495-522.
33. Bennett, M.J., Choe, S. & Eisenberg, D. (1994). Domain swapping: entangling alliances between proteins. Proc. Natl Acad. Sci. USA 91, 3127-3131.
34. Deyoung, L.R., Dill, K.A. & Fink, A.L. (1993). Aggregation and denaturation of apomyoglobin in aqueous urea solutions Biochemistry 32, 3877-3886.
35. Tennent, G.A., Lovat, L.B. & Pepys, M.B. (1995). Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc. Natl Acad. Sci. USA 92, 4299-4303.
36. Havel, H.A., Kauffman, E.W., Plaisted, S.M. & Brems, D.N. (1986). Reversible self-association of bovine growth hormone during equilibrium unfolding. Biochemistry 25, 6533-6538.
37. Brems, D.N., Plaisted, S.M., Dougherty, J.J., Jr & Holzman, T.F. (1987). The kinetics of bovine growth hormone folding are consistent with a framework model. J. Biol. Chem. 262, 2590-2596.
38. Brems, D.N. & Havel, H.A. (1989). Folding of bovine growth hormone is consistent with the molten globule hypothesis. Proteins 5, 93-95.
39. Brems, D.N., Brown, P.L. & Becker, G.W. (1990). Equilibrium denaturation of human growth hormone and its cysteine-modified forms. J. Biol. Chem. 265, 5504-5511.
40. Defelippis, M.R., Alter, L.A., Pekar, A.H., Havel, H.A. & Brems, D.N. (1993). Evidence for a self-associating equilibrium intermediate during folding of human growth hormone. Biochemistry 32, 1555-1562.
41. Rinas, U. & Bailey, J.E. (1992). Protein compositional analysis of inclusion bodies produced in recombinant Escherichia coli. Appl. Microbiol. Biotechnol. 37, 609-614.
42. Chrunyk, B.A., Evans, J., Lillquist, J., Young, P. & Wetzel, R. (1993). Inclusion body formation and protein stability in sequence variants of interleukin-1β J. Biol. Chem. 268, 18053-18061.
43. Teschke, C.M. & King, J. (1993). Folding of the phage P22 coat protein in vitro. Biochemistry 32, 10839-10847.
44. Georgiou, G., Valax, P., Ostermeier, M. & Horowitz P.M. (1994). Folding and aggregation of TEM β-lactamase: analogies with the formation of inclusion bodies in Escherichia coli. Protein Sci. 3, 1953-1960.
45. Georgiou, G., Telford, J.N., Shuler, M.L. & Wilson, D.B. (1986). Localization of inclusion bodies in Escherichia coli overproducing beta-lactamase or alkaline phosphatase. Appl. Environ. Microbiol. 52, 1157-1161.
46. Bowden, G.A. & Georgiou, G. (1990). Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli. J. Biol. Chem. 265, 16760-16766
47. Wilkinson, D.L. & Harrison, R.G. (1991). Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology (N.Y.) 9, 443-448.
48. Hlodan, R., Craig, S. & Pain, R.H. (1991). Protein folding and its implications for the production of recombinant proteins. Biotechnol. Genet. Eng. Rev. 9, 47-88.
49. Hart, R.A., Rinas, U. & Bailey, J.E. (1990). Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli. J. Biol. Chem. 265, 12728-12733.
50. Bowden, G.A., Paredes, A.M. & Georgiou, G. (1991). Structure and morphology of protein inclusion bodies in Escherichia coli. Biotechnology (N.Y.) 9, 725-730.
51. Haase-Pettingell, C.A. & King, J. (1988). Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation. J. Biol. Chem. 263, 4977-4983.
52. Mitraki, A., Fane, B., Haasepettingell, C., Sturtevant, J. & King, J. (1991). Global suppression of protein folding defects and inclusion body formation. Science 253, 54-58.
53. Mitraki, A. & King, J. (1992). Amino acid substitutions influencing intracellular protein folding pathways . FEBS Lett. 307, 20-25.
54. Speed, M.A., Wang, D.I.C. & King, J. (1996). Specific aggregation of partially folded polypeptide chains - the molecular basis of inclusion body composition Nat. Biotechnol. 14, 1283-1287.
55. Speed, MA, Morshead, T., Wang, D.I.C. & King, J. (1997). Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Protein Sci. 6, 99-108.
56. Wetzel, R., Perry, L.J. & Veilleux, C. (1991). Mutations in human Interferon gamma affecting inclusion body formation identified by a general immunochemical screen. Biotechnology (N.Y.) 9, 731-737.
57. Izard, J., Parker, M.W., Chartier, M., Duche, D. & Baty, D. (1994). A single amino acid substitution can restore the solubility of aggregated colicin A mutants in Escherichia coli. Protein Eng. 7, 1495-1500.
58. Krueger, J.K., Stock, J. & Schutt, C.E. (1992). Evidence that the methylesterase of bacterial chemotaxis may be a serine hydrolase. Biochim. Biophys. Acta 1119, 322-326.
59. Wetzel, R. & Chrunyk, B.A. (1994). Inclusion body formation by interleukin-1β depends on the thermal sensitivity of a folding intermediate. FEBS Lett. 350, 245-248.
60. Chrunyk, B.A. & Wetzel, R. (1993). Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1 beta point mutant modified in a surface loop. Protein Eng. 6, 733-738.
61. Nieba, L., Honegger, A., Krebber, C. & Pluckthun, A. (1997). Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng. 10, 435-444.
62. Przybycien, T.M., Dunn, J.P., Valax, P. & Georgiou, G. (1994). Secondary structure characterization of beta-lactamase inclusion bodies. Protein Eng. 7, 131-136.
63. Hawkins, P.N., Wootton, R. & Pepys, M.B. (1990). Metabolic studies of radioiodinated serum amyloid P component in normal subjects and patients with systemic amyloidosis. J. Clin. Invest. 86, 1862-1869.
64. Kisilevsky, R. & Fraser, P. (1996). Proteoglycans and amyloid fibrillogenesis. Ciba Found. Symp. 199, 58-67.
65. Wisniewski, T. & Frangione, B. (1992). Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci. Lett. 135, 235-238.
66. Hamazaki, H. (1995). Amyloid P component promotes aggregation of Alzheimer's β-amyloid peptide. Biochem. Biophys. Res. Commun. 211, 349-353.
67. Kisilevsky, R., Lemieux, L.J., Fraser, P.E., Kong, X., Hultin, P.G. & Szarek, W.A. (1995). Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nat. Med. 1, 143-148.
68. Colon, W. & Kelly, J.W. (1992). Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31, 8654-8660.
69. Lai, Z., Colon, W. & Kelly, J.W. (1996). The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 35, 6470-6482.
70. Booth, D.R., et al., & Pepys, M.B. (1997). Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385, 787-793.
71. Colon, W., Lai, Z., McCutchen, S.L., Miroy, G.J., Strang, C. & Kelly, J.W. (1996). FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation. Ciba Found. Symp. 199, 228-238.
72. Kelly, J.W. (1996). Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6, 11-17.
73. Helms, L.R. & Wetzel, R. (1996). Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis. J. Mol. Biol. 257, 77-86.
74. Jarrett, J.T., Berger, E.P. & Lansbury, P.T., Jr (1993). The C-terminus of the beta protein is critical in amyloidogenesis. Ann. N.Y. Acad. Sci. 695, 144-148.
75. Inouye, H. & Kirschner, D.A. (1997). X-ray diffraction analysis of scrapie prion: intermediate and folded structures in a peptide containing two putative alpha-helices. J. Mol. Biol. 268, 375-389.
76. Kelly, J.W. (1997). Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases. Structure 5, 595-600.
77. Nguyen, J., Baldwin, M.A., Cohen, F.E. & Prusiner, S.B. (1995). Prion protein peptides induce alpha-helix to beta-sheet conformational transitions. Biochemistry 34, 4186-4192.
78. Safar, J., Roller P.P., Gajdusek D.C. & Gibbs C.J., Jr (1994). Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry 33, 8375-8383.
79. Myatt, E.A., Westholm, F.A., Weiss, D.T., Solomon, A., Schiffer, M. & Stevens, F.J. (1994). Pathogenic potential of human monoclonal immunoglobulin light chains: relationship of in vitro aggregation to in vivo organ deposition. Proc. Natl Acad. Sci. USA 91, 3034-3038.
80. Wood, S.J., Maleeff, B., Hart, T. & Wetzel, R. (1996). Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide. J. Mol. Biol. 256, 870-877.
81. Lansbury, P.T., Jr., et al., & Griffen, R.G. (1995). Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat. Struct. Biol. 2, 990-998.
82. Inouye, H., Fraser, P.E. & Kirschner, D.A. (1993). Structure of betacrystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by X-ray diffraction. Biophys. J. 64, 502-519.
83. Blake, C. & Serpell, L. (1996). Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure 4, 989-998.
84. Serpell, L.C., et al., & Blake, C.C. (1995). Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J. Mol. Biol. 254, 113-118.
85. Lazo, N.D. & Downing, D.T. (1997). β-Helical fibrils from a model peptide. Biochem. Biophys. Res. Commun. 235, 675-679.
86. Inouye, H. & Kirschner, D.A. (1996). Refined fibril structures: the hydrophobia core in Alzheimer's amyloid beta-protein and prion as revealed by X-ray diffraction. Ciba Found. Symp. 199, 22-35.
87. Harper, J.D., Wong, S.S., Lieber, C.M. & Lansbury, P.T. (1997). Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125.
88. Glenner, G.G., Ein, D., Eanes, E.D., Bladen, H.A., Terry, W. & Page, D.L. (1971). Creation of "amyloid" fibrils from Bence Jones proteins in vitro. Science 174, 712-714.
89. Linke, R.P., Tischendorf, F.W., Zucker-Franklin, D. & Franklin, E.C. (1973). The formation of amyloid-like fibrils in vitro from Bence Jones proteins of the V λ I subclass. J. Immunol. 111, 24-26.
90. Harrison, P.M., Bamborough, P., Daggett, V., Prusiner, S.B. & Cohen, F.E. (1997). The prion folding problem. Curr. Opin. Struct. Biol. 7, 53-59.
91. Lansbury, P.T. & Caughey, B. (1996). The double life of the prion protein. Curr. Opin. Struct Biol. 6, 914-916.
92. Patino, M.M., Liu, J.J., Glover, J.R. & Lindquist, S. (1996). Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273, 622-626.
93. Cohen, F.E., Pan, K.M., Huang, Z., Baldwin, M., Retterick, R.J. & Prusiner, S.B. (1994). Structural clues to prion replication. Science 264, 530-531.
94. Cleland, J.L. & Wang, D.I.C. (1990). Refolding and aggregation of bovine carbonic anhydrase-B - quasi-elastic light scattering analysis. Biochemistry 29, 11072-11078.
95. Cleland, J.L. & Wang, D.I.C. (1992). Transient association of the first intermediate during the refolding of bovine carbonic anhydrase B. Biotechnol. Prog. 8, 97-103.
96. Mendoza, J.A, Rogers, E., Lorimer, G.H. & Horowitz, P.M. (1991). Unassisted refolding of urea unfolded rhodanese J. Biol. Chem. 266, 13587-13591.
97. Goldberg, M.E., Rudolph, R. & Jaenicke, R. (1991). A kinetic study of the competition between renaturation and aggregation during the refolding of denatured reduced egg white lysozyme. Biochemistry 30, 2790-2797.
98. Raman, B., Ramakrishna, T. & Rao, C.M. (1996). Refolding of denatured and denatured/reduced lysozyme at high concentrations. J. Biol. Chem. 271, 17067-17072.
99. Fischer, B., Sumner, I. & Goodenough, P. (1993). Renaturation of lysozyme - temperature dependence of renaturation rate, renaturation yield, and aggregation - identification of hydrophobic folding intermediates. Arch. Biochem. Biophys. 306, 183-187.
100. Clark, A.H., Saunderson, D.H. & Suggett, A. (1981). Infrared and laser-raman spectroscopic studies of thermally-induced globular protein gels. Int. J. Pept. Protein Res. 17, 353-364.
101. Ismail, A.A., Mantsch, H.H. & Wong, P.T.T. (1992). Aggregation of chymotrypsinogen - portrait by infrared spectroscopy. Biochim. Biophys. Acta 1121, 183-188.
102. Kato, A. & Takagi, T. (1988). Formation of intermolecular β-sheet structure during heat denaturation of ovalbumin. J. Agric. Food Chem. 36, 1156-1159.
103. Fink, A.L., Oberg, K.A. & Seshadri, S. (1997). Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin Fold Des. 3, 19-25.
104. Parker, T.G. & Dalgleish, D.G. (1977). The use of light-scattering and turbidity measurements to study the kinetics of extensively aggregating proteins: alpha-casein. Biopolymers 16, 2533-2547.
105. Shen, C.L., Scott, G.L., Merchant, F. & Murphy, R.M. (1993). Light scattering analysis of fibril growth from the amino-terminal fragment beta(1-28) of beta-amyloid peptide. Biophys. J. 65, 2383-2395.
106. Eigen, M. (1996). Prionics or the kinetic basis of prion diseases. Biophys. Chem. 63, A1-A18.
107. Tomski, S.J. & Murphy, R.M. (1992). Kinetics of aggregation of synthetic beta-amyloid peptide. Arch. Biochem. Biophys. 294, 630-638.
108. Harper, J.D. & Lansbury, P.T., Jr (1997). Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66, 385-407.
109. Kiefhaber, T., Rudolph, R., Kohler, H.H. & Buchner, J. (1991). Protein aggregation in vitro and in vivo - a quantitative model of the kinetic competition between folding and aggregation. Biotechnology (N.Y.) 9, 825-829.
110. Patro, S.Y. & Przybycien, T.M. (1994). Simulations of kinetically irreversible protein aggregate structure. Biophys. J. 66, 1274-1289.
111. Lomakin, A., Teplow, D.B., Kirschner, D.A. & Benedek, G.B. (1997). Kinetic theory of fibrillogenesis of amyloid beta-protein. Proc. Natl Acad. Sci. USA 94, 7942-7947.
112. Jarrett, J.T. & Lansbury, P.T., Jr (1992). Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry 31, 12345-12352.
113. Roefs, S.P. & De Kruif, K.G. (1994). A model for the denaturation and aggregation of β-lactoglobulin. Eur. J. Biochem. 226, 883-889.
114. Shen, C.L. & Murphy, R.M. (1995). Solvent effects on self-assembly of beta-amyloid peptide. Biophys. J. 69, 640-651.
115. Vitek, M.P. (1996). Radical changes in β-amyloid form and function. Mol. Chem. Neuropathol. 28, 49-55.
116. Naiki, H. & Nakakuki, K. (1996). First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Lab. Invest. 74, 374-383.
117. Zettlmeissl, G., Rudolph, R. & Jaenicke, R. (1979). Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical Properties of Aggregation. Biochemistry 18, 5567-5571.
118. Rudolph, R., Zettlmeissl, G. & Jaenicke, R. (1979). Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 2. Reactivation of irreversibly denatured aggregates. Biochemistry 18, 5572-5575.
119. Klein, J. & Dhurjati, P. (1995). Protein aggregation kinetics in an Escherichia coli strain overexpressing a Salmonella typhimurium CheY mutant gene. Appl. Environ. Microbiol. 61, 1220-1225.
120. Shen, C.L., Scott, G.L., Merchant, F. & Murphy, R.M. (1993). Light scattering analysis of fibril growth from the amino-terminal fragment β(1-28) of β-amyloid peptide. Biophys. J. 65, 2383-2395.
121. Lundberg, K.M., Stenland, C.J., Cohen, F.E., Prusiner, S.B. & Millhauser, G.L. (1997). Kinetics and mechanism of amyloid formation by the prion protein H1 peptide as determined by time-dependent ESR. Chem. Biol. 4, 345-355.
122. Fink, A.L., Calciano, L.J., Goto, Y., Kurotsu, T. & Palleros, D.R. (1994). Classification of acid denaturation of proteins - intermediates and unfolded states. Biochemistry 33, 12504-12511.
123. Fink, A.L., Calciano, L.J., Goto, Y., Nishimura, M. & Swedberg, S.A. (1993). Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease. Protein Sci. 2, 1155-1160.
124. Yoshida, K., Shibata, T., Masai, J., Sato, K., Noguti, T., Go, M. & Yanagawa, H. (1993). Protein anatomy: spontaneous formation of filamentous helical structures from the N-terminal module of barnase. Biochemistry 32, 2162-2166.
125. Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-579.
126. + but not ATP hydrolysis. Nature 365, 664-666.
127. Palleros, D.R., Shi, L., Reid, K.L. & Rnk, A.L. (1994). Hsp70-protein complexes - complex stability and conformation of bound substrate protein. J. Biol. Chem. 269, 13107-13114.
128. McCarty, J.S., Buchberger, A., Reinstein, J. & Bukau, B. (1995). The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249, 126-137.
129. Martin, J. & Hartl, F.U. (1997). Chaperone-assisted protein folding. Curr. Opin. Struct. Biol. 7, 41-52.
130. Farr, G.W., Scharl, E.C., Schumacher, R.J., Sondek, S. & Horwich, A.L. (1997). Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms. Cell 89, 927-937.
131. Fenton, W.A. & Norwich, A.L. (1997). GroEL-mediated protein folding. Protein Sci. 6, 743-760.
132. Walter, S., Lorimer, G.H. & Schmid, F.X. (1996). A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc. Natl Acad. Sci. USA 93, 9425-9430.
133. Thomas, J.G. & Baneyx, F. (1996). Protein folding in the cytoplasm of Escherichia coli: requirements for the DnaK-DnaJ-GrpE and GroEL-GroES molecular chaperone machines. Mol. Microbiol. 21, 1185-1196.
134. Schwarz, E., Lilie, H. & Rudolph, R. (1996). The effect of molecular chaperones on in vivo and in vitro folding processes. Biol. Chem. 377, 411-416.
135. Artigues, A., Iriarte, A. & Martinezcarrion, M. (1997). Refolding intermediates of acid-unfolded mitochondrial aspartate aminotransferase bind to hsp70. J. Biol. Chem. 272, 16852-16861.
136. Blum, P., Velligan, M., Lin, N. & Matin, A. (1992). DnaK-mediated alterations in human growth hormone protein inclusion bodies. Biotechnology (N.Y.) 10, 301-304.
137. Gragerov, A., Nudler, E., Komissarova, N., Gaitanaris, G.A., Gottesman, M.E. & Nikiforov, V. (1992). Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc. Natl Acad. Sci. USA 89, 10341-10344.
138. Buchberger, A., Schrder, H., Hesterkamp, T., Schonfeld, H.J. & Bukau, B. (1996). Substrate shuttling between the DnaK and GroEL Systems indicates a chaperone network promoting protein folding. J. Mol. Biol. 261, 328-333.
139. Buchberger, A., Valencia, A., McMacken, R., Sander, C. & Bukau, B. (1994). The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J. 13, 1687-1695.
140. Szabo, A., Langer, T., Schroder, H., Flanagan, J., Bukau, B. & Hartl, F.U. (1994). The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc. Natl Acad. Sci. USA 91, 10345-10349.
141. Hendrick J.P. & Hartl F.U. (1993). Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
142. Thomas, J.G. & Baneyx, F. (1996). Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins. J. Biol. Chem. 271, 11141-11147.
143. Rudolph, R. & Lilie, H. (1996). In vitro folding of inclusion body proteins. FASEB J. 10, 49-56.
144. Chaudhuri, J.B., Batas, B. & Guise, A.D. (1996). Improving protein refolding yields by minimizing aggregation. Ann. N.Y. Acad. Sci. 782, 495-505.
145. Wetlaufer, D.B. & Xie, Y. (1995). Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II. Protein Sci. 4, 1535-1543.
146. Miroy, G.J., Lai, Z., Lashuel, H.A., Peterson, S.A., Strang, C. & Kelly, J.W. (1996). Inhibiting transthyretin amyloid fibril formation via protein stabilization. Proc. Natl Acad. Sci. USA 93, 15051-15056.
147. Buchner, J. & Rudolph, R. (1991). Routes to active proteins from transformed microorganisms. Curr. Opin. Biotechnol. 2, 532-538.
148. Guise, A.D., West, S.M. & Chaudhuri, J.B. (1996). Protein folding in vivo and renaturation of recombinant proteins from inclusion bodies. Mol. Biotechnol. 6, 53-64.
149. Thomas, J.G., Ayling, A. & Baneyx, F. (1997). Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold. Appl. Biochem. Biotechnol. 66, 197-238.
150. Stempfer, G., Holl-Neugebauer, B. & Rudolph, R. (1996). Improved refolding of an immobilized fusion protein. Nat Biotechnol. 14, 329-334.
151. Georgiou, G. & Valax, P. (1996). Expression of correctly folded proteins in Escherichia coli. Curr. Opin. Biotechnol. 7, 190-197.
152. Rozema, D. & Gellman, S.H. (1996). Artificial chaperone-assisted refolding of denatured-reduced lysozyme - modulation of the competition between renaturation and aggregation Biochemistry 35, 15760-15771.
153. Collins, K.D. & Washabaugh, M.W. (1985). The Hofmeister effect and the behaviour of water at interfaces Q. Rev. Biophys. 18, 323-422.
154. Tatzelt, J., Prusiner, S.B. & Welch, W.J. (1996). Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 15, 6363-6373.
155. Xie, Y. & Wetlaufer, D.B. (1996). Control of aggregation in protein refolding: the temperature-leap tactic. Protein Sci. 5, 517-523.
156. Ghanta, J., Shen, C.L., Kiessling, L.L. & Murphy, R.M. (1996). A strategy for designing inhibitors of β-amyloid toxicity. J. Biol. Chem. 271, 29525-29528.
157. Soto, C., Kindy, M.S., Baumann, M. & Frangione, B. (1996). Inhibition of Alzheimers amyloidosis by peptides that prevent β-sheet conformation. Biochem. Biophys. Res. Commun. 226, 672-680.
158. Kisilevsky, R. (1996). Anti-amyloid drugs: potential in the treatment of diseases associated with aging. Drugs Aging 8, 75-83.
159. Wood, S.J., Chan, W. & Wetzel, R. (1996). Seeding of A-beta fibril formation is inhibited by all three isotypes of apolipoprotein E. Biochemistry 35, 12623-12628.