• Wiley Online Library will be disrupted on 26 May from 10:00-12:00 BST (05:00-07:00 EDT) for essential maintenance

SEARCH

SEARCH BY CITATION

References

  • Altieri F, Mattingly JR, Rodriguez-Berrocal FJ, Youssef J, Iriarte A, Wu T, Martinez-Carrion M. 1989. Isolation and properties of a liver mitochondrial precursor protein to aspartate aminotransferase expressed in Escherichia coli. J Biol Chem 264: 47824786.
  • Artigues A, Iriarte A, Martinez-Carrion M. 1994. Acid-induced reversible unfolding of mitochondrial aspartate aminotransferase. J Biol Chem 269: 2199021999.
  • Artigues A, Iriarte A, Martinez-Carrion M. 1997. Refolding intermediates of acid-unfolded mitochondrial aspartate aminotransferase bind to hsp70. J Biol Chem 272: 1685216861.
  • Brems DN, Havel HA. 1989. Folding of bovine growth hormone is consistent with the molten globule hypothesis. Proteins 5: 9395.
  • Clark AC, Frieden C. 1997. GroEL-mediated folding of structurally homologous dihydrofolate reductases. J Mol Biol 268 512525.
  • Clark AC, Hugo E, Frieden C. 1996. Determination of regions in the dihydro-folate reductase structure that interact with the molecular chaperonin GroEL. Biochemistry 35 58935901.
  • Cleland JL, Hedgepeth C, Wang DI. 1992. Polyethylene glycol enhanced re-folding of bovine carbonic anhydrase B. Reaction stoichiometry and refolding model. J Biol Chem 267: 1332713334.
  • Cleland JL, Wang DL 1990. Cosolvent assisted protein refolding. Biotechnology 8: 12741278.
  • Ellis RJ, van der Vies SM. 1991. Molecular chaperones. Annu Rev Biochem 60: 321347.
  • Engelhard M, Evans PA. 1995. Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates. Protein Sci 4: 15531562.
  • Fenton WA, Horwich AL. 1997. GroEL-mediated protein folding. Protein Sci 6: 743760.
  • Fink AL. 1995. Compact intermediate states in protein folding. Annu Rev Bio-phys Biomol Struct 24: 495522.
  • Goldberg ME, 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: 27902797.
  • Hendrick JP, Hartl FU. 1993. Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem 62: 349384.
  • Huynh QK, Sakakibara R, Watanabe T, Wada H. 1980. Glutamic oxaloacetic transaminase isozymes from rat liver. Purification and physicochemical characterization. J Biochem (Tokyo) 88: 231239.
  • Itzhaki LS, Otzen DE, Fersht AR. 1995. Nature and consequences of GroEL-protein interactions. Biochemistry 34: 1458114587.
  • Jansonius JN, Vincent MG. 1987. Structural basis for catalysis by aspartate aminotransferase. In: JumakFA, McPhersonA, eds. Biological macromol-ecules and assemblies. New York: John Wiley & Sons. pp 187285.
  • Kim PS, Baldwin RL. 1990. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 59: 631660.
  • Kuwajima K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6: 37103.
  • Lain B, Iriarte A, Martinez-Carrion M. 1994. Dependence of the folding and import of the precursor to mitochondrial aspartate aminotransferase on the nature of the cell-free translation system. J Biol Chem 269: 1558815596.
  • Lichtenberg D, Robson RJ, Dennis EA. 1983. Solubilization of phospholipids by detergents. Structural and kinetic aspects. Biochim Biophp Acta 737: 285294.
  • Lin S, Schwarz FP, Eisenstein E. 1995. The hydrophobic nature of GroEL-substrate binding. J Biol Chem 270: 10111014.
  • Matthews CR. 1993. Pathways of protein folding. Annu Rev Biochem 62: 653683.
  • Mattingly JR, Iriarte A, Martinez-Canion M. 1993a. Structural features which control folding of homologous proteins in cell-free translation systems. The effect of a mitochondrial targeting presequence on aspartate aminotransferase. J Biol Chem 268: 2632026327.
  • Mattingly JR, Iriarte A, Martinez-Carrion M. 1995. Homologous proteins with different affinities for GroEL. The refolding of the aspartate aminotransferase isozymes at varying temperatures. J Biol Chem 270: 11381148.
  • Mattingly JR, Rodriguez-Berrocal FJ, Gordon J, Iriarte A, Martinez-Carrion M. 1987. Molecular cloning and in vivo expression of a precursor to rat mitochondrial aspartate aminotransferase. Biochem Biophys Res Commun 149: 859865.
  • Mattingly JR, Youssef J, Iriarte A, Martinez-Canion M. 1993b. Protein folding in a cell-free translation system. The fate of the precursor to mitochondrial aspartate aminotransferase. J Biol Chem 268: 39253937.
  • Pave-Preux M, Ferry N, Bouguet J, Hanoune J, Barouki R. 1988. Nucleotide sequence and glucocorticoid regulation of the mRNAs for the isozymes of rat aspartate aminotransferase. J Biol Chem 263: 1745917466.
  • Reyes AM, Iriarte A, Martinez-Canion M. 1993. Refolding of the precursor and mature forms of mitochondrial aspartate aminotransferase after guanidine hydrochloride denaturation. J Biol Chem 268: 2228122291.
  • Rozema D, Gellman SH. 1995. Artificial chaperones: Protein refolding via sequential use of detergents and cyclodextrin. J Am Chem Soc 117: 23732374.
  • Rozema D, Gellman SH. 1996a. Artificial chaperone-assisted refolding of carbonic anhydrase B. J Biol Chem 271: 34783487.
  • Rozema D, Gellman SH. 1996b. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation. Biochemistv 35: 1576015771.
  • Staniforth RA, Cortes A, Burston SG, Atkinson T, Holbrook JJ, Clarke AR. 1994. The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding. FEBS Lett 344: 129135.
  • Tandon S, Horowitz P. 1986. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. J Biol Chem 261: 1561515618.
  • Tandon S, Horowitz PM. 1987. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effects of the concentration and type of detergent. J Biol Chem 262: 44864491.
  • Todd MJ, Lorimer GM. 1995. Stability of the asymmetric Escherichia coli chaperonin complex. Guanidine chloride causes rapid dissociation. J Biol Chem 270 53885394.
  • Torella C, Mattingly JR Jr., Artigues A, Iriarte A, Martinez-Carrion M. 1998. Insight into the conformation of protein folding intermediate(s) trapped by GroEL. J Biol Chem 273: 39153925.
  • Wetlaufer DB, Xie Y. 1995. Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase 11. Protein Sci 4: 15351543.
  • Zardeneta G, Horowitz PM. 1992a. Micelle-assisted protein folding. Denatured rhodanese binding to cardiolipin-containing lauryl maltoside micelles results in slower refolding kinetics but greater enzyme reactivation. J Bid Chem 267 58115816.
  • Zardeneta G, Horowitz PM. 1992b. Cardiolipin liposomes sequester a reactivatable partially folded rhodanase intermediate. Eur J Biochem 210: 831837.