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Mendoza, J A; Demeler, B; Horowitz, P M (1994) Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action. J Biol Chem 269:2447-51
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Miller-Martini, D M; Hua, S; Horowitz, P M (1994) Cysteine 254 can cooperate with active site cysteine 247 in reactivation of 5,5'-dithiobis(2-nitrobenzoic acid)-inactivated rhodanese as determined by site-directed mutagenesis. J Biol Chem 269:12414-8
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Mendoza, J A; Horowitz, P M (1994) The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptide. J Protein Chem 13:15-22
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Zardeneta, G; Horowitz, P M (1994) Protein refolding at high concentrations using detergent/phospholipid mixtures. Anal Biochem 218:392-8
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Luo, G X; Horowitz, P M (1994) The stability of the molecular chaperonin cpn60 is affected by site-directed replacement of cysteine 518. J Biol Chem 269:32151-4
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Luo, G X; Horowitz, P M (1994) The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249. J Biol Chem 269:8220-5
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Miller-Martini, D M; Chirgwin, J M; Horowitz, P M (1994) Mutations of noncatalytic sulfhydryl groups influence the stability, folding, and oxidative susceptibility of rhodanese. J Biol Chem 269:3423-8
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Sloan, I S; Horowitz, P M; Chirgwin, J M (1994) Rapid secretion by a nonclassical pathway of overexpressed mammalian mitochondrial rhodanese. J Biol Chem 269:27625-30
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Islam, T A; Miller-Martini, D M; Horowitz, P M (1994) Mutation of cysteine 254 facilitates the conformational changes accompanying the interconversion of persulfide-substituted and persulfide-free rhodanese. J Biol Chem 269:7903-13
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Luo, G X; Horowitz, P M (1993) The folding and stability of rhodanese are influenced by the replacement of glutamic acid 17 in the NH2-terminal helix by proline but not by glutamine. J Biol Chem 268:10246-51
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