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The Journal of Biological Chemistry|December 25, 1986
Oxidative inactivation of the enzyme rhodanese by reduced nicotinamide adenine dinucleotideP M Horowitz, K FalksenBiochimica Et Biophysica Acta|February 4, 1982
A fluorescence study of conformational changes induced by substrate and temperature in bovine liver thiosulfate sulfurtransferaseZ Wasylewski, P M HorowitzJournal of Protein Chemistry|December 29, 2000
Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodaneseM Panda, P M HorowitzThe Journal of Biological Chemistry|September 29, 1995
Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptidesJ Ybarra, P M HorowitzThe Journal of Biological Chemistry|December 1, 1995
The chaperonin GroEL is destabilized by binding of ADPB M Gorovits, P M HorowitzThe Journal of Biological Chemistry|January 5, 1996
Ligand-induced conformational changes in the apical domain of the chaperonin GroELD L Gibbons, P M HorowitzJournal of Protein Chemistry|July 8, 1999
Nucleotide and Mg2+ induced conformational changes in GroEL can be detected by sulfhydryl labelingE A Jai, P M HorowitzJournal of Protein Chemistry|December 1, 1992
Sulfhydryl modification of E. coli Cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complexJ A Mendoza, P M HorowitzThe Journal of Biological Chemistry|February 5, 1992
Sulfhydryl groups on yeast ribosomal proteins L7 and L26 are significantly more reactive in the 80 S particles than in the 60 S subunitsJ C Lee, P M HorowitzBiochimica Et Biophysica Acta|April 8, 1976
Denaturation-induced disulfide formation in the enzyme rhodaneseR D Baillie, P M HorowitzPageof 15