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The Journal of Biological Chemistry|October 25, 1988
Acceptor substrate-potentiated inactivation of bovine liver rhodaneseB A Aird, P M HorowitzBiochimica Et Biophysica Acta|April 8, 1976
A reexamination of the postulated charge transfer interactions at the active site of the enzyme rhodaneseR D Baillie, P M HorowitzThe Journal of Biological Chemistry|June 2, 1995
The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded proteinB M Gorovits, P M HorowitzThe Journal of Biological Chemistry|December 23, 1994
The stability of the molecular chaperonin cpn60 is affected by site-directed replacement of cysteine 518G X Luo, P M HorowitzThe Journal of Biological Chemistry|December 22, 1995
The C-terminal sequence of the chaperonin GroES is required for oligomerizationJ W Seale, P M HorowitzBiochimica Et Biophysica Acta|January 5, 1987
Chemical modification of bovine liver rhodanese with tetrathionate: differential effects on the sulfur-free and sulfur-containing catalytic intermediatesA R Prasad, P M HorowitzThe Journal of Biological Chemistry|August 15, 1985
Spectral differences between rhodanese catalytic intermediates unrelated to enzyme conformationS F Chow, P M HorowitzThe Journal of Biological Chemistry|December 15, 1985
Tetracyanonickelate probes the active site of sulfur-free rhodaneseS F Chow, P M HorowitzThe Journal of Biological Chemistry|March 31, 1995
Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401D L Gibbons, P M HorowitzBiochimica Et Biophysica Acta|March 29, 1990
A physical characterization of sulfane sulfurtransferaseB A Aird, P M HorowitzPageof 15