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Journal of Protein Chemistry|January 1, 1994
The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptideJ A Mendoza, P M HorowitzBiochemistry|May 23, 1998
High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structureB M Gorovits, P M HorowitzBiochimica Et Biophysica Acta|April 14, 1976
The aromatic residue content of the enzyme rhodaneseR D Baillie, P M HorowitzThe Journal of Biological Chemistry|June 9, 2001
The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivationA M Bhattacharyya, P M HorowitzBiochimica Et Biophysica Acta|August 31, 1988
The differential functional stability of various forms of bovine liver rhodaneseB A Aird, P M HorowitzThe Journal of Biological Chemistry|October 21, 1994
Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomersJ A Mendoza, P M HorowitzProtein Expression and Purification|October 1, 1991
Purification of bovine liver rhodanese by low-pH column chromatographyG P Kurzban, P M HorowitzBiochemistry|May 21, 1985
Differential binding of the fluorescent probe 8-anilinonaphthalene-2-sulfonic acid to rhodanese catalytic intermediatesP M Horowitz, N L CriscimagnaBiochimica Et Biophysica Acta|March 11, 1976
A study of the single polypeptide nature of rhodanese. A comparison of different preparationsJ M Crawford, P M HorowitzThe Journal of Biological Chemistry|March 18, 1994
The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249G X Luo, P M HorowitzPageof 15