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P M Horowitz

Showing results (91-100 of 151) with videos related to

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The Journal of Biological Chemistry|November 4, 1994
Rapid secretion by a nonclassical pathway of overexpressed mammalian mitochondrial rhodaneseI S Sloan, P M Horowitz, J M Chirgwin
Biochimie|September 1, 1991
The initiation codon AUG binds at a hydrophobic site on yeast 40S ribosomal subunits as revealed by fluorescence studies with bis (1,8-anilinonaphthalenesulfonate)J C Lee, L C Yeh, P M Horowitz
The Journal of Biological Chemistry|April 29, 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 mutagenesisD M Miller-Martini, S Hua, P M Horowitz
Biochemistry|June 17, 1986
Detection of energy transfer between tryptophan residues in the tubulin molecule and bound bis(8-anilinonaphthalene-1-sulfonate), an inhibitor of microtubule assembly, that binds to a flexible region on tubulinA R Prasad, R F Luduena, P M Horowitz
Biochimica Et Biophysica Acta|March 21, 1998
Rhodanese folding is controlled by the partitioning of its folding intermediatesB M Gorovits, W A McGee, P M Horowitz
The Journal of Biological Chemistry|December 5, 1992
Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodaneseJ A Mendoza, M C Butler, P M Horowitz
Biochimica Et Biophysica Acta|March 15, 1995
Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independentJ A Mendoza, J L Martinez, P M Horowitz
Biochemistry|October 12, 1982
Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-coA synthetase from Escherichia coliA R Prasad, J S Nishimura, P M Horowitz
Biochemistry|October 24, 1995
Residual structure in urea-denatured chaperonin GroELB M Gorovits, J W Seale, P M Horowitz
Protein Science : a Publication of the Protein Society|November 1, 1994
Folding and aggregation of TEM beta-lactamase: analogies with the formation of inclusion bodies in Escherichia coliG Georgiou, P Valax, M Ostermeier, et al.
Pageof 16

Showing results (91-100 of 151) with videos related to

Sort By:
Pageof 16
The Journal of Biological Chemistry|November 4, 1994
Rapid secretion by a nonclassical pathway of overexpressed mammalian mitochondrial rhodaneseI S Sloan, P M Horowitz, J M Chirgwin
Biochimie|September 1, 1991
The initiation codon AUG binds at a hydrophobic site on yeast 40S ribosomal subunits as revealed by fluorescence studies with bis (1,8-anilinonaphthalenesulfonate)J C Lee, L C Yeh, P M Horowitz
The Journal of Biological Chemistry|April 29, 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 mutagenesisD M Miller-Martini, S Hua, P M Horowitz
Biochemistry|June 17, 1986
Detection of energy transfer between tryptophan residues in the tubulin molecule and bound bis(8-anilinonaphthalene-1-sulfonate), an inhibitor of microtubule assembly, that binds to a flexible region on tubulinA R Prasad, R F Luduena, P M Horowitz
Biochimica Et Biophysica Acta|March 21, 1998
Rhodanese folding is controlled by the partitioning of its folding intermediatesB M Gorovits, W A McGee, P M Horowitz
The Journal of Biological Chemistry|December 5, 1992
Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodaneseJ A Mendoza, M C Butler, P M Horowitz
Biochimica Et Biophysica Acta|March 15, 1995
Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independentJ A Mendoza, J L Martinez, P M Horowitz
Biochemistry|October 12, 1982
Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-coA synthetase from Escherichia coliA R Prasad, J S Nishimura, P M Horowitz
Biochemistry|October 24, 1995
Residual structure in urea-denatured chaperonin GroELB M Gorovits, J W Seale, P M Horowitz
Protein Science : a Publication of the Protein Society|November 1, 1994
Folding and aggregation of TEM beta-lactamase: analogies with the formation of inclusion bodies in Escherichia coliG Georgiou, P Valax, M Ostermeier, et al.
Pageof 16