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P M Horowitz

Showing results (21-30 of 151) with videos related to

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Biochimica Et Biophysica Acta|June 12, 1995
Rhodanese conformational changes permit oxidation to give disulfides that form in a kinetically determined sequenceP M Horowitz, S Hua
The Journal of Biological Chemistry|September 25, 1992
Acid pH-induced conformational changes in bovine liver rhodaneseP M Horowitz, R Xu
The Journal of Biological Chemistry|February 5, 1993
Interactive intermediates are formed during the urea unfolding of rhodaneseP M Horowitz, M Butler
The Journal of Biological Chemistry|December 25, 1986
Oxidative inactivation of the enzyme rhodanese by reduced nicotinamide adenine dinucleotideP M Horowitz, K Falksen
Biochimica 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 Horowitz
Biochemical and Biophysical Research Communications|May 30, 1980
Some comparisons between solution and crystal properties of thiosulfate sulfurtransferaseP M Horowitz, K Patel
The Journal of Biological Chemistry|December 5, 1992
Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequenceG Zardeneta, P M Horowitz
Journal of Protein Chemistry|December 29, 2000
Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodaneseM Panda, P M Horowitz
The 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 Horowitz
The Journal of Biological Chemistry|December 1, 1995
The chaperonin GroEL is destabilized by binding of ADPB M Gorovits, P M Horowitz
Pageof 16

Showing results (21-30 of 151) with videos related to

Sort By:
Pageof 16
Biochimica Et Biophysica Acta|June 12, 1995
Rhodanese conformational changes permit oxidation to give disulfides that form in a kinetically determined sequenceP M Horowitz, S Hua
The Journal of Biological Chemistry|September 25, 1992
Acid pH-induced conformational changes in bovine liver rhodaneseP M Horowitz, R Xu
The Journal of Biological Chemistry|February 5, 1993
Interactive intermediates are formed during the urea unfolding of rhodaneseP M Horowitz, M Butler
The Journal of Biological Chemistry|December 25, 1986
Oxidative inactivation of the enzyme rhodanese by reduced nicotinamide adenine dinucleotideP M Horowitz, K Falksen
Biochimica 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 Horowitz
Biochemical and Biophysical Research Communications|May 30, 1980
Some comparisons between solution and crystal properties of thiosulfate sulfurtransferaseP M Horowitz, K Patel
The Journal of Biological Chemistry|December 5, 1992
Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequenceG Zardeneta, P M Horowitz
Journal of Protein Chemistry|December 29, 2000
Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodaneseM Panda, P M Horowitz
The 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 Horowitz
The Journal of Biological Chemistry|December 1, 1995
The chaperonin GroEL is destabilized by binding of ADPB M Gorovits, P M Horowitz
Pageof 16