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P Wikstrom

Showing results (1-10 of 20) with videos related to

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Archives of Biochemistry and Biophysics|April 15, 1983
An exploration of the primary specificity site of cathepsin BE Shaw, P Wikstrom, J Ruscica
Analytical Biochemistry|February 1, 1988
Iodination of peptidyl chloromethyl ketones for protease affinity labelsP Rauber, P Wikstrom, E Shaw
The Biochemical Journal|September 15, 1985
Evaluation of inhibitor constants and alkylation rates for a series of thrombin affinity labelsB Walker, P Wikstrom, E Shaw
FEBS Letters|February 8, 1988
Active center differences between cathepsins L and B: the S1 binding regionH Kirschke, P Wikstrom, E Shaw
Journal of Enzyme Inhibition|January 1, 1992
Additional peptidyl diazomethyl ketones, including biotinyl derivatives, which affinity-label calpain and related cysteinyl proteinasesP Wikstrom, J Anagli, H Angliker, et al.
The Biochemical Journal|August 15, 1989
The inactivation of the cysteinyl exopeptidases cathepsin H and C by affinity-labelling reagentsH Angliker, P Wikstrom, H Kirschke, et al.
Archives of Biochemistry and Biophysics|April 1, 1989
The properties of peptidyl diazoethanes and chloroethanes as protease inactivatorsP Wikstrom, H Kirschke, S Stone, et al.
The Biochemical Journal|February 1, 1987
The synthesis of lysylfluoromethanes and their properties as inhibitors of trypsin, plasmin and cathepsin BH Angliker, P Wikstrom, P Rauber, et al.
The Biochemical Journal|August 1, 1988
The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin BC Crawford, R W Mason, P Wikstrom, et al.
Biomedica Biochimica Acta|January 1, 1986
Peptidyl fluoromethyl ketones as thiol protease inhibitorsE Shaw, H Angliker, P Rauber, et al.
Pageof 2

Showing results (1-10 of 20) with videos related to

Sort By:
Pageof 2
Archives of Biochemistry and Biophysics|April 15, 1983
An exploration of the primary specificity site of cathepsin BE Shaw, P Wikstrom, J Ruscica
Analytical Biochemistry|February 1, 1988
Iodination of peptidyl chloromethyl ketones for protease affinity labelsP Rauber, P Wikstrom, E Shaw
The Biochemical Journal|September 15, 1985
Evaluation of inhibitor constants and alkylation rates for a series of thrombin affinity labelsB Walker, P Wikstrom, E Shaw
FEBS Letters|February 8, 1988
Active center differences between cathepsins L and B: the S1 binding regionH Kirschke, P Wikstrom, E Shaw
Journal of Enzyme Inhibition|January 1, 1992
Additional peptidyl diazomethyl ketones, including biotinyl derivatives, which affinity-label calpain and related cysteinyl proteinasesP Wikstrom, J Anagli, H Angliker, et al.
The Biochemical Journal|August 15, 1989
The inactivation of the cysteinyl exopeptidases cathepsin H and C by affinity-labelling reagentsH Angliker, P Wikstrom, H Kirschke, et al.
Archives of Biochemistry and Biophysics|April 1, 1989
The properties of peptidyl diazoethanes and chloroethanes as protease inactivatorsP Wikstrom, H Kirschke, S Stone, et al.
The Biochemical Journal|February 1, 1987
The synthesis of lysylfluoromethanes and their properties as inhibitors of trypsin, plasmin and cathepsin BH Angliker, P Wikstrom, P Rauber, et al.
The Biochemical Journal|August 1, 1988
The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin BC Crawford, R W Mason, P Wikstrom, et al.
Biomedica Biochimica Acta|January 1, 1986
Peptidyl fluoromethyl ketones as thiol protease inhibitorsE Shaw, H Angliker, P Rauber, et al.
Pageof 2