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P E Scarborough

Showing results (1-10 of 14) with videos related to

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Protein Engineering|April 1, 1994
Redesign of the substrate specificity of human cathepsin D: the dominant role of position 287 in the S2 subsiteP E Scarborough, B M Dunn
Methods in Molecular Biology (Clifton, N.J.)|January 1, 1994
Analysis of proteinase specificity by studies of peptide substrates. The use of UV and fluorescence spectroscopy to quantitate rates of enzymatic cleavageB M Dunn, P E Scarborough, R Davenport, et al.
Drug Metabolism Reviews|March 5, 1999
P450 subfamily CYP2J and their role in the bioactivation of arachidonic acid in extrahepatic tissuesP E Scarborough, J Ma, W Qu, et al.
Advances in Experimental Medicine and Biology|January 1, 1995
Comparison of the active site specificity of the aspartic proteinases based on a systematic series of peptide substratesB M Dunn, P E Scarborough, W T Lowther, et al.
Advances in Experimental Medicine and Biology|January 1, 1991
Comparison of kinetic properties of native and recombinant human cathepsin DP E Scarborough, G R Richo, J Kay, et al.
Protein Science : a Publication of the Protein Society|February 1, 1993
Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modelingP E Scarborough, K Guruprasad, C Topham, et al.
American Journal of Respiratory Cell and Molecular Biology|November 6, 2001
Airway inflammation and responsiveness in prostaglandin H synthase-deficient mice exposed to bacterial lipopolysaccharideD C Zeldin, C Wohlford-Lenane, P Chulada, et al.
Advances in Experimental Medicine and Biology|April 30, 1998
Comparison of the specificity of the aspartic proteinases towards internally consistent sets of oligopeptide substratesB M Dunn, K Oda, J Kay, et al.
Advances in Experimental Medicine and Biology|January 1, 1991
Structure-function database for active site binding to the aspartic proteinasesC Rao, P E Scarborough, W T Lowther, et al.
The Journal of Biological Chemistry|June 11, 1999
Molecular cloning, enzymatic characterization, developmental expression, and cellular localization of a mouse cytochrome P450 highly expressed in kidneyJ Ma, W Qu, P E Scarborough, et al.
Pageof 2

Showing results (1-10 of 14) with videos related to

Sort By:
Pageof 2
Protein Engineering|April 1, 1994
Redesign of the substrate specificity of human cathepsin D: the dominant role of position 287 in the S2 subsiteP E Scarborough, B M Dunn
Methods in Molecular Biology (Clifton, N.J.)|January 1, 1994
Analysis of proteinase specificity by studies of peptide substrates. The use of UV and fluorescence spectroscopy to quantitate rates of enzymatic cleavageB M Dunn, P E Scarborough, R Davenport, et al.
Drug Metabolism Reviews|March 5, 1999
P450 subfamily CYP2J and their role in the bioactivation of arachidonic acid in extrahepatic tissuesP E Scarborough, J Ma, W Qu, et al.
Advances in Experimental Medicine and Biology|January 1, 1995
Comparison of the active site specificity of the aspartic proteinases based on a systematic series of peptide substratesB M Dunn, P E Scarborough, W T Lowther, et al.
Advances in Experimental Medicine and Biology|January 1, 1991
Comparison of kinetic properties of native and recombinant human cathepsin DP E Scarborough, G R Richo, J Kay, et al.
Protein Science : a Publication of the Protein Society|February 1, 1993
Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modelingP E Scarborough, K Guruprasad, C Topham, et al.
American Journal of Respiratory Cell and Molecular Biology|November 6, 2001
Airway inflammation and responsiveness in prostaglandin H synthase-deficient mice exposed to bacterial lipopolysaccharideD C Zeldin, C Wohlford-Lenane, P Chulada, et al.
Advances in Experimental Medicine and Biology|April 30, 1998
Comparison of the specificity of the aspartic proteinases towards internally consistent sets of oligopeptide substratesB M Dunn, K Oda, J Kay, et al.
Advances in Experimental Medicine and Biology|January 1, 1991
Structure-function database for active site binding to the aspartic proteinasesC Rao, P E Scarborough, W T Lowther, et al.
The Journal of Biological Chemistry|June 11, 1999
Molecular cloning, enzymatic characterization, developmental expression, and cellular localization of a mouse cytochrome P450 highly expressed in kidneyJ Ma, W Qu, P E Scarborough, et al.
Pageof 2