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Biochemistry
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July 28, 2004
Thermodynamic evaluation of a covalently bonded transition state analogue inhibitor: inhibition of beta-lactamases by phosphonates
Rajesh Nagarajan, R F Pratt
The Journal of Organic Chemistry
|
October 23, 2004
Synthesis and evaluation of new substrate analogues of streptomyces R61 DD-peptidase: dissection of a specific ligand
Rajesh Nagarajan, R F Pratt
The Biochemical Journal
|
December 1, 1993
Structure-activity relationships in the inhibition of serine beta-lactamases by phosphonic acid derivatives
J Rahil, R F Pratt
Biochemistry
|
January 11, 1994
Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements: phosphonate monoester inhibitors of a beta-lactamase
J Rahil, R F Pratt
Biochemistry
|
July 27, 2005
Transpeptidation reactions of a specific substrate catalyzed by the Streptomyces R61 DD-peptidase: the structural basis of acyl acceptor specificity
Ish Kumar, R F Pratt
Biochemistry
|
September 28, 2013
Kinetics of action of a two-stage pro-inhibitor of serine β-lactamases
Ronak Tilvawala, R F Pratt
Bioorganic & Medicinal Chemistry
|
March 17, 2004
Kinetic and structural consequences of the leaving group in substrates of a class C beta-lactamase
Yong-Mo Ahn, R F Pratt
The Journal of Biological Chemistry
|
January 10, 1980
Phenylpropynal, a specific, irreversible, non-beta-lactam inhibitor of beta-lactamases
D P Schenkein, R F Pratt
The Biochemical Journal
|
January 1, 1991
Inactivation of the RTEM-1 cysteine beta-lactamase by iodoacetate. The nature of active-site functional groups and comparisons with the native enzyme
A K Knap, R F Pratt
Antimicrobial Agents and Chemotherapy
|
July 1, 1990
Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein
J R Knox, R F Pratt
Page
of 14
Search research articles
Search
Showing results (21-30 of 139) with videos related to
Sort By:
Page
of 14
Biochemistry
|
July 28, 2004
Thermodynamic evaluation of a covalently bonded transition state analogue inhibitor: inhibition of beta-lactamases by phosphonates
Rajesh Nagarajan, R F Pratt
The Journal of Organic Chemistry
|
October 23, 2004
Synthesis and evaluation of new substrate analogues of streptomyces R61 DD-peptidase: dissection of a specific ligand
Rajesh Nagarajan, R F Pratt
The Biochemical Journal
|
December 1, 1993
Structure-activity relationships in the inhibition of serine beta-lactamases by phosphonic acid derivatives
J Rahil, R F Pratt
Biochemistry
|
January 11, 1994
Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements: phosphonate monoester inhibitors of a beta-lactamase
J Rahil, R F Pratt
Biochemistry
|
July 27, 2005
Transpeptidation reactions of a specific substrate catalyzed by the Streptomyces R61 DD-peptidase: the structural basis of acyl acceptor specificity
Ish Kumar, R F Pratt
Biochemistry
|
September 28, 2013
Kinetics of action of a two-stage pro-inhibitor of serine β-lactamases
Ronak Tilvawala, R F Pratt
Bioorganic & Medicinal Chemistry
|
March 17, 2004
Kinetic and structural consequences of the leaving group in substrates of a class C beta-lactamase
Yong-Mo Ahn, R F Pratt
The Journal of Biological Chemistry
|
January 10, 1980
Phenylpropynal, a specific, irreversible, non-beta-lactam inhibitor of beta-lactamases
D P Schenkein, R F Pratt
The Biochemical Journal
|
January 1, 1991
Inactivation of the RTEM-1 cysteine beta-lactamase by iodoacetate. The nature of active-site functional groups and comparisons with the native enzyme
A K Knap, R F Pratt
Antimicrobial Agents and Chemotherapy
|
July 1, 1990
Different modes of vancomycin and D-alanyl-D-alanine peptidase binding to cell wall peptide and a possible role for the vancomycin resistance protein
J R Knox, R F Pratt
Page
of 14