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The Journal of Biological Chemistry
|
December 15, 1991
The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate
M D Toney, J F Kirsch
Biochemistry
|
September 28, 1971
Kinetics and thermodynamics of the reactions of acyl-papains. Effects of pH, temperature, solvents, ionic strength, and added nucleophiles
P M Hindle, J F Kirsch
Biochemistry
|
November 29, 1977
Pyridoxamine-pyruvate transaminase. 2. Temperature-jump and stopped-flow kinetic investigation of the rates and mechanism of the reaction of 5'-deoxypyridoxal with the enzyme
P J Gilmer, J F Kirsch
Biochemistry
|
April 23, 1996
The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis
J M Goldberg, J F Kirsch
Biochemistry
|
February 16, 1993
Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift
M D Toney, J F Kirsch
Frontiers in Computational Neuroscience
|
August 4, 2015
Velocity neurons improve performance more than goal or position neurons do in a simulated closed-loop BCI arm-reaching task
James Y Liao, Robert F Kirsch
Science (New York, N.Y.)
|
March 17, 1989
Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
M D Toney, J F Kirsch
Biochemistry
|
November 11, 1980
Kinetics and mechanism of inhibition of Escherichia coli alkaline phosphatase by permanganate ion
R A Thomas, J F Kirsch
Biochemistry
|
July 1, 1999
A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system
M K Geck, J F Kirsch
Biochemistry
|
January 14, 1986
Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase
M Bazelyansky, E Robey, J F Kirsch
Page
of 33
Search research articles
Search
Showing results (101-110 of 327) with videos related to
Sort By:
Page
of 33
The Journal of Biological Chemistry
|
December 15, 1991
The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate
M D Toney, J F Kirsch
Biochemistry
|
September 28, 1971
Kinetics and thermodynamics of the reactions of acyl-papains. Effects of pH, temperature, solvents, ionic strength, and added nucleophiles
P M Hindle, J F Kirsch
Biochemistry
|
November 29, 1977
Pyridoxamine-pyruvate transaminase. 2. Temperature-jump and stopped-flow kinetic investigation of the rates and mechanism of the reaction of 5'-deoxypyridoxal with the enzyme
P J Gilmer, J F Kirsch
Biochemistry
|
April 23, 1996
The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis
J M Goldberg, J F Kirsch
Biochemistry
|
February 16, 1993
Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift
M D Toney, J F Kirsch
Frontiers in Computational Neuroscience
|
August 4, 2015
Velocity neurons improve performance more than goal or position neurons do in a simulated closed-loop BCI arm-reaching task
James Y Liao, Robert F Kirsch
Science (New York, N.Y.)
|
March 17, 1989
Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
M D Toney, J F Kirsch
Biochemistry
|
November 11, 1980
Kinetics and mechanism of inhibition of Escherichia coli alkaline phosphatase by permanganate ion
R A Thomas, J F Kirsch
Biochemistry
|
July 1, 1999
A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system
M K Geck, J F Kirsch
Biochemistry
|
January 14, 1986
Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase
M Bazelyansky, E Robey, J F Kirsch
Page
of 33