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Analytical Biochemistry
|
April 1, 1988
Application of 19F nuclear magnetic resonance to examine covalent modification reactions of tyrosyl derivatives: a study of calcineurin catalysis
B L Martin, D J Graves
Biochemical Pharmacology
|
March 9, 1993
Clearance of N-nitrosodimethylamine and N-nitrosodiethylamine by the perfused rat liver. Relationship to the Km and Vmax for nitrosamine metabolism
R J Graves, P F Swann
Methods in Enzymology
|
January 1, 1983
Separation of the subunits of muscle phosphorylase kinase
K F Chan, D J Graves
Bulletin of the Medical Library Association
|
April 1, 1981
Library instruction within the medical record administration curriculum
J M Marcotte, K J Graves
Methods in Enzymology
|
January 1, 1980
The use of alternative substrates to study enzyme-catalyzed chemical modification
D J Graves, T M Martensen
Biochemical and Biophysical Research Communications
|
January 23, 1970
Ultraviolet spectral differences between phosphorylase a and b
M L Bartlett, D J Graves
The Journal of Biological Chemistry
|
July 10, 1973
Association-dissociation properties of sodium borohydride-reduced phosphorylase b
J I Tu, D J Graves
The Journal of Biological Chemistry
|
May 25, 1979
Complementation of glycogen phosphorylase b' with synthetic peptides. Influence of nucleotides
A M Janski, D J Graves
Proceedings of the National Academy of Sciences of the United States of America
|
May 1, 1990
Alkylation interference identifies essential DNA contacts for sequence-specific binding of the eukaryotic transcription factor C/EBP
J A Nye, B J Graves
The Journal of Biological Chemistry
|
December 25, 1987
Relationship of phosphorylation and ADP-ribosylation using a synthetic peptide as a model substrate
S V Kharadia, D J Graves
Page
of 80
Search research articles
Search
Showing results (101-110 of 793) with videos related to
Sort By:
Page
of 80
Analytical Biochemistry
|
April 1, 1988
Application of 19F nuclear magnetic resonance to examine covalent modification reactions of tyrosyl derivatives: a study of calcineurin catalysis
B L Martin, D J Graves
Biochemical Pharmacology
|
March 9, 1993
Clearance of N-nitrosodimethylamine and N-nitrosodiethylamine by the perfused rat liver. Relationship to the Km and Vmax for nitrosamine metabolism
R J Graves, P F Swann
Methods in Enzymology
|
January 1, 1983
Separation of the subunits of muscle phosphorylase kinase
K F Chan, D J Graves
Bulletin of the Medical Library Association
|
April 1, 1981
Library instruction within the medical record administration curriculum
J M Marcotte, K J Graves
Methods in Enzymology
|
January 1, 1980
The use of alternative substrates to study enzyme-catalyzed chemical modification
D J Graves, T M Martensen
Biochemical and Biophysical Research Communications
|
January 23, 1970
Ultraviolet spectral differences between phosphorylase a and b
M L Bartlett, D J Graves
The Journal of Biological Chemistry
|
July 10, 1973
Association-dissociation properties of sodium borohydride-reduced phosphorylase b
J I Tu, D J Graves
The Journal of Biological Chemistry
|
May 25, 1979
Complementation of glycogen phosphorylase b' with synthetic peptides. Influence of nucleotides
A M Janski, D J Graves
Proceedings of the National Academy of Sciences of the United States of America
|
May 1, 1990
Alkylation interference identifies essential DNA contacts for sequence-specific binding of the eukaryotic transcription factor C/EBP
J A Nye, B J Graves
The Journal of Biological Chemistry
|
December 25, 1987
Relationship of phosphorylation and ADP-ribosylation using a synthetic peptide as a model substrate
S V Kharadia, D J Graves
Page
of 80