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The Journal of Biological Chemistry
|
July 25, 1975
Intermediates and enzymes between alpha-ketoarginine and gamma-guanidinobutyrate in the L-arginine catabolic pathway of Pseudomonas putida
A S Vanderbilt, N S Gaby, V W Rodwell
The Journal of Biological Chemistry
|
December 25, 1977
Interconversion of active and inactive forms of rat liver hydroxymethylglutaryl-CoA reductase
J L Nordstrom, V W Rodwell, J J Mitschelen
Biochemistry
|
January 8, 2000
Investigation of the conserved lysines of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase
D A Bochar, C V Stauffacher, V W Rodwell
The Journal of Biological Chemistry
|
March 10, 1984
Allosteric activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by nucleoside diphosphates
H J Harwood, K G Brandt, V W Rodwell
Science (New York, N.Y.)
|
June 23, 1995
Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution
C M Lawrence, V W Rodwell, C V Stauffacher
Journal of Bacteriology
|
October 1, 1989
(S)-3-hydroxy-3-methylglutaryl coenzyme A reductase, a product of the mva operon of Pseudomonas mevalonii, is regulated at the transcriptional level
Y L Wang, M J Beach, V W Rodwell
FEBS Letters
|
June 9, 1986
Hydroxymethylglutaryl-CoA reductase--the rate-limiting enzyme of cholesterol biosynthesis. A report of a meeting held at Nijenrode Castle, Breukelen, The Netherlands, August 24, 1985
M J Geelen, D M Gibson, V W Rodwell
Biotechnology and Bioengineering
|
January 1, 1983
Reduction of acetoin to 2,3-butanediol in Klebsiella pneumoniae: a new model
M Voloch, M R Ladisch, V W Rodwell, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 23, 1999
Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase
L Tabernero, D A Bochar, V W Rodwell, et al.
Biochemistry
|
July 22, 1999
Aminoethylcysteine can replace the function of the essential active site lysine of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase
D A Bochar, L Tabernero, C V Stauffacher, et al.
Page
of 8
Search research articles
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Showing results (61-70 of 79) with videos related to
Sort By:
Page
of 8
The Journal of Biological Chemistry
|
July 25, 1975
Intermediates and enzymes between alpha-ketoarginine and gamma-guanidinobutyrate in the L-arginine catabolic pathway of Pseudomonas putida
A S Vanderbilt, N S Gaby, V W Rodwell
The Journal of Biological Chemistry
|
December 25, 1977
Interconversion of active and inactive forms of rat liver hydroxymethylglutaryl-CoA reductase
J L Nordstrom, V W Rodwell, J J Mitschelen
Biochemistry
|
January 8, 2000
Investigation of the conserved lysines of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase
D A Bochar, C V Stauffacher, V W Rodwell
The Journal of Biological Chemistry
|
March 10, 1984
Allosteric activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by nucleoside diphosphates
H J Harwood, K G Brandt, V W Rodwell
Science (New York, N.Y.)
|
June 23, 1995
Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution
C M Lawrence, V W Rodwell, C V Stauffacher
Journal of Bacteriology
|
October 1, 1989
(S)-3-hydroxy-3-methylglutaryl coenzyme A reductase, a product of the mva operon of Pseudomonas mevalonii, is regulated at the transcriptional level
Y L Wang, M J Beach, V W Rodwell
FEBS Letters
|
June 9, 1986
Hydroxymethylglutaryl-CoA reductase--the rate-limiting enzyme of cholesterol biosynthesis. A report of a meeting held at Nijenrode Castle, Breukelen, The Netherlands, August 24, 1985
M J Geelen, D M Gibson, V W Rodwell
Biotechnology and Bioengineering
|
January 1, 1983
Reduction of acetoin to 2,3-butanediol in Klebsiella pneumoniae: a new model
M Voloch, M R Ladisch, V W Rodwell, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 23, 1999
Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase
L Tabernero, D A Bochar, V W Rodwell, et al.
Biochemistry
|
July 22, 1999
Aminoethylcysteine can replace the function of the essential active site lysine of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase
D A Bochar, L Tabernero, C V Stauffacher, et al.
Page
of 8