Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM042436-20
Application #
2181375
Study Section
Biochemistry Study Section (BIO)
Project Start
1976-05-01
Project End
1998-01-31
Budget Start
1995-08-01
Budget End
1998-01-31
Support Year
20
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Rice University
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
050299031
City
Houston
State
TX
Country
United States
Zip Code
77005
Deng, H; Kurz, L C; Rudolph, F B et al. (1998) Characterization of hydrogen bonding in the complex of adenosine deaminase with a transition state analogue: a Raman spectroscopic study. Biochemistry 37:4968-76
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Sideraki, V; Mohamedali, K A; Wilson, D K et al. (1996) Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase. Biochemistry 35:7862-72
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Sideraki, V; Wilson, D K; Kurz, L C et al. (1996) Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation. Biochemistry 35:15019-28
Blackburn, M R; Datta, S K; Wakamiya, M et al. (1996) Metabolic and immunologic consequences of limited adenosine deaminase expression in mice. J Biol Chem 271:15203-10
Mohamedali, K A; Kurz, L C; Rudolph, F B (1996) Site-directed mutagenesis of active site glutamate-217 in mouse adenosine deaminase. Biochemistry 35:1672-80
Cooper, B F; Rudolph, F B (1995) Product inhibition applications. Methods Enzymol 249:188-211
Blackburn, M R; Wakamiya, M; Caskey, C T et al. (1995) Tissue-specific rescue suggests that placental adenosine deaminase is important for fetal development in mice. J Biol Chem 270:23891-4

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