Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK044841-03
Application #
2144102
Study Section
Biochemistry Study Section (BIO)
Project Start
1993-12-01
Project End
1997-11-30
Budget Start
1996-01-29
Budget End
1996-11-30
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Temple University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
City
Philadelphia
State
PA
Country
United States
Zip Code
19122
Lavulo, Lopeti T; Emig, Frances A; Ash, David E (2002) Functional consequences of the G235R mutation in liver arginase leading to hyperargininemia. Arch Biochem Biophys 399:49-55
Colleluori, D M; Morris Jr, S M; Ash, D E (2001) Expression, purification, and characterization of human type II arginase. Arch Biochem Biophys 389:135-43
Colleluori, D M; Ash, D E (2001) Classical and slow-binding inhibitors of human type II arginase. Biochemistry 40:9356-62
Lavulo, L T; Sossong Jr, T M; Brigham-Burke, M R et al. (2001) Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid. J Biol Chem 276:14242-8
Cox, J D; Cama, E; Colleluori, D M et al. (2001) Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase. Biochemistry 40:2689-701
Kim, N N; Cox, J D; Baggio, R F et al. (2001) Probing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase as a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum. Biochemistry 40:2678-88
Ash, D E; Cox, J D; Christianson, D W (2000) Arginase: a binuclear manganese metalloenzyme. Met Ions Biol Syst 37:407-28
Baggio, R; Emig, F A; Christianson, D W et al. (1999) Biochemical and functional profile of a newly developed potent and isozyme-selective arginase inhibitor. J Pharmacol Exp Ther 290:1409-16
Ash, D E; Scolnick, L R; Kanyo, Z F et al. (1998) Molecular basis of hyperargininemia: structure-function consequences of mutations in human liver arginase. Mol Genet Metab 64:243-9
Esch, F; Lin, K I; Hills, A et al. (1998) Purification of a multipotent antideath activity from bovine liver and its identification as arginase: nitric oxide-independent inhibition of neuronal apoptosis. J Neurosci 18:4083-95

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