Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
7R01GM049878-03
Application #
2187436
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1993-07-01
Project End
1997-03-31
Budget Start
1995-07-01
Budget End
1997-03-31
Support Year
3
Fiscal Year
1995
Total Cost
Indirect Cost

  Institution

Name
Vanderbilt University Medical Center
Department
Biochemistry
Type
Schools of Medicine
DUNS #
004413456
City
Nashville
State
TN
Country
United States
Zip Code
37212

  Publications

Armstrong, R N; Cassidy, C S (2000) New structural and chemical insight into the catalytic mechanism of epoxide hydrolases. Drug Metab Rev 32:327-38
Armstrong, R N (1999) Kinetic and chemical mechanism of epoxide hydrolase. Drug Metab Rev 31:71-86
Tzeng, H F; Laughlin, L T; Armstrong, R N (1998) Semifunctional site-specific mutants affecting the hydrolytic half-reaction of microsomal epoxide hydrolase. Biochemistry 37:2905-11
Laughlin, L T; Tzeng, H F; Lin, S et al. (1998) Mechanism of microsomal epoxide hydrolase. Semifunctional site-specific mutants affecting the alkylation half-reaction. Biochemistry 37:2897-904
Lacourciere, G M; Armstrong, R N (1994) Microsomal and soluble epoxide hydrolases are members of the same family of C-X bond hydrolase enzymes. Chem Res Toxicol 7:121-4