Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK040441-08
Application #
2141327
Study Section
Biochemistry Study Section (BIO)
Project Start
1988-09-01
Project End
1998-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
8
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Indiana University-Purdue University at Indianapolis
Department
Biochemistry
Type
Schools of Medicine
DUNS #
005436803
City
Indianapolis
State
IN
Country
United States
Zip Code
46202
Popov, K M; Shimomura, Y; Hawes, J W et al. (2000) Branched-chain alpha-keto acid dehydrogenase kinase. Methods Enzymol 324:162-78
Hawes, J W; Crabb, D W; Chan, R J et al. (2000) Mammalian 3-hydroxyisobutyrate dehydrogenase. Methods Enzymol 324:218-28
Kedishvili, N Y; Goodwin, G W; Popov, K M et al. (2000) Mammalian methylmalonate-semialdehyde dehydrogenase. Methods Enzymol 324:207-18
Shimomura, Y; Murakami, T; Nakai, N et al. (2000) 3-hydroxyisobutyryl-CoA hydrolase. Methods Enzymol 324:229-40
Nakai, N; Kobayashi, R; Popov, K M et al. (2000) Determination of branched-chain alpha-keto acid dehydrogenase activity state and branched-chain alpha-keto acid dehydrogenase kinase activity and protein in mammalian tissues. Methods Enzymol 324:48-62
Hawes, J W; Harper, E T; Crabb, D W et al. (1997) Structural and mechanistic aspects of a new family of dehydrogenases, the beta-hydroxyacid dehydrogenases. Adv Exp Med Biol 414:395-402
Taniguchi, K; Nonami, T; Nakao, A et al. (1996) The valine catabolic pathway in human liver: effect of cirrhosis on enzyme activities. Hepatology 24:1395-8
Jaskiewicz, J; Zhao, Y; Hawes, J W et al. (1996) Catabolism of isobutyrate by colonocytes. Arch Biochem Biophys 327:265-70
Hawes, J W; Jaskiewicz, J; Shimomura, Y et al. (1996) Primary structure and tissue-specific expression of human beta-hydroxyisobutyryl-coenzyme A hydrolase. J Biol Chem 271:26430-4
Hawes, J W; Harper, E T; Crabb, D W et al. (1996) Structural and mechanistic similarities of 6-phosphogluconate and 3-hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the 3-hydroxyacid dehydrogenases. FEBS Lett 389:263-7

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