Agency
National Institute of Health (NIH)
Institute
National Institute on Drug Abuse (NIDA)
Type
Research Project (R01)
Project #
7R01DA002243-16
Application #
3207205
Study Section
Drug Abuse Biomedical Research Review Committee (DABR)
Project Start
1992-09-01
Project End
1996-02-28
Budget Start
1992-09-01
Budget End
1993-02-28
Support Year
16
Fiscal Year
1992
Total Cost
Indirect Cost
Name
University of Kentucky
Department
Type
Schools of Medicine
DUNS #
832127323
City
Lexington
State
KY
Country
United States
Zip Code
40506
Song, Eun Suk; Ozbil, Mehmet; Zhang, Tingting et al. (2015) An Extended Polyanion Activation Surface in Insulin Degrading Enzyme. PLoS One 10:e0133114
Guan, Hanjun; Chow, K Martin; Song, Eunsuk et al. (2015) The Mitochondrial Peptidase Pitrilysin Degrades Islet Amyloid Polypeptide in Beta-Cells. PLoS One 10:e0133263
Sexton, Travis; Hitchcook, Lisa J; Rodgers, David W et al. (2012) Active site mutations change the cleavage specificity of neprilysin. PLoS One 7:e32343
Guan, H; Chow, K M; Shah, R et al. (2012) Degradation of islet amyloid polypeptide by neprilysin. Diabetologia 55:2989-98
Noinaj, Nicholas; Song, Eun Suk; Bhasin, Sonia et al. (2012) Anion activation site of insulin-degrading enzyme. J Biol Chem 287:48-57
Song, Eun Suk; Melikishvili, Manana; Fried, Michael G et al. (2012) Cysteine 904 is required for maximal insulin degrading enzyme activity and polyanion activation. PLoS One 7:e46790
Song, Eun Suk; Rodgers, David W; Hersh, Louis B (2011) Mixed dimers of insulin-degrading enzyme reveal a cis activation mechanism. J Biol Chem 286:13852-8
Chirra, Hariharasudhan D; Sexton, Travis; Biswal, Dipti et al. (2011) Catalase-coupled gold nanoparticles: comparison between the carbodiimide and biotin-streptavidin methods. Acta Biomater 7:2865-72
Noinaj, Nicholas; Bhasin, Sonia K; Song, Eun Suk et al. (2011) Identification of the allosteric regulatory site of insulysin. PLoS One 6:e20864
Shen, Xin-Ming; Crawford, Thomas O; Brengman, Joan et al. (2011) Functional consequences and structural interpretation of mutations of human choline acetyltransferase. Hum Mutat 32:1259-67

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