Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM067172-02
Application #
6693408
Study Section
Physical Biochemistry Study Section (PB)
Program Officer
Ikeda, Richard A
Project Start
2003-01-01
Project End
2007-12-31
Budget Start
2004-01-01
Budget End
2004-12-31
Support Year
2
Fiscal Year
2004
Total Cost
$229,500
Indirect Cost

  Institution

Name
Case Western Reserve University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
077758407
City
Cleveland
State
OH
Country
United States
Zip Code
44106

  Publications

Fishovitz, Jennifer; Li, Min; Frase, Hilary et al. (2011) Active-site-directed chemical tools for profiling mitochondrial Lon protease. ACS Chem Biol 6:781-8
Patterson-Ward, Jessica; Tedesco, Johnathan; Hudak, Jason et al. (2009) Utilization of synthetic peptides to evaluate the importance of substrate interaction at the proteolytic site of Escherichia coli Lon protease. Biochim Biophys Acta 1794:1355-63
Licht, Stuart; Lee, Irene (2008) Resolving individual steps in the operation of ATP-dependent proteolytic molecular machines: from conformational changes to substrate translocation and processivity. Biochemistry 47:3595-605
Lee, Irene; Suzuki, Carolyn K (2008) Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates. Biochim Biophys Acta 1784:727-35
Patterson-Ward, Jessica; Huang, Jon; Lee, Irene (2007) Detection and characterization of two ATP-dependent conformational changes in proteolytically inactive Escherichia coli Lon mutants by stopped flow kinetic techniques. Biochemistry 46:13593-605
Frase, Hilary; Lee, Irene (2007) Peptidyl boronates inhibit Salmonella enterica serovar Typhimurium Lon protease by a competitive ATP-dependent mechanism. Biochemistry 46:6647-57
Lee, Irene; Berdis, Anthony J; Suzuki, Carolyn K (2006) Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies. Mol Biosyst 2:477-83
Vineyard, Diana; Zhang, Xuemei; Lee, Irene (2006) Transient kinetic experiments demonstrate the existence of a unique catalytic enzyme form in the peptide-stimulated ATPase mechanism of Escherichia coli Lon protease. Biochemistry 45:11432-43
Frase, Hilary; Hudak, Jason; Lee, Irene (2006) Identification of the proteasome inhibitor MG262 as a potent ATP-dependent inhibitor of the Salmonella enterica serovar Typhimurium Lon protease. Biochemistry 45:8264-74
Vineyard, Diana; Patterson-Ward, Jessica; Lee, Irene (2006) Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease. Biochemistry 45:4602-10

Showing the most recent 10 out of 13 publications