Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32HL010082-01
Application #
2711267
Study Section
Special Emphasis Panel (ZRG4-HEM-2 (01))
Project Start
1998-12-16
Project End
Budget Start
1998-07-01
Budget End
1999-06-30
Support Year
1
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Vanderbilt University Medical Center
Department
Pathology
Type
Schools of Medicine
DUNS #
004413456
City
Nashville
State
TN
Country
United States
Zip Code
37212
Ohanyan, Vahagn; Yin, Liya; Bardakjian, Raffi et al. (2015) Requisite Role of Kv1.5 Channels in Coronary Metabolic Dilation. Circ Res 117:612-621
Chilian, William M; Penn, Marc S; Pung, Yuh Fen et al. (2012) Coronary collateral growth--back to the future. J Mol Cell Cardiol 52:905-11
Dai, Qiuyun; Dong, Mingxin; Liu, Zhuguo et al. (2011) Ca 2+-induced self-assembly in designed peptides with optimally spaced gamma-carboxyglutamic acid residues. J Inorg Biochem 105:52-7
Boxrud, Paul D; Bock, Paul E (2004) Coupling of conformational and proteolytic activation in the kinetic mechanism of plasminogen activation by streptokinase. J Biol Chem 279:36642-9
Boxrud, Paul D; Verhamme, Ingrid M; Bock, Paul E (2004) Resolution of conformational activation in the kinetic mechanism of plasminogen activation by streptokinase. J Biol Chem 279:36633-41
Boxrud, P D; Verhamme, I M; Fay, W P et al. (2001) Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation. J Biol Chem 276:26084-9
Boxrud, P D; Fay, W P; Bock, P E (2000) Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen. J Biol Chem 275:14579-89
Boxrud, P D; Bock, P E (2000) Streptokinase binds preferentially to the extended conformation of plasminogen through lysine binding site and catalytic domain interactions. Biochemistry 39:13974-81