Abstract

The Molecular Biology and Cell Culture Core will provide a centralized facility for carrying out all site-directed mutagenesis experiments, construction of new expression plasmids and creation of bacterial and baby hamster kidney cell lines expressing the desired proteins required by the P.I.s of the four projects. Construction of plasmids for e3xpression of new serpins will be done in consultation with the appropriate P.I. The core will occupy common space with the Protein Expression and Purification core. The Administrative Director will be responsible for overnight of the core and for ensuring equitable service to all of the projects.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Program Projects (P01)
Project #
5P01HL064013-03
Application #
6565129
Study Section
Heart, Lung, and Blood Initial Review Group (HLBP)
Project Start
2001-12-01
Project End
2002-11-30
Budget Start
Budget End
Support Year
3
Fiscal Year
2002
Total Cost
$214,708
Indirect Cost

  Institution

Name
University of Illinois at Chicago
Department
Type
DUNS #
121911077
City
Chicago
State
IL
Country
United States
Zip Code
60612

  Publications

Duhan, U; Patston, P (2010) Explanation for the high heat stability of thyroxine binding globulin-Chicago. Endocr Regul 44:43-7
Swanson, Richard; Raghavendra, Manikanahally P; Zhang, Weiqing et al. (2007) Serine and cysteine proteases are translocated to similar extents upon formation of covalent complexes with serpins. Fluorescence perturbation and fluorescence resonance energy transfer mapping of the protease binding site in CrmA complexes with granzyme J Biol Chem 282:2305-13
Dementiev, Alexey; Dobo, Jozsef; Gettins, Peter G W (2006) Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase. J Biol Chem 281:3452-7
Simonovic, Miljan; Denault, Jean-Bernard; Salvesen, Guy S et al. (2005) Lack of involvement of strand s1'A of the viral serpin CrmA in anti-apoptotic or caspase-inhibitory functions. Arch Biochem Biophys 440:1-9
Tesch, Lisa D; Raghavendra, Manikanahally P; Bedsted-Faarvang, Tina et al. (2005) Specificity and reactive loop length requirements for crmA inhibition of serine proteases. Protein Sci 14:533-42
Gettins, Peter G W; Backovic, Marija; Peterson, Francis C (2004) Use of NMR to study serpin function. Methods 32:120-9
Al-Ayyoubi, Maher; Gettins, Peter G W; Volz, Karl (2004) Crystal structure of human maspin, a serpin with antitumor properties: reactive center loop of maspin is exposed but constrained. J Biol Chem 279:55540-4
Dementiev, Alexey; Petitou, Maurice; Herbert, Jean-Marc et al. (2004) The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity. Nat Struct Mol Biol 11:863-7
Patston, Philip A; Church, Frank C; Olson, Steven T (2004) Serpin-ligand interactions. Methods 32:93-109
O'Keeffe, Denis; Olson, Steven T; Gasiunas, Nijole et al. (2004) The heparin binding properties of heparin cofactor II suggest an antithrombin-like activation mechanism. J Biol Chem 279:50267-73

Showing the most recent 10 out of 26 publications