Abstract

) The CORE B Protein Expression Facility will provide investigators a common source of highly purified proteins and the technical knowledge for use of these proteins to meet the experimental objectives of this Program Project. The CORE will consolidate the efforts of six laboratories into one facility, eliminating unnecessary duplication of technical expertise and decreasing expresses for technical staff, while providing quality control for critical reagents. The CORE will provide active recombinant caspase, caspase inhibitory proteins (crmA, p35, IAPs), functional fragments of TNF family receptors, and functional fragments of TRAF-family proteins using bacterial and baculovirus expression systems. A formalized procedure for establishing priority reagent requests among the investigators are described. The CORE B will be located both at the Burnham Institute with bacterial expression under the direction of Dr. Welsh and at the La Jolla Institute for Allergy & Immunology with baculoviral expression under the direction of Dr. Ware.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Program Projects (P01)
Project #
5P01CA069381-07
Application #
6595006
Study Section
Project Start
2002-05-28
Project End
2003-04-30
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
7
Fiscal Year
2002
Total Cost
$168,360
Indirect Cost

  Institution

Name
Sanford-Burnham Medical Research Institute
Department
Type
DUNS #
009214214
City
La Jolla
State
CA
Country
United States
Zip Code
92037

  Publications

Xu, X-P; Zhai, D; Kim, E et al. (2013) Three-dimensional structure of Bax-mediated pores in membrane bilayers. Cell Death Dis 4:e683
Chipuk, Jerry E; McStay, Gavin P; Bharti, Archana et al. (2012) Sphingolipid metabolism cooperates with BAK and BAX to promote the mitochondrial pathway of apoptosis. Cell 148:988-1000
Fujikura, D; Ito, M; Chiba, S et al. (2012) CLIPR-59 regulates TNF-?-induced apoptosis by controlling ubiquitination of RIP1. Cell Death Dis 3:e264
Zervoudi, Efthalia; Papakyriakou, Athanasios; Georgiadou, Dimitra et al. (2011) Probing the S1 specificity pocket of the aminopeptidases that generate antigenic peptides. Biochem J 435:411-20
Pop, Cristina; Oberst, Andrew; Drag, Marcin et al. (2011) FLIP(L) induces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity. Biochem J 433:447-457
Cheung, Timothy C; Ware, Carl F (2011) The canonical and unconventional ligands of the herpesvirus entry mediator. Adv Exp Med Biol 691:353-62
Garrison, Jason B; Correa, Ricardo G; Gerlic, Motti et al. (2011) ARTS and Siah collaborate in a pathway for XIAP degradation. Mol Cell 41:107-16
Lu, Jennifer V; Weist, Brian M; van Raam, Bram J et al. (2011) Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity. Proc Natl Acad Sci U S A 108:15312-7
Ponder, Elizabeth L; Albrow, Victoria E; Leader, Brittany A et al. (2011) Functional characterization of a SUMO deconjugating protease of Plasmodium falciparum using newly identified small molecule inhibitors. Chem Biol 18:711-21
Timmer, John C; Salvesen, Guy S (2011) N-terminomics: a high-content screen for protease substrates and their cleavage sites. Methods Mol Biol 753:243-55

Showing the most recent 10 out of 192 publications