Abstract

PROTEIN EXPRESSION FACILITY The first goal of this facility is the purification of highly homogeneous proteins which are required by the Project members. It is anticipated that all Program members will engage in biochemical projects which require the use of homogeneous proteins;proteins that are either unavailable through commercial sources, or significantly more expensive or of lower quality that obtainable in a dedicated core staffed by experienced scientists. Consolidating the efforts of all Program members into one facility will eliminate unnecessary duplication of technical expertise, decrease expenses for the technical staff, while providing control for critical reagents. Once a purification has been established for a given protein, repetitive preparations will be highly consistent. This will establish a high level of quality control. The second goal of the facility is to produce large quantities of highly purified proteins for X-ray diffraction analysis. The number of these proteins will be significantly lower, but their amounts will be much higher.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Program Projects (P01)
Project #
5P01CA069381-14
Application #
7849759
Study Section
Subcommittee G - Education (NCI)
Project Start
Project End
Budget Start
2009-05-01
Budget End
2010-04-30
Support Year
14
Fiscal Year
2009
Total Cost
$90,290
Indirect Cost

  Institution

Name
Sanford-Burnham Medical Research Institute
Department
Type
DUNS #
020520466
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
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
Oberst, Andrew; Dillon, Christopher P; Weinlich, Ricardo et al. (2011) Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis. Nature 471:363-7
Leverrier, S; Salvesen, G S; Walsh, C M (2011) Enzymatically active single chain caspase-8 maintains T-cell survival during clonal expansion. Cell Death Differ 18:90-8
Krajewska, Maryla; You, Zerong; Rong, Juan et al. (2011) Neuronal deletion of caspase 8 protects against brain injury in mouse models of controlled cortical impact and kainic acid-induced excitotoxicity. PLoS One 6:e24341

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