Abstract

The first goal of this facility is the purification of highly homogeneous proteins which are required by theProject members. It is anticipated that all Program members will engage in biochemical projects whichrequire the use of homogeneous proteins; proteins that are either unavailable through commercial sources, orsignificantly more expensive or of lower quality that obtainable in a dedicated core staffed by experiencedscientists. Consolidating the efforts of all Program members into one facility will eliminate unnecessaryduplication of technical expertise, decrease expenses for the technical staff, while providing control forcritical reagents. Once a purification has been established for a given protein, repetitive preparations will behighly 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 diffractionanalysis. 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 #
2P01CA069381-10
Application #
6935680
Study Section
Subcommittee G - Education (NCI)
Project Start
2005-05-01
Project End
2010-04-30
Budget Start
2005-05-01
Budget End
2006-04-30
Support Year
10
Fiscal Year
2005
Total Cost
$63,320
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
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