During 2011-2012, the Protein Chemistry Core provided services to investigators in the NCI-CCR as well as other NIH institutes. In addition, the Protein Chemistry Core collaborated with laboratories in the extramural community. The Core performed endoproteolytic digestions on 32-P labeled protein samples and analyzed the resulting peptides by high pressure liquid chomatography, phosphoamino acid analysis and Edman degredation, resulting in the identification of sites of protein phosphorylation. The Core also processed samples for comparative 2D-gel analysis and served as a resource to investigators regarding these techniques.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Scientific Cores Intramural Research (ZIC)
Project #
1ZICBC011083-04
Application #
8554109
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
4
Fiscal Year
2012
Total Cost
$175,378
Indirect Cost
Name
National Cancer Institute Division of Basic Sciences
Department
Type
DUNS #
City
State
Country
Zip Code
Sarkar, Tapasree Roy; Sharan, Shikha; Wang, Jun et al. (2012) Identification of a Src tyrosine kinase/SIAH2 E3 ubiquitin ligase pathway that regulates C/EBP? expression and contributes to transformation of breast tumor cells. Mol Cell Biol 32:320-32
Ritt, Daniel A; Monson, Daniel M; Specht, Suzanne I et al. (2010) Impact of feedback phosphorylation and Raf heterodimerization on normal and mutant B-Raf signaling. Mol Cell Biol 30:806-19
Dougherty, Michele K; Ritt, Daniel A; Zhou, Ming et al. (2009) KSR2 is a calcineurin substrate that promotes ERK cascade activation in response to calcium signals. Mol Cell 34:652-62
McKay, Melissa M; Ritt, Daniel A; Morrison, Deborah K (2009) Signaling dynamics of the KSR1 scaffold complex. Proc Natl Acad Sci U S A 106:11022-7