@article{deterding_williams_humble_petrovich_wei_trempus_gates_zhu_smart_tennant_et al._2011, title={CD34 antigen: Determination of specific sites of phosphorylation in vitro and in vivo}, volume={301}, ISSN={["1387-3806"]}, DOI={10.1016/j.ijms.2010.05.027}, abstractNote={CD34, a type I transmembrane glycoprotein, is a surface antigen which is expressed on several cell types, including hematopoietic progenitors, endothelial cells, as well as mast cells. Recently, CD34 has been described as a marker for epidermal stem cells in mouse hair follicles, and is expressed in outer root sheath cells of the human hair follicle. Although the biological function and regulation of CD34 is not well understood, it is thought to be involved in cell adhesion as well as possibly having a role in signal transduction. In addition, CD34 was shown to be critical for skin tumor development in mice, although the exact mechanism remains unknown. Many proteins’ functions and biological activities are regulated through post-translational modifications. The extracellular domain of CD34 is heavily glycosylated but the role of these glycans in CD34 function is unknown. Additionally, two sites of tyrosine phosphorylation have been reported on human CD34 and it is known that CD34 is phosphorylated, at least in part, by protein kinase C; however, the precise location of the sites of phosphorylation has not been reported. In an effort to identify specific phosphorylation sites in CD34 and delineate the possible role of protein kinase C, we undertook the identification of the in vitro sites of phosphorylation on the intracellular domain of mouse CD34 (aa 309–382) following PKC treatment. For this work, we are using a combination of enzymatic proteolysis and peptide sequencing by mass spectrometry. After which the in vivo sites of phosphorylation of full-length mouse CD34 expressed from HEK293F cells were determined. The observed in vivo sites of phosphorylation, however, are not consensus PKC sites, but our data indicate that one of these sites may possibly be phosphorylated by AKT2. These results suggest that other kinases, as well as PKC, may have important signaling functions in CD34.}, number={1-3}, journal={INTERNATIONAL JOURNAL OF MASS SPECTROMETRY}, author={Deterding, Leesa J. and Williams, Jason G. and Humble, Margaret M. and Petrovich, Robert M. and Wei, Sung-Jen and Trempus, Carol S. and Gates, Matthew B. and Zhu, Feng and Smart, Robert C. and Tennant, Raymond W. and et al.}, year={2011}, month={Mar}, pages={12–21} }
 @article{zhang_li_zhu_cui_li_li_wang_wang_wang_yan_2009, title={Subcellular localization of APMCF1 and its biological significance of expression pattern in normal and malignant human tissues}, volume={28}, journal={Journal of Experimental & Clinical Cancer Research}, author={Zhang, Y. Q. and Li, Q. L. and Zhu, F. and Cui, J. H. and Li, K. N. and Li, Q. and Wang, R. A. and Wang, W. Y. and Wang, W. H. and Yan, W.}, year={2009} }
 @article{ewing_zhu_zhu_house_smart_2008, title={C/EBP beta represses p53 to promote cell survival downstream of DNA damage independent of oncogenic Ras and p19(Arf)}, volume={15}, ISSN={["1476-5403"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-54049144611&partnerID=MN8TOARS}, DOI={10.1038/cdd.2008.105}, abstractNote={CCAAT/enhancer-binding protein-β (C/EBPβ) is a mediator of cell survival and tumorigenesis. When C/EBPβ−/− mice are treated with carcinogens that produce oncogenic Ras mutations in keratinocytes, they respond with abnormally elevated keratinocyte apoptosis and a block in skin tumorigenesis. Although this aberrant carcinogen-induced apoptosis results from abnormal upregulation of p53, it is not known whether upregulated p53 results from oncogenic Ras and its ability to induce p19Arf and/or activate DNA-damage response pathways or from direct carcinogen-induced DNA damage. We report that p19Arf is dramatically elevated in C/EBPβ−/− epidermis and that C/EBPβ represses a p19Arf promoter reporter. To determine whether p19Arf is responsible for the proapoptotic phenotype in C/EBPβ−/− mice, C/EBPβ−/−;p19Arf−/− mice were generated. C/EBPβ−/−;p19Arf−/− mice responded to carcinogen treatment with increased p53 and apoptosis, indicating p19Arf is not essential. To ascertain whether oncogenic Ras activation induces aberrant p53 and apoptosis in C/EBPβ−/− epidermis, we generated K14-ER:Ras;C/EBPβ−/− mice. Oncogenic Ras activation induced by 4-hydroxytamoxifen did not produce increased p53 or apoptosis. Finally, when C/EBPβ−/− mice were treated with differing types of DNA-damaging agents, including alkylating chemotherapeutic agents, they displayed aberrant levels of p53 and apoptosis. These results indicate that C/EBPβ represses p53 to promote cell survival downstream of DNA damage and suggest that inhibition of C/EBPβ may be a target for cancer cotherapy to increase the efficacy of alkylating chemotherapeutic agents.}, number={11}, journal={CELL DEATH AND DIFFERENTIATION}, author={Ewing, S. J. and Zhu, S. and Zhu, F. and House, J. S. and Smart, R. C.}, year={2008}, month={Nov}, pages={1734–1744} }