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Mok, Samuel C.,Bonome, Tomas,Vathipadiekal, Vinod,Bell, Aaron,Johnson, Michael E.,Wong, kwong-kwok,Park, Dong-Choon,Hao, Ke,Yip, Daniel K.P.,Donninger, Howard,Ozbun, Laurent,Samimi, Goli,Brady, John,R Elsevier 2009 CANCER CELL Vol.16 No.6
<P><B>Summary</B></P><P>Advanced stage papillary serous tumors of the ovary are responsible for the majority of ovarian cancer deaths, yet the molecular determinants modulating patient survival are poorly characterized. Here, we identify and validate a prognostic gene expression signature correlating with survival in a series of microdissected serous ovarian tumors. Independent evaluation confirmed the association of a prognostic gene microfibril-associated glycoprotein 2 (<I>MAGP2</I>) with poor prognosis, whereas in vitro mechanistic analyses demonstrated its ability to prolong tumor cell survival and stimulate endothelial cell motility and survival via the α<SUB>V</SUB>β<SUB>3</SUB> integrin receptor. Increased MAGP2 expression correlated with microvessel density suggesting a proangiogenic role in vivo. Thus, MAGP2 may serve as a survival-associated target.</P>
High temperature operation and stability of phosphorescent OLEDs
V. I. Adamovich,M. S. Weaver,R. C. Kwong,J. J. Brown 한국물리학회 2005 Current Applied Physics Vol.5 No.1
Phosphorescent organic light emitting diodes were fabricated that show high eciencies with commercially viable lifetimes atdisplay brightnesses of tens of thousands of hours at room temperature. We investigate here the performance of theses devices atelevated temperatures. We demonstrate that devices containing phosphorescent dopants can be operated at temperatures up to 130.C. We also demonstrate improved device performance due to thermal treating e.g. a red phosphorescent device that decays by only10% in the rst 5500 h of operation driven with an initial luminance of 300 cd/m2
Choi, D.,Moon, J. H.,Kim, H.,Sung, B. J.,Kim, M. W.,Tae, G. Y.,Satija, S. K.,Akgun, B.,Yu, C.-J.,Lee, H. W.,Lee, D. R.,Henderson, J. M.,Kwong, J. W.,Lam, K. L.,Lee, K. Y. C.,Shin, K. The Royal Society of Chemistry 2012 Soft matter Vol.8 No.32
<P>X-Ray and neutron reflectivity measurements on systems composed of a 1,2-dipalmitoyl-<I>sn</I>-glycero-3-phosphocholine (DPPC) bilayer and transcription-activating-factor derived peptides (TDPs) have allowed us to determine the mechanism of membrane translocation. By monitoring the structural changes of the bilayers caused by the binding of TDPs while systemically varying temperature and TDP concentration, our results revealed the detailed molecular structures of the stepwise interactions that occurred during the translocation of TDP across the lipid bilayers. While little indication of membrane perturbation was observed at low TDP concentrations, we found that the TDP movement across the membrane induced defect formations in the membrane at higher TDP concentrations.</P> <P>Graphic Abstract</P><P>X-Ray and neutron reflectivity have allowed us to reveal the detailed molecular structures of cell penetrating peptides across the supported lipid bilayers. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c2sm25913c'> </P>