Search results for "gne-6776" | DICTAF
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Nline submission ?Thorough peer review ?Inclusion in PubMed and all major indexing services ?Maximum visibility for your research Submit your manuscript at www.biomedcentral.com/submitQuadri et al. BMC Cancer (2017) 17:495 DOI 10.1186/s12885-017-3481-RESEARCH ARTICLEOpen AccessExpression of the scaffold connector enhancer of kinase suppressor of Ras 1 (CNKSR1) is correlated with clinical out
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Ibed above. With phosphorylation of extracellular-signalregulated kinase (ERK) inducing nuclear translocation staining was predominantly nuclear with a few cases also showing cytoplasmic staining. Scoring of p-ERK1/2 was done blinded to the CNKSR1 results using standard intensity scores above (0 = no staining, 1 = weak staining, 2 = moderate staining, 3 = strong staining). In addition, the percent
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R of proteins either indirectly or directly connected to MAPK/ERK signaling (Ras, ERBB2, Myc) [4, 31]. A limitation of this study was that the dataset did not include all clinical variables, such as complete TNM staging and chemotherapy treatment, and thus we could not evaluate all variables that might impact survival. While the HRs of known clinical (TNM system N and M stage) and pathological var
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Ns including phosphorylation of select sites of CNKSR1, appears in line with our findings of a correlation between the cellular distribution of CNKSR1 and nuclear p-ERK expression levels [30].Fig. 8 Cellular distribution of CNKSR1 is associated with p-ERK expression levels in pancreatic cancer specimens. a p-ERK cellular distribution and nuclear expression levels (scored as 1+, 2+, and 3+) in 86 c
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Ns including phosphorylation of select sites of CNKSR1, appears in line with our findings of a correlation between the cellular distribution of CNKSR1 and nuclear p-ERK expression levels [30].Fig. 8 Cellular distribution of CNKSR1 is associated with p-ERK expression levels in pancreatic cancer specimens. a p-ERK cellular distribution and nuclear expression levels (scored as 1+, 2+, and 3+) in 86 c
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Ained parallel sections with a pooled IgG control. This protein-level confirmation of our microarray data gave us the impetus to pursue functional in vitro and in vivo assays with galectin-1 over-expressing GBM cells.Extracellular matrix attachmentResultsIdentification of galectin-1 as a potential mediator of glioma invasionThe quantity of RNA obtained from various xenograft tumors was highly vari
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That is relatively over-expressed at the tumor periphery. These graphical representations of gene expression data compare the relative expression of galectin-1 from the core and edge of tumors to pooled data from normal mouse brain samples. (Graphics from GeneSpringW).created. To ensure that galectin-1 over-expression would not enhance proliferation of the U87MG line (and hence alter the interpret
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Assays of GBM cells stably transfected to over-express galectin-1, perfectly fit in with the previous studies mentioned above and highlight the importance of galectin-1 in the biologically aggressive behavior of experimental GBMs. While there was no enhancement of proliferation or change inattachment to fibronectin, galectin-1 upregulation induced more rapid two-dimensional migration and enhanced