The Experts below are selected from a list of 81 Experts worldwide ranked by ideXlab platform
Odd Nygard - One of the best experts on this subject based on the ideXlab platform.
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probing the structure of mouse ehrlich Ascites Cell 5 8s 18s and 28s ribosomal rna in situ
Nucleic Acids Research, 1994Co-Authors: Lovisa Holmberg, Yvette Melander, Odd NygardAbstract:The secondary structure of mouse Ehrlich Ascites 18S, 5.8S and 28S ribosomal RNA in situ was investigated by chemical modification using dimethyl sulphate and 1-cyclohexyl-3-(morpholinoethyl) carbodiimide metho-p-toluene sulphonate. These reagents specifically modify unpaired bases in the RNA. The reactive bases were localized by primer extension followed by gel electrophoresis. The three rRNA species were equally accessible for modification i.e. approximately 10% of the nucleotides were reactive. The experimental data support the theoretical secondary structure models proposed for 18S and 5.8/28S rRNA as almost all modified bases were located in putative single-strand regions of the rRNAs or in helical regions that could be expected to undergo dynamic breathing. However, deviations from the suggested models were found in both 18S and 28S rRNA. In 18S rRNA some putative helices in the 5'-domain were extensively modified by the single-strand specific reagents as was one of the suggested helices in domain III of 28S rRNA. Of the four eukaryote specific expansion segments present in mouse Ehrlich Ascites Cell 28S rRNA, segments I and III were only partly available for modification while segments II and IV showed average to high modification.
Lovisa Holmberg - One of the best experts on this subject based on the ideXlab platform.
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probing the structure of mouse ehrlich Ascites Cell 5 8s 18s and 28s ribosomal rna in situ
Nucleic Acids Research, 1994Co-Authors: Lovisa Holmberg, Yvette Melander, Odd NygardAbstract:The secondary structure of mouse Ehrlich Ascites 18S, 5.8S and 28S ribosomal RNA in situ was investigated by chemical modification using dimethyl sulphate and 1-cyclohexyl-3-(morpholinoethyl) carbodiimide metho-p-toluene sulphonate. These reagents specifically modify unpaired bases in the RNA. The reactive bases were localized by primer extension followed by gel electrophoresis. The three rRNA species were equally accessible for modification i.e. approximately 10% of the nucleotides were reactive. The experimental data support the theoretical secondary structure models proposed for 18S and 5.8/28S rRNA as almost all modified bases were located in putative single-strand regions of the rRNAs or in helical regions that could be expected to undergo dynamic breathing. However, deviations from the suggested models were found in both 18S and 28S rRNA. In 18S rRNA some putative helices in the 5'-domain were extensively modified by the single-strand specific reagents as was one of the suggested helices in domain III of 28S rRNA. Of the four eukaryote specific expansion segments present in mouse Ehrlich Ascites Cell 28S rRNA, segments I and III were only partly available for modification while segments II and IV showed average to high modification.
Patricia A. Johnson - One of the best experts on this subject based on the ideXlab platform.
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VEGF expression and the effect of NSAIDs on Ascites Cell proliferation in the hen model of ovarian cancer
Gynecologic oncology, 2008Co-Authors: Mary Ellen Urick, James R. Giles, Patricia A. JohnsonAbstract:Objectives. We aimed to determine the expression of vascular endothelial growth factor (VEGF) and the effect of nonsteroidal antiinflammatory drugs (NSAIDs) on the proliferation of Cells isolated from Ascites in the hen model of ovarian cancer. Methods. Ovarian tumor and normal ovary were collected from hens and Ascites Cells were isolated from hens with ovarian cancer. Quantitative real-time PCR was used to quantify mRNA expression. Immunohistochemical and/or Western blot analyses were used to localize protein expression in ovarian tumors, normal ovaries, and Ascites Cells. Cells were treated with a nonspecific, COX-1-specific, or COX-2-specific NSAID and proliferation was determined. Results. VEGF mRNA was increased in Ascites Cells and there was a trend for a correlation between VEGF mRNA in Ascites Cells and Ascites volume. VEGF protein was localized to theca Cells of normal ovaries, in glandular areas of tumors, and to the cytoplasm of Ascites Cells. Aspirin and a COX-1-specific inhibitor decreased the proliferation of Ascites Cells, whereas a COX-2-specific inhibitor did not. Conclusions. VEGF may play a role in ovarian cancer progression in the hen and the proliferation of Ascites Cells can be decreased by targeting the COX-1 but not COX-2 pathway.
Yun Yang - One of the best experts on this subject based on the ideXlab platform.
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Comparative study of phosphotyrosyl protein phosphatase of mice normal liver, regenerating liver, and mice H22a hepatoma Ascites Cell
Chinese Journal of Cancer Research, 1991Co-Authors: Yuhuan Wang, Yun YangAbstract:In regenerating liver of mice, marked increase of the activity of phosphotyrosyl protein phosphatase (PTPP) in cytosol was observed. The PTPP activity varied with time and reached the highest level between 24 to 48 hours after partial hepatectomy. In H22a Cells the PTPP activity found in every subCellular fraction was lower than that of the normal liver. The PTPP activity was mostly concentrated in lysosomes of normal liver, but mainly distributed in nucleus, cytosol and microsome of regenerating liver. In H22a Cells PTPP activity seemed distribute evenly. Five similar major PTPP peaks (I–V) were obtained on DEAE Cellulose chromatography of cytosols from all three of liver Cells studied. However, two additional PTPP peaks, a and b, were also obtained from cytosol of liver.
Yvette Melander - One of the best experts on this subject based on the ideXlab platform.
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probing the structure of mouse ehrlich Ascites Cell 5 8s 18s and 28s ribosomal rna in situ
Nucleic Acids Research, 1994Co-Authors: Lovisa Holmberg, Yvette Melander, Odd NygardAbstract:The secondary structure of mouse Ehrlich Ascites 18S, 5.8S and 28S ribosomal RNA in situ was investigated by chemical modification using dimethyl sulphate and 1-cyclohexyl-3-(morpholinoethyl) carbodiimide metho-p-toluene sulphonate. These reagents specifically modify unpaired bases in the RNA. The reactive bases were localized by primer extension followed by gel electrophoresis. The three rRNA species were equally accessible for modification i.e. approximately 10% of the nucleotides were reactive. The experimental data support the theoretical secondary structure models proposed for 18S and 5.8/28S rRNA as almost all modified bases were located in putative single-strand regions of the rRNAs or in helical regions that could be expected to undergo dynamic breathing. However, deviations from the suggested models were found in both 18S and 28S rRNA. In 18S rRNA some putative helices in the 5'-domain were extensively modified by the single-strand specific reagents as was one of the suggested helices in domain III of 28S rRNA. Of the four eukaryote specific expansion segments present in mouse Ehrlich Ascites Cell 28S rRNA, segments I and III were only partly available for modification while segments II and IV showed average to high modification.
