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Full-Text Articles in Life Sciences
Phosphorylation Of The Estrogen Receptor Alpha (Erα) At Serine 118 By Phospho-P44/42 Mapk And Regulation By Estrogen And Progesterone In Human Uterine Leiomyoma Tissue And Cells, Tonia Lakisha Hermon
Phosphorylation Of The Estrogen Receptor Alpha (Erα) At Serine 118 By Phospho-P44/42 Mapk And Regulation By Estrogen And Progesterone In Human Uterine Leiomyoma Tissue And Cells, Tonia Lakisha Hermon
Theses and Dissertations in Biomedical Sciences
It is thought that the growth of uterine leiomyomas may be mediated by the interaction of estrogen receptor alpha (ERα) and growth factor pathways and that phosphorylation of ERα at serine 118 (ERα-phospho-Ser118) is important in this interaction. In tissue, immunoblotting and immunohistochemistry were used to investigate the expression of ERα-phospho-Ser118, phosphorylated p44/42 mitogen-activated protein kinase (phospho-p44/42 MAPK), and proliferating cell nuclear antigen (PCNA) in human leiomyoma and myometrial tissues during the proliferative and secretory phases of the menstrual cycle. In vitro studies to assess proliferation of uterine leiomyoma (UtLM) and uterine smooth muscle (UtSMC) cells and expression of ERα-phospho-Ser118 …
Molecular Dynamics Study Of Single Stranded Peptide Nucleic Acids, Anna K. Manukyan
Molecular Dynamics Study Of Single Stranded Peptide Nucleic Acids, Anna K. Manukyan
Theses and Dissertations in Biomedical Sciences
A PNA molecule is a DNA strand where the sugar-phosphate backbone has been replaced by a structurally homomorphous pseudopeptide chain consisting of N(2-aminoethyl)-glycine units. PNA binds strongly to both DNA and RNA. However, an analysis of the X-ray and NMR data show that the dihedral angles of PNA/DNA or PNA/DNA complexes are very different from those of DNA:DNA or RNA:RNA complexes. In addition, the PNA strand is very flexible. One way to improve the binding affinity of PNA for DNA/RNA is to design a more pre-organized PNA structure. An effective way to rigidify the PNA strand is to introduce …
Computational Studies On R67 Dihydrofolate Reductase: An Investigation Into Its Unique Binding Patterns, Chuanyin Shi
Computational Studies On R67 Dihydrofolate Reductase: An Investigation Into Its Unique Binding Patterns, Chuanyin Shi
Theses and Dissertations in Biomedical Sciences
R67 dihydrofolate reductase (R67 DHFR) is a plasmid encoded enzyme which catalyzes the reduction of dihydrofolate (DHF) to tetrahydrofolate (THF) using NADPH as a cofactor. R67 DHFR is a homo-tetramer and D2 symmetric. It contains only one active site, which spans the central channel of the enzyme. The active site can bind either two reactants (DHF), two cofactors (NADPH) or one of each (NADPH/DHF), which is the productive ternary complex (i.e. the complex which yields product). In order to favor formation of the productive complex, this enzyme exhibits binding cooperativity. Unlike other allosteric enzymes which achieve binding cooperativity through conformational …