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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
81

The metabolism of tRNAAspargine in the friend erthroleukemia cell /

Miller, Harvey January 1992 (has links)
No description available.
82

New methods for the chemical synthesis of ribonucleotides and their analogues : a thesis

Nemer, Mona J. January 1981 (has links)
Note:
83

In vitro effects of insulin on RNA synthesis in isolated rat hepatocytes

Baltes, Marsha Lynne January 1978 (has links)
This document only includes an excerpt of the corresponding thesis or dissertation. To request a digital scan of the full text, please contact the Ruth Lilly Medical Library's Interlibrary Loan Department (rlmlill@iu.edu).
84

Cis and trans reactions of a self-splicing group II intron /

Jarrell, Kevin A. January 1987 (has links)
No description available.
85

Post-transcriptional modifications of oat coleoptile ribonucleic acid : 5'-terminal capping and methylation of internal nucleosides in poly(A) RNA /

Haugland, Richard Alan January 1978 (has links)
No description available.
86

NonO is a multifunctional protein that associates with RNA polymerase II and induces senescence in malignant cell lines

Xie, Weijun. January 2002 (has links)
Thesis (Ph. D.)--University of Texas at Austin, 2002. / Vita. Includes bibliographical references. Available also from UMI Company.
87

Demonstration of specific physical interaction between CHOP mRNA and intracellular proteins

Chan, Yin-tung, Crystal., 陳燕彤. January 2011 (has links)
The ability of a cell to respond precisely to environmental stress depends on the expression of a large number of genes in a finely coordinated manner. One of such genes is CHOP that encodes the CCAAT/Enhancer-Binding Protein Homologous Protein. CHOP is usually expressed to mediate apoptosis under the condition of excessive stress. The expression of CHOP therefore has to be stringently regulated as its expression will determine the fate of a cell under stress. The expression of many genes is regulated at the posttranscriptional level through the metabolism of their mRNA, such as maturation, transport, storage, and degradation of mRNA. Many metabolic processes of mRNA are known to be mediated by RNA-binding proteins that specifically interact with the mRNA. RNA-binding proteins that interact with the CHOP mRNA have until present not been identified. The aim of this study is to investigate what proteins may bind specifically to CHOP mRNA. The study will enable further understanding regarding how the expression of CHOP is regulated in cellular stress response. Proteins extracted from HeLa cells were incubated with a 335bp [3H]-labelled CHOP RNA probe that spans over a part of the coding region and the 3’UTR of CHOP mRNA. Sucrose density gradient ultracentrifugation revealed that after incubation with proteins extracted from HeLa cells, the sedimentation rate of the [3H]-CHOP RNA probe was significantly higher than that of the free [3H]-RNA probe. The formation of heavy molecular complexes involving the [3H]-CHOP RNA probe was therefore suggested. However, no increase in sedimentation rate of the [3H]-CHOP RNA probe was observed in the presence of an excess of unlabelled CHOP RNA probe. Similar observations were made when the experiments were performed using proteins isolated from cells treated with As2O3. Two putative sequence elements, the Adenylate-Uridylate-Rich Element (ARE) and the Putative Regulatory Element (PRE) located respectively in the 3’UTR and coding region of the CHOP mRNA were then examined for their involvement in RNA-protein interaction. The deletion of ARE and/or PRE, from the [3H]-CHOP RNA probe had little effect on the binding of the RNA probe to the HeLa cell proteins. Consistently, unlabelled CHOP RNA probes with the same deletions were only slightly weaker in competing with the intact [3H]-CHOP RNA probe to bind to HeLa cell proteins. Human Antigen R (HuR) was identified by Western blot analysis to be present in the proteins that were obtained by pull-down assays using biotinylated CHOP RNA as a probe. The deletion of ARE and/or PRE resulted in a slight reduction of HuR obtained by pull down assays. This study provides the first evidence that physical binding interaction occurs between intracellular RNA-binding proteins and CHOP mRNA. More importantly, one such protein is HuR. Data suggest that HuR binding to the CHOP mRNA is mediated by sequences in the CHOP mRNA other than ARE and PRE. / published_or_final_version / Biochemistry / Master / Master of Philosophy
88

Snu40p and Snu66p are required for spliceosome activation at suboptimal temperatures

Roth, Andrew Adam 29 August 2008 (has links)
In addressing the pre-mRNA substrate, the splicing machinery requires rearrangement of multiple RNA and protein components. The classical model of spliceosome formation begins with the U1 snRNA recognition of the 5" splice site and U2 snRNP interaction with the branch point. This process is followed by the engagement of a pre-assembled U4/U6·U5 tri-snRNP to form the A2-1 complex. The spliceosome is subsequently activated through a number of structural rearrangements. Among these is the unwinding of the U4/U6 intermolecular helix by the tri-snRNP component Brr2p. While numerous protein components of the tri-snRNP have been identified, the function of many of these remain unknown. The nonessential Snu66p (U4/U6·U5-110K in humans) stably associates only with the U4/U6·U5 tri-snRNP while the similarly nonessential Snu40p (U5-52K in humans) associates exclusively with the U5 snRNP. To understand why two non-essential pre-mRNA splicing factors have been so well conserved through great evolutionary distances, we examined their roles in the assembly and function of the tri-snRNP. Removal of SNU40 alone does not affect snRNP levels, however deletion of SNU66 results in reduced levels of tri-snRNP. The U4/U6·U5 snRNPs in [Delta]snu66 cells are resistant to the ATP-dependent U4/U6 unwinding by Brr2p, and profound U4/U6 accumulation occurs at reduced temperatures. Remarkably, subsequent removal of SNU40 in a [Delta]snu66 strain bypasses the tri-snRNP formation defect while unwinding of U4/U6 remains defective. Additional investigation revealed that Prp6p, another tri-snRNP protein, is destabilized from the complex. Based upon this data in total, I present a model in which Snu40p and Snu66p interact sequentially with Prp6p to maintain directionality for proper biogenesis of the tri-snRNP. Further, the U4/U6 unwinding defect of the double mutant should theoretically arrest the A2-1 spliceosome. Indeed, native gel analysis confirms the buildup of a large complex later determined to be A2-1. I have purified this complex, functionally tested its catalytic viability, and identified its components via mass spectrometry. This is the first full characterization of the A2-1 precatalytic spliceosome complex in Saccharomyces cerevisiae. / text
89

NonO is a multifunctional protein that associates with RNA polymerase II and induces senescence in malignant cell lines

Xi, Weijun 09 May 2011 (has links)
Not available / text
90

Genetic analysis of RNA splicing in the thymidylate synthase gene of bacteriophage T4

Brown, Michael Dean 12 1900 (has links)
No description available.

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