Global ETD Search

41	Self-Incompatibility in African Lycium (Solanaceae) Feliciano, Natalie M 01 January 2008 (has links) (PDF) Chapter one of my thesis has been published in the May 2008 issue of the journal Evolution under the title “A TALE OF TWO CONTINENTS: BAKER’S RULE AND THE MAINTENANCE OF SELF-INCOMPATIBILITY IN LYCIUM (SOLANACEAE).” This chapter was co-authored by Dr. Jill S. Miller and Dr. Rachel Levin. self-incompatibility evolution Lycium Baker's Rule SLF S-RNase Biology
42	The Antiviral and Antitumor Function of RNase L Li, Geqiang 13 October 2004 (has links) No description available. Biology, Molecular RNase 2-5A JNK FAK Cell Integrin Apoptosis
43	SUBSTRATE SPECIFIC CONTRIBUTIONS OF THE PROTEIN SUBUNIT OF E.COLI RNASE P TO SUBSTRATE RECOGNITION AND CATALYSIS SUN, LEI January 2008 (has links) No description available. Biology, Molecular RNase P C5 protein substrate recognition catalysis
44	Fluor-labeling of RNA and Fluorescence-based Studies of Precursor-tRNA Cleavage by Escherichia coli Ribonuclease P Wallace, Andrew J. 24 October 2013 (has links) No description available. Biochemistry RNase P Ribonuclease P Click Chemistry high-throughput screening
45	Role of RNase L in Inducing Autophagy and Regulating the Crosstalk from Autophagy to Apoptosis Siddiqui, Mohammad Adnan January 2015 (has links) No description available. Molecular Biology Virology RNase L, Autophagy, Apoptosis, Beclin-1
46	Elucidating the role of protein cofactors in RNA catalysis using ribonuclease P as the model system Tsai, Hsin-Yue 15 March 2006 (has links) No description available. Bacterial/archaeal RNase P RNA-protein interactions RNP reconstitution
47	Biochemical studies on archaeal ribonuclease P reveal thematic convergence in protein-facilitated RNA catalysis Pulukkunat, Dileep K. 14 April 2008 (has links) No description available. Biochemistry Chemistry RNase P RNP complex ptRNA processing
48	Structure and Interactions of Archaeal RNase P Proteins: RPP29 and RPP21 Xu, Yiren 23 August 2010 (has links) No description available. Biochemistry RNase P Protein-protein interaction NMR spectroscopy ITC
49	Defective tRNA Processing by RNase P Contributes to Neurodegeneration in Mice Lai, Stella Myra 12 October 2017 (has links) No description available. Anatomy and Physiology Biochemistry Molecular Biology RNase P tRNA processing neurodegeneration
50	Studies on human ribonuclease H1 and its action on 2'-fluoroarabinose oligonucleotide hybrid substrates Alla, Nageswara Rao January 2012 (has links) Ribonuclease H1 is a conserved enzyme that is localized in the nuclear and mitochondrial compartments of eukaryotic cells, and functions in DNA replication, repair, recombination and transcription. (Arunachandran et al., 2000; Cerritelli et al., 2003) Oligonucleotide binding to a complementary RNA sequence can provide a substrate for RNase H1, and provides the mechanistic basis for antisense oligonucleotide (AON)-directed gene silencing in cells (Opalinska et al., 2002). Effective evaluation of the therapeutic efficacy of next-generation AONs with novel structures requires an in vitro system involving, purified, highly active RNase H1 of human cells, and a full understanding of the catalytic mechanism of the enzyme. The goal of project 1 described in chapter 3, was to determine the involvement of a conserved Histidine (H264) in the catalytic mechanism of human RNase H1. Based on this analysis I was able to conclude that H264 has a dual role in phosphodiester hydrolysis and in product release. The goal of project 2 (Chapter 4) was to examine the reactivities towards human RNase H1 of model hybrid substrates containing specific types of 2'-FANA substitutions (abbreviated as `F', with 2'-deoxyribose abbreviated as `D'), either at the "wings" of the molecule ("7-gapmer"; each wing=7 nt: FFFFFFF-DDDDDDD-FFFFFFF), or with 3 nt alternations ("3-altimer": FFF-DDD-FFF-DDD-FFF-DDD-FFF). The results of this study strongly support the continued examination of the potential therapeutic utility of the 2'-FANA modification in AONs. The highly efficient and selective inhibition of protein expression is a primary basis of action of most antisense therapeutic strategies. These data suggest that the 2'-FANA modification supports sustained silencing after a single administration, either by mRNA cleavage or by a translational block, and at substantially lower concentrations compared to the unmodified AON. The results of this project underscore the proposal that 2'-FANA-modified AONs will be important additions to the repertoire of rational antisense strategies for the effective treatment of disease. / Chemistry Chemistry Biochemistry 2'-fana Antisense C-myb Rnase H1

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