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Import of chimeric proteins into plant mitochondriaMahe, Laetitia. January 2001 (has links)
No description available.
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Construction of a single-chain antibody against intermediate filamentsRutherford, Sharon Ann January 1994 (has links)
No description available.
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The expression of neurofilament protein and mRNA levels in the lateral geniculate nucleus and area V1 of the developing and adult vervet monkey (Ceorcopithicus aethiops) /Kogan, Cary. January 1999 (has links)
No description available.
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Phospho-Regulation of Actin Organization and Endocytosis in Yeast by the PP1 Targeting Protein Scd5pChang, Ji Suk January 2005 (has links)
No description available.
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Identification and Characterization of New and Distinct Functional Roles of Posttranscriptional Control Elements in Cytoplasmic Expression of Retroviral RNAHull, Stacey Lynn 20 December 2002 (has links)
No description available.
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Compounds and Methods to Study O-GlcNAc Modification of ProteinsZheng, Hongchao 08 1900 (has links)
<p> A variety of important cell functions rely on O-GlcNAcylation of proteins, a kind of post-translational glycosylation that modifies nuclear and cytoplasmic proteins on serine or threonine residues by the addition of the single sugar moiety β-N-acetylglucosamine (O-GlcNAc). Generally, two enzymes can catalyze the formation and cleavage of the O-GlcNAc O-glycosidic linkage. The O-GlcNAc transferase (OGT) catalyzes the transfer of N-acetylglucosamine from uridine diphosphate N-acetylglucosamine to the hydroxyl group of specific Thr and Ser residues. On the other hand, hydrolysis of the sugar moiety from proteins is achieved via the bi-functional nuclear cytoplasmic O-GlcNAcase and acetyltransferase (NCOAT). Since O-GlcNAcylation plays very important roles in many cell processes such as transcription, translation and protein-protein interaction, my research mainly focused on preparing compounds and developing methods to study the O-GlcNAcylation process and discover the structural information of OGT and NCOAT.</p> <p> In this thesis, the important enzyme substrates (YSDSPSTST for OGT and YSDSP(O-GlcNAc-Ser)TST for NCOAT) were prepared by solid phase synthesis and purified by preparative reverse phase HPLC. Their structure and sequence were confirmed by ESI-MS and tandem MS (MS/MS). The building block S-GlcNAc-Ac3-Ser-COOBn for preparing S-GlcNAcylated peptides was prepared by a multistep procedure. Two potent photoaffinity labeled probes for mapping the active site of sOGT were designed and synthesized, and their IC50 values for sOGT were measured by CapLC and a beta-elimination method. Also, many analytical methods were developed for studying the O-glcNAcylation, including discovering the O-Glycosylation site of peptides by MS/MS and beta-elimination methods, sequencing peptides by MS/MS, analyzing the protein digests by CapLC-MALDI MS and studying the ion mobility of peptides and glycopeptides
using ion mobility spectrometry.</p> / Thesis / Master of Science (MSc)
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The role of TUDOR in Drosophila polar granule assembly and germ cell formationThomson, Travis. January 1900 (has links)
Thesis (Ph.D.). / Written for the Dept. of Biology. Title from title page of PDF (viewed 2008/07/24). Includes bibliographical references.
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The function of the germline rna helicase (GLH) genes in caenorhabditis elegansKuznicki, Kathleen January 2000 (has links)
Thesis (Ph. D.)--University of Missouri--Columbia, 2000. / Typescript. Vita. Includes bibliographical references (leaves 107-112). Also available on the Internet.
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Modulation of nuclear receptor function by interacting proteins /Osman, Waffa, January 2007 (has links)
Diss. (sammanfattning) Stockholm : Karolinska institutet, 2007. / Härtill 4 uppsatser.
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Molecular cloning and characterization of the murine acyl-CoA thioesterase CTE-I /Lindquist, Per J. G., January 2004 (has links)
Diss. (sammanfattning) Stockholm : Karol. inst., 2004. / Härtill 5 uppsatser.
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