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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.
1

Structure function analysis of the deubiquitylating enzyme Fam

Khut, Poon-Yu January 2006 (has links)
The ubiquitin pathway is a highly conserved post-translational modification system best characterised for its roles in protein degradation and intracellular trafficking and is involved in a diverse spectrum of cellular processes. Ubiquitylation is opposed by deubiquitylating enzymes (Dubs), and the ubiquitin specific peptidase (USP) class of Dubs remove ubiquitin from specific substrates, thereby affecting protein fate. USPs exhibit broad sequence diversity except over their catalytic cores and it has been suggested that this sequence variation constitutes their individual substrate-specific binding sites. Fat Facets in Mouse (Fam) is a developmentally regulated USP whose function is crucial for mouse pre-implantation development. Fam is expressed in a complex fashion throughout development in a number of diverse tissue types and time points, well beyond its critical role in the early embryo. Fam's orthologue in fly, Fat Facets (faf) is also developmentally regulated and is required for both drosophila eye and syncytial stage development. Given the strengths of the zebrafish system as a developmental tool, the zebrafish orthologue of Fam, usp9 was identified and found to be highly conserved. Analysis of its expression pattern found considerable overlap with the published mouse patterns. Given the similarities between the mouse and zebrafish systems, a series of cross-species experiments were conducted to determine whether exogenous expression of highly conserved regions of FAM, could cause dominant-negative phenotypes in developing zebrafish embryos. Outside of the catalytic core, FAM's large N and C-terminal extensions consist of novel sequence bearing no similarity to any known domain. To delineate FAM domains, fulllength FAM was expressed in insect cells and subjected to partial proteolysis. Combining this data with recent structural predictions and computer analyses of the FAM sequence, four FAM domains were characterised with the first domain containing three possible subdomains. The predominant helical nature of the N and C-terminal extensions of FAM were predicted to form scaffolding structures, well suited to protein binding. / Thesis (M.Sc.)-- University of Adelaide, School of Molecular and Biomedical Science, 2006.
2

Novel anti-interferon mechanism : influenza B virus both induces and blocks the activity of the ubiquitin-like ISG15 protein /

Yuan, Weiming, January 2000 (has links)
Thesis (Ph. D.)--University of Texas at Austin, 2000. / Vita. Includes bibliographical references (leaves 85-98). Available also in a digital version from Dissertation Abstracts.
3

A functional analysis of the mammalian E3 ubiquitin ligase WWP1 in a yeast model

Sankaran, Saumya M. January 2009 (has links)
Thesis (M.S.)--Brandeis University, 2009. Senior honors thesis--Brandeis University, 2009. / Title from PDF title page (viewed on June 29, 2009). Includes bibliographical references.
4

Control of mitotic progression by components of two ubiquitin systems /

Topper, Leana Miller. January 2001 (has links)
Thesis (Ph. D.)--University of Virginia, 2001. / Includes bibliographical references (leaves 170-194). Also available online through Digital Dissertations.

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