Thesis (Ph. D.)--Ohio State University, 2008. / Title from first page of PDF file. Includes vita. Includes bibliographical references (p. 99-109).

Thesis (doctoral)--University of Uppsala, 1984. / Includes bibliographical references (p. 29-37).

Theses (M.S.)--Marshall University, 2006. / Title from document title page. Includes abstract. Document formatted into pages: contains viii, 87 p. including illustrations. Bibliography: p. 78-86.

Thesis (Ph. D.)--Florida State University, 2005. / Advisor: Timothy S. Moerland, Florida State University, College of Arts and Sciences, Dept. of Biological Science. Title and description from dissertation home page (viewed May 11, 2006). Document formatted into pages; contains viii, 76 pages. Includes bibliographical references.

No description available.

Shope fibroma virus (SFV) N1R is a member of a family of poxvirus proteins that is associated with virulence and largely defined by the presence of a C-terminal RING finger motif and localization to virus factories within the cytoplasm of infected cells. Altered proteins, with deletions and site-specific mutations, were transiently expressed in vaccinia virus infected cells to discern regions of the protein that are required for localization. Deletion mutagenesis implicated a requirement of a small central region of the RING for localization, but the RING motif alone was not sufficient. A chimeric protein, however, in which the RING motif of the herpes simplex virus-1 ICP0 protein replaced the SFV N1R RING motif did localize to virus factories, indicating that the specificity for factory localization resided outside the RING motif of N1R. Critical evaluation of an alignment of poxviral N1R homologs identified a short, highly conserved N-terminal sequence 24-YINIT-28. When this sequence was deleted from N1R localization was abolished. Recombinant N1R protein isolated from vaccinia virus (VV) infected cells bound to calf-thymus DNA cellulose. Elution from this matrix required 0.5–0.75M NaCl, suggesting N1R localizes to the factory through an inherent DNA binding activity. Structural prediction analysis inferred that the conserved N-terminal region required for N1Rs factory localization forms a short β strand and subsequent alignment analysis with β sheet DNA binding proteins uncovered significant homology with the ribbon-helix-helix motif family which utilize a short β sheet for specific DNA interaction. Characterization of the factory localization of five N1R mutants, each having a single potential β strand residue replaced with Ala revealed that Asn 26 was the most important residue for factory localization. In contrast to N1R, which strongly binds DNA and rapidly sediments with the virus factories, SFV-N1RAsn26ΔAla mutant protein was found in the soluble fraction of infected cell lysates and failed to bind DNA cellulose. These results indicate that the N1R RING finger motif may not be central to DNA interactions and that N1R β strand residues particularly Asn 26 are involved in DNA binding and targeting N1R to the virus factories. Overexpression of N1R in vaccinia virus (VV) infected cells was found to inhibit virus induced apoptosis. To clarify the role of N1R protein with respect to apoptosis and to examine whether the related ectromelia virus virulence factor p28 (EVp28) might also play a role in apoptosis protection, a p28-mutant EV virus and the VV-N1R virus were tested for their ability to interfere with apoptosis induced by different signals. VV and EV infection were found to protect cells from Ultra Violet (UV) light, Tumor necrosis factor alpha (TNFα) and anti-Fas induced apoptosis. Expression of SFV N1R and EVp28 however, only protected infected HeLa cells from apoptosis induced by UV light, and did not protect from apoptosis induced by TNFα or anti-Fas antibody. Immunoblot analysis indicated EVp28 blocks processing of procaspase-3 suggesting EVp28 acts upstream of this protease in response to UV induced apoptotic signals. The requirement of EVp28 to promote replication and virulence in vivo may be related to apoptosis suppression because the number of progeny virus harvested from p28-mutant EV virus infected cells compared to wild type EV was similar following mock UV induced apoptosis, but significantly reduced following apoptosis induction by UV. / Graduate

Iron deficiency anaemia is perhaps the most widespread nutritional deficiency disease; as result, the topic of iron absorption has received intensive investigation over a relatively long period of time. Most of the investigative thrust has come from clinical medicine and allied fields, with some associated biochemical investigation. Evidence from the latter has pointed towards the involvement of iron-binding proteins especially ferritin and transferrin in the absorptive process. While the biochemical literature on these two proteins, particularly transferrin, is vast, their roles in iron absorption are obscure. This study was undertaken, therefore, as an investigation into these proteins, their quantitation and role in iron absorption. The physiology of absorption was studied by injection of radiolabelled ferrous ascorbate into isolated intestinal loops and the determination of mucosal, blood and carcass uptake.

Wang, Jia. / Thesis (Ph.D.)--Chinese University of Hong Kong, 2013. / Includes bibliographical references (leaves 99-115). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Abstract also in Chinese.

Cheung, Siu Yuen. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2008. / Includes bibliographical references (leaves 178-200). / Abstracts in English and Chinese. / Abstract --- p.i / Chinese abstract --- p.iii / Acknowledgements --- p.v / Table of contents --- p.vii / Chapter Chapter One --- General Introduction --- p.1 / Chapter 1.1 --- S100 Proteins --- p.1 / Chapter 1.1.1 --- Structure of S100 proteins --- p.2 / Chapter 1.1.2 --- Possible functions of S100 proteins --- p.4 / Chapter 1.1.3 --- Genomic organization of S100 genes --- p.6 / Chapter 1.1.4 --- Clinical importance of S100 proteins --- p.7 / Chapter 1.2 --- S100A1 Protein --- p.8 / Chapter 1.2.1 --- Possible functions of the S100A1 protein --- p.10 / Chapter 1.2.1.1 --- Regulation of cardiac and skeletal muscle contractility --- p.10 / Chapter 1.2.1.2 --- Functional roles in the central nervous system (CNS) --- p.12 / Chapter 1.2.1.3 --- Other possible functions of the S100A1 protein --- p.13 / Chapter 1.2.2 --- S100A1 knockout mice --- p.14 / Chapter 1.2.3 --- Relationships between S100A1 and S100B proteins --- p.16 / Chapter 1.3 --- S100B Protein --- p.18 / Chapter 1.3.1 --- Possible functions of S100B protein --- p.19 / Chapter 1.3.2 --- S100B knockout mice --- p.20 / Chapter 1.4 --- RNA interference --- p.22 / Chapter 1.4.1 --- Mechanisms of RNA interference --- p.24 / Chapter 1.4.2 --- Efficacy and selectivity of siRNA --- p.25 / Chapter 1.4.3 --- siRNA delivery --- p.27 / Chapter 1.5 --- Objective --- p.31 / Figures and legends --- p.34 / Chapter Chapter Two --- S100A1 expression in normal mouse embryos and characterization of S100A1 knockout mouse embryos --- p.40 / Chapter 2.1 --- Introduction --- p.40 / Chapter 2.2 --- Materials and Methods --- p.44 / Chapter 2.2.1 --- Mouse strains --- p.44 / Chapter 2.2.2 --- RNA extraction --- p.46 / Chapter 2.2.3 --- Reverse Transcription-Polymerase Chain Reaction (RT-PCR) --- p.46 / Chapter 2.2.4 --- Protein extraction --- p.48 / Chapter 2.2.5 --- Western blotting --- p.49 / Chapter 2.2.6 --- Immunohistochemical staining --- p.50 / Chapter 2.3 --- Results --- p.53 / Chapter 2.3.1 --- S100A1 mRNA expression in normal mouse embryo --- p.53 / Chapter 2.3.2 --- S100A1 protein expression in normal mouse embryos --- p.55 / Chapter 2.3.2.1 --- Temporal expression of the S100A1 protein --- p.55 / Chapter 2.3.2.2 --- Spatial expression of the S100A1 protein --- p.57 / Chapter 2.3.3 --- Morphological and histological characterization of SI00A1 knockout mouse embryos --- p.60 / Chapter 2.3.4 --- S100B protein expression pattern in Wt and S100A1 KO mouse embryos --- p.62 / Chapter 2.4 --- Discussion --- p.64 / Tables --- p.73 / Figures and legends --- p.76 / Chapter Chapter Three --- Knockdown of S100A1 in S100B in knockout mouse embryos --- p.118 / Chapter 3.1 --- Introduction --- p.118 / Chapter 3.2 --- Materials and Methods --- p.128 / Chapter 3.2.1 --- Mouse strains --- p.128 / Chapter 3.2.2 --- Short-interfering RNA (siRNA) --- p.129 / Chapter 3.2.3 --- In-uterus surgery --- p.130 / Chapter 3.2.4 --- RNA extraction and RT-PCR --- p.132 / Chapter 3.2.5 --- Immunohistochemical staining of S100A1 and S100B --- p.132 / Chapter 3.3 --- Results --- p.133 / Chapter 3.3.1 --- Characterization of S100B knockout mouse embryos --- p.133 / Chapter 3.3.2 --- S100A1 knockdown in S100B wild-type (Wt) mouse embryos --- p.133 / Chapter 3.3.3 --- S100A1 knockdown in S100B knockout (KO) mouse embryos --- p.139 / Chapter 3.4 --- Discussion --- p.146 / Tables --- p.153 / Figures and legends --- p.154 / Chapter Chapter Four --- General Discussion and Conclusions --- p.175 / Reference --- p.178

Thesis (M.S.)--University of Toledo, 2007 / "In partial fulfillment of the requirements for the degree of Master of Science in Biomedical Sciences." Title from title page of PDF document. Bibliography: p. 37-48, 62-84.