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Organellar proteomics of the Golgi apparatus and Golgi derived COPI vesiclesAu, Catherine Elaine. January 1900 (has links)
Thesis (Ph.D.). / Written for the Dept. of Anatomy and Cell Biology. Title from title page of PDF (viewed 2008/05/08). Includes bibliographical references.
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An analysis of Golgi structure and inheritance in budding yeast /Walton, Olivia A. January 2000 (has links)
Thesis (Ph. D.)--University of Chicago, Dept. of Molecular Genetics and Cell Biology. / Includes bibliographical references. Also available on the Internet.
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Biogenesis and dynamics of the early secretory pathway in Pichia pastoris /Bevis, Brooke J. January 2002 (has links)
Thesis (Ph. D.)--University of Chicago, Pritzker School of Medicine, Department of Molecular Genetics and Cell Biology, June 2002. / Includes bibliographical references. Also available on the Internet.
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Analysis of the localization of Pichia pastoris Sec12p to transitional endoplasmic reticulum sites /Soderholm, Jonathan F. January 2003 (has links)
Thesis (Ph. D.)--University of Chicago, Dept. of Molecular Genetics and Cell Biology, June 2003. / Includes bibliographical references. Also available on the Internet.
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The role of the AP-1 adaptor complex in trafficking between the trans-Golgi Network and endosomal systemFoote, Christopher, January 2005 (has links)
Thesis (Ph. D.)--University of Missouri-Columbia, 2005. / The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file viewed on (November 7, 2006) Vita. Includes bibliographical references.
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Subcellular localization of plant vacuolar sorting receptor proteins and their roles in mediating protein degradation during seed germination. / CUHK electronic theses & dissertations collection / Digital dissertation consortiumJanuary 2003 (has links)
by Yubing Li. / "September 2003." / Thesis (Ph.D.)--Chinese University of Hong Kong, 2003. / Includes bibliographical references (p. 173-190). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Electronic reproduction. Ann Arbor, MI : ProQuest Information and Learning Company, [200-] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Mode of access: World Wide Web. / Abstracts in English and Chinese.
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Functional characterization of the secretory pathway and the role of COPI vesicles /Hiding, Johan, January 2007 (has links)
Diss. (sammanfattning) Göteborg : Göteborgs universitet, 2007. / Härtill 3 uppsatser.
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Using RNA interference to study the function of the tethering protein p115 in ER-Golgi trafficGrabski, Robert. January 2008 (has links) (PDF)
Thesis (Ph. D.)--University of Alabama at Birmingham, 2008. / Title from first page of PDF file (viewed Feb. 12, 2009). Includes bibliographical references.
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Golgi specificity and development of autoreactive B cellsNawazi, Fazlullah Salar Khan, January 2008 (has links) (PDF)
Thesis (Ph.D.)--University of Tennessee Health Science Center, 2008. / Title from title page screen (viewed on September 9, 2008). Research advisor: Marko Z. Radic, Ph.D. Document formatted into pages (xi,111 p. : ill.). Vita. Abstract. Includes bibliographical references (p. 91-111).
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Golgi pH and glycosylationRivinoja, A. (Antti) 13 October 2009 (has links)
Abstract
Glycans, as a part of glycoproteins, glycolipids and other glycoconjugates, are involved in many vital intra- and inter-cellular tasks, such as protein folding and sorting, protein quality
control, vesicular trafficking, cell signalling, immunological defence, cell motility and adhesion. Therefore, their correct construction is crucial for the normal functioning of eukaryotic cells and
organisms they form. Most cellular glycans are constructed in the Golgi, and abnormalities in their structure may derive, for instance, from alkalinization of the Golgi lumen.
In this work we show that Golgi pH is generally higher and more variable in abnormally glycosylating, i.e. strongly T-antigen (Gal-β1,3-GalNAc-ser/thr) expressing cancer cells, than in
non-T-antigen expressing cells. We also confirmed that the Golgi pH alterations detected in cancer cells have the potential to induce glycosylation changes. A mere 0.2 pH unit increase in Golgi pH is
able to induce T-antigen expression and inhibit terminal N-glycosylation in normally glycosylating cells. The mechanism of inhibition involves mislocalization of the corresponding
glycosyltransferases.
We also studied potential factors that can promote Golgi pH misregulation in health and disease, and found that cultured cancer cells, despite variation and elevation in Golgi pH, are fully
capable of acidifying the Golgi lumen under the normal Golgi pH. Moreover, we introduce a Golgi localized Cl-/HCO3- exchanger, AE2a, that participates in Golgi pH regulation by
altering luminal bicarbonate concentration and thus also buffering capacity. Participation of AE2a in Golgi pH regulation is especially intriguing, because it also provides a novel mechanism for
expelling protons from the Golgi lumen.
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