Thesis (Ph. D.)--Northeastern University, 2008. / Title from title page (viewed Mar. 24, 2009). Graduate School of Arts and Sciences, Dept. of Chemistry and Chemical Biology. Includes bibliographical references (p. 173-176).

Thesis (M.S. in environmental science)--Washington State University, August 2009. / Title from PDF title page (viewed on Aug. 7, 2009). "School of Earth and Environmental Sciences." Includes bibliographical references (p. 85-94).

Thesis (M. Med. Sc.)--University of Hong Kong, 2004. / Also available in print.

Thesis (Ph. D.)--Washington State University, December 2006. / Includes bibliographical references.

Thesis (Ph. D.)--Ohio State University, 2007. / Title from first page of PDF file. Includes bibliographical references (p. 107-128).

Yes / Today, practical, functional and symbolic choices inform the selection of raw materials for worked objects. In cases where we can discern the origin of worked bone, tooth, ivory and antler objects in the past, we assume that similar choices are being made. However, morphological species identification of worked objects is often impossible due to the loss of identifying characteristics during manufacture. Here, we describe a novel non-destructive ZooMS (Zooarchaeology by Mass Spectrometry) method which was applied to bone points from Pre-Contact St. Lawrence Iroquoian village sites in southern Quebec, Canada. The traditional ZooMS technique requires destructive analysis of a sample, which can be problematic when dealing with artefacts. Here we instead extracted proteins from the plastic bags in which the points had been stored. ZooMS analysis revealed hitherto unexpected species, notably black bear (Ursus americanus) and human (Homo sapiens sapiens), used in point manufacture. These surprising results (confirmed through genomic sequencing) highlight the importance of advancing biomolecular research in artefact studies. Furthermore, they unexpectedly and exceptionally allow us to identify and explore the tangible, material traces of the symbolic relationship between bears and humans, central to past and present Iroquoian cosmology and mythology. / Wellcome Trust (grant number 104911/Z/14/); the Leverhulme Trust through a Philip Leverhulme Prize (grant number DNRF128); and the Social Sciences and Humanities Research Council of Canada (SSHRC) through an Insight Development Grant (430-2014-00558)

Dystroglycan is a ubiquitous protein that links the extracellular matrix to the cytoskeleton and is the central unit of the dystrophin glycoprotein complex (DGC), a membrane complex that connects the cytoskeleton to the extracellular matrix (ECM). Dystroglycan is composed of two subunits that are tightly but non-covalently linked. alpha Dystroglycan (alpha DG) is located extracellularly and it is the only component of the DGC linked to the ECM, while beta Dystroglycan (beta DG) spans the plasma membrane and has both an extracellular and a cytoplasmic domain. The DGC is involved in skeletal muscle maintenance and viability, and in the organization and stabilization of the neuromuscular junction, but its function in brain is poorly understood. DGC components are target of several protein kinases, indicating that they are involved in cell signalling pathways. The finding of new dystroglycan interacting proteins could help to obtain some insights in its function in brain tissues. Previous immunoprecipitation and pull down experiments have been used to identify proteins interacting with the cytoplasmic tail of beta DG in brain tissues. Here, we attempt to extend the use of these techniques by using pull down experiments performed with the Glutathione-S-transferase (GST) fusion expression system as a tool for the proteomic analysis of Dystroglycan interacting proteins in the brain.

No description available.

Wu, Ting. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2011. / Includes bibliographical references (leaves 56-70). / Abstracts in English and Chinese. / ACKNOWLEDGEMENTS --- p.Ill / ABSTRACT --- p.V / TABLE OF CONTENTS --- p.IX / LIST OF ABBREVIATIONS --- p.XII / Chapter CHAPTER 1. --- LITERATURE REVIEW --- p.1 / Chapter 1.1 --- THE DISEASE OF MALARIA --- p.1 / Chapter 1.1.1 --- Pathogenesis --- p.2 / Chapter 1.1.2 --- The treatment of malaria --- p.4 / Chapter 1.2 --- THE PLANT OF ARTEMISIA ANNUA L --- p.5 / Chapter 1.2.1. --- Horticulture --- p.5 / Chapter 1.2.2. --- Historical Importance --- p.6 / Chapter 1.3 --- ARTEMISININ --- p.7 / Chapter 1.3.1 --- The content and distribution of artemisinin --- p.7 / Chapter 1.3.2 --- The biosynthesis of artemisnin --- p.8 / Chapter 1.4 --- TRICHOMES --- p.13 / Chapter 1.4.1 --- Structure and function of trichomes --- p.13 / Chapter 1.4.2 --- Trichome investigation in A. annua --- p.14 / Chapter 1.5 --- PROTEOMICS --- p.17 / Chapter 1.5.1 --- The basic principle of proteomics --- p.17 / Chapter 1.5.2 --- Two-dimensional gel electrophoresis --- p.18 / Chapter 1.5.3 --- Mass Spectrometry --- p.19 / Chapter 1.5.4 --- Gel-free proteomics --- p.20 / Chapter 1.6 --- OBJECTIVES --- p.21 / Chapter CHAPTER 2. --- MATERIALS AND METHODS --- p.23 / Chapter 2.1 --- CHEMICALS --- p.23 / Chapter 2.2 --- PLANT MATERIALS --- p.23 / Chapter 2.3 --- ISOLATION OF GLANDULAR TRICHOMES --- p.23 / Chapter 2.4 --- PROTEIN EXTRACTION . --- p.25 / Chapter 2.5 --- Two DIMENSIONAL GEL ELECTROPHORESIS --- p.25 / Chapter 2.6 --- IMAGINE ANALYSIS --- p.26 / Chapter 2.7 --- IN GEL DIGESTION AND PROTEIN IDENTIFICAIOTN BY MASS SPECTROMETRY --- p.27 / Chapter CHAPTER 3. --- RESULTS AND DISCUSSION --- p.29 / Chapter 3.1 --- THE ISOLATION OF GLANDULAR TRICHOMES --- p.29 / Chapter 3.2 --- 2DE PATTERNS OF A. ANNUA LEAVE TRICHOMES AND LEAF TISSUE --- p.32 / Chapter 3.3 --- IDENTIFICATION OF PROTEINS IN GLANDULAR TRICHOMES --- p.34 / Chapter 3.3.1 --- Protein involved in electron transport chain --- p.47 / Chapter 3.3.2 --- Protiens invovled in metabolism --- p.48 / Chapter 3.3.2.1 --- artemisinin biosynthesis --- p.48 / Chapter 3.3.2.2 --- glycolysis --- p.49 / Chapter 3.3.2.3 --- other metabolic enzymes --- p.50 / Chapter 3.3.3 --- Proteins involved in transcription and translation --- p.51 / Chapter 3.3.4 --- Protein involved in proteolysis --- p.51 / Chapter 3.3.5 --- "Detoxificaiton, stress related protein" --- p.52 / Chapter 3.4 --- PERSPECTIVE --- p.53 / Chapter 3.5 --- CONCLUSION --- p.53 / REFERENCES --- p.56

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