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    <link>http://hdl.handle.net/2436/6295</link>
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    <pubDate>Sat, 18 May 2013 22:35:53 GMT</pubDate>
    <dc:date>2013-05-18T22:35:53Z</dc:date>
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      <title>Case study of Felty’s Syndrome</title>
      <link>http://hdl.handle.net/2436/30258</link>
      <description>Title: Case study of Felty’s Syndrome
Authors: Nelson, Paul N.; Bowman, S.J.
Abstract: This book: is an introductory level text on the biological principles of human disease. The book is aimed at medical students in degree courses in biomedical science.  The book fuses the biological (physiological and biochemical) processes which underlie the clinical manifestations of disease.  As such, it brings together material which is conventionally dealt with by several books. The authors have covered the fundamentals of each topic in a readable manner, which should encourage students to develop a fuller understanding, where necessary, by reference to more comprehensive texts.</description>
      <pubDate>Mon, 01 Jan 2001 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://hdl.handle.net/2436/30258</guid>
      <dc:date>2001-01-01T00:00:00Z</dc:date>
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      <title>Generating monoclonal antibody probes and techniques for characterizing and localizing reactivity to antigenic determinants</title>
      <link>http://hdl.handle.net/2436/30257</link>
      <description>Title: Generating monoclonal antibody probes and techniques for characterizing and localizing reactivity to antigenic determinants
Authors: Nelson, Paul N.
Abstract: This book: Epitope Mapping covers all the major methods for the identification and definition of epitopes. The Pepscan assay is used to define B cell epitopes and makes use of synthetic peptides but can only be used if the amino acid sequence is known. It can be adapted for the delineation of both helper T cells and cytotoxic T cells. The identification of combined B and T cell epitopes can also be achieved using synthetic peptides. There are other methodologies for analysing for cytotxic T cell epitopes such as the purification of antigens presented by MHC class I molecules and expression cloning. Site directed mutagenesis is also a powerful tool in epitope mapping and can be used to evaluate the role of single amino acids in immune complex formation. Protein footprinting makes use of monoclonal antibodies produced by hybridoma technology and relies on the fact that the epitope is protected from cleavage when bound as an antibody-antigen complex. It is only useful for small antigens. Other monoclonal antibody assays such as enzyme linked immunosorbent assay and haemaglutination and slot-blotting may also be used in epitope mapping. Random phage display libraries bring together the genetic and amino acid peptide sequence and can be screened with antibody and the resulting peptide DNA sequenced to confirm the amino acid sequence of a specific eptiope. Investigation of carbohydrates can also be useful to eptitope mapping as deglycosylation can lead to loss of antigenic activity. Epitopes are important to the pharmaceutical industry and wherever appropriate, pharmaceutical applications of the methods described are included. For each method there is a description of the technology, protocols, trouble-shooting, and advice on when to use the method. This book will therefore be invaluable to any researcher involved in epitope mapping.</description>
      <pubDate>Mon, 01 Jan 2001 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://hdl.handle.net/2436/30257</guid>
      <dc:date>2001-01-01T00:00:00Z</dc:date>
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      <title>Monoclonal antibodies: The tools of the trade within biomedical science</title>
      <link>http://hdl.handle.net/2436/30256</link>
      <description>Title: Monoclonal antibodies: The tools of the trade within biomedical science
Authors: Nelson, Paul N.; Astley, S.J.; Warren, Phil
Abstract: This book: The latest edition of this highly successful text, covers the major advances in the methods used in cellular and molecular pathology. In recent years, knowledge of the molecular organization of the cell has led to the development of powerful new techniques that bring greater accuracy and objectives to the diagnosis, prognosis and management of many diseases and to the study of pathological states. This book describes the latest molecular techniques available for the analysis of diseases. In particular it includes new techniques using fluorescent dyes, DNA microarrays, protein chemistry, and mass spectrometry. It also incorporates information from the Human Genome Project, and the new disciplines of genomics and proteomics, where relevant to pathology. Color plates are a new feature of this edition, illustrating the advances in fluorescence labeling of cells.</description>
      <pubDate>Wed, 01 Jan 2003 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://hdl.handle.net/2436/30256</guid>
      <dc:date>2003-01-01T00:00:00Z</dc:date>
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      <title>Generation and characterization of monoclonal antibodies to the neural crest.</title>
      <link>http://hdl.handle.net/2436/30255</link>
      <description>Title: Generation and characterization of monoclonal antibodies to the neural crest.
Authors: Shakil, T.; Richardson, M. K.; Waldron, E.E.; Conde, Gillian; Wood, S.; Bland, Y.; Reynolds, Gary; Murray, Paul G.; Nelson, Paul N.
Abstract: The generation of monoclonal antibodies (MAbs) specific for quail neural crest may provide valuable tools for studying the differentiation of embryonic precursor cells. Unfortunately, relatively few antibodies are available because of the difficulty in obtaining sufficient cells for in vivo immunization strategies. We have overcome this problem by using intrasplenic immunization with formaldehyde-fixed cells harvested from neural crest cultures. In addition, booster injections of cultured whole-embryo cells were administered intraperitoneally. Following two fusions, a total of 18 hybridomas were generated with antibody reactivity to the cytoplasm of neural crest cells. Furthermore, 32 were reactive against both somite (a noncrest mesodermal control) and crest cultures, whilst 15 were not reactive. Out of those hybridomas reactive with neural crest, six designated 160D, 164D, OE, 12E, 120E and 124E were further characterized. Interestingly MAb supernatants OE, 12E, 120E, and 124E exhibited reactivity against some but not all neural crest cells suggesting that they might recognise subpopulations. Immunoglobulin isotyping of supernatants revealed that 4 (160D, 164D, OE, and 120E) were IgM and 2 (12E and 124E) were IgG(2b). On assessing their reactivity against human tissue sections, all six hybridoma supernatants cross-reacted with neuroendocrine cells within appendix, colon and rectum. These MAbs could provide novel reagents for the understanding of neural crest development.</description>
      <pubDate>Mon, 01 Jan 2001 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">http://hdl.handle.net/2436/30255</guid>
      <dc:date>2001-01-01T00:00:00Z</dc:date>
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