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          <dc:identifier>https://hdl.handle.net/2286/R.I.16831</dc:identifier>
                  <dc:rights>http://rightsstatements.org/vocab/InC/1.0/</dc:rights>
                  <dc:date>2013-05</dc:date>
                  <dc:format>24 pages</dc:format>
                  <dc:language>eng</dc:language>
                  <dc:contributor>Alam, Now Bahar</dc:contributor>
          <dc:contributor>Sierks, Michael</dc:contributor>
          <dc:contributor>Pauken, Christine</dc:contributor>
          <dc:contributor>Williams, Stephanie</dc:contributor>
          <dc:contributor>Barrett, The Honors College</dc:contributor>
          <dc:contributor>Department of Psychology</dc:contributor>
          <dc:contributor>Harrington Bioengineering Program</dc:contributor>
                  <dc:type>Text</dc:type>
                  <dc:description>Misfolding and aggregation of alpha-synuclein (a-syn) has been strongly correlated with the pathogenesis of Parkinson&#039;s disease (PD). Reagents such as single chain antibody fragments (scFv) that can interact with specific aggregate forms of a-syn can be very useful to study how different aggregate forms affect cells. Here we utilize two scFvs, D5 and 10H, that recognize two distinct oligomeric forms of a-syn to characterize the presence of different a-syn aggregates in animal models of PD.</dc:description>
                  <dc:subject>Neurotoxin Cell Model of Parkinson&#039;s Disease</dc:subject>
          <dc:subject>Therapeutic Antibodies</dc:subject>
          <dc:subject>Transgenic Mice Model</dc:subject>
          <dc:subject>THY-1</dc:subject>
          <dc:subject>Parkinson&#039;s disease</dc:subject>
                  <dc:title>Detecting Oligomeric Forms of Alpha-Synuclein in Cell and Mouse Tissue</dc:title></oai_dc:dc></metadata></record></GetRecord></OAI-PMH>
