<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Merlo A</dc:creator>
  <dc:creator>Bettler B</dc:creator>
  <dc:date>2004</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">The mechanism by which the tumor suppressor PTEN slows tumor cell migration is not well characterized. A recent study by Raftopoulou et al. shows that a lack of PTEN protein phosphatase activity accelerates the migration of glioblastoma cells. The protein phosphatase activity of PTEN is directly or indirectly responsible for dephosphorylating a PTEN residue, threonine-383, which is necessary for slowing cell migration. These findings have implications for the design of new therapies against glioblastomas and other highly invasive cancers.</dc:description>
  <dc:identifier>https://sonar.ch/global/documents/12084</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1126/stke.2292004pe18</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/15100429</dc:relation>
  <dc:source>Science's STKE : signal transduction knowledge environment. - 2004</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Glioblastoma</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Humans</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Neoplasm Invasiveness</dc:subject>
  <dc:title xmlns:ns4="xml" ns4:lang="en">Glioblastomas on the move.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
