<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>Niggli V</dc:creator>
  <dc:creator>Sigel E</dc:creator>
  <dc:date>2008</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Cation-transporting P-type ATPases show a high degree of structural and functional homology. Nevertheless, for many members of this large family, the molecular mechanism of transport is unclear; namely, whether transport is electrogenic or not and if countertransport is involved remains to be established. In a few well-studied cases such as the Na(+)-K(+)-ATPase, plasma membrane Ca(2+) ATPase (PMCA) and sarcoplasmic reticulum Ca(2+) ATPase (SERCA) countertransport has been clearly demonstrated. New data based on the crystal structure of SERCA now strongly indicate that countertransport could be mandatory for all P-type ATPases. This concept should be verified for other known and for all newly characterized P-type ATPases.</dc:description>
  <dc:identifier>https://sonar.ch/global/documents/162353</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.tibs.2007.12.005</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/18343670</dc:relation>
  <dc:source>Trends in biochemical sciences. - 2008</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Biological Transport</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Cation Transport Proteins</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Crystallography, X-Ray</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Electrophysiology</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Humans</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Ion Transport</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Models, Biological</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Plant Proteins</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Plasma Membrane Calcium-Transporting ATPases</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Protein Transport</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Sarcoplasmic Reticulum</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Sarcoplasmic Reticulum Calcium-Transporting ATPases</dc:subject>
  <dc:title xmlns:ns14="xml" ns14:lang="en">Anticipating antiport in P-type ATPases.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>