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  • Mauro Pessia, Paola Imbrici, Maria Cristina D’Adamo, Lorena Salvatore, Stephen J. Tucker
  • Medicine, Chemistry
  • The Journal of physiology
  • 2001 (First Publication: 1 April 2001)
  • 1. The inwardly rectifying potassium channel Kir5.1 appears to form functional channels only by coexpression with either Kir4.1 or Kir4.2. Kir4.1-Kir5.1 heteromeric channels have been shown to existExpand
  • Stephen J. Tucker, Chris T. Bond, Patrick Herson, Mauro Pessia, John P Adelman
  • Medicine, Biology
  • The Journal of Biological Chemistry
  • 1996 (First Publication: 8 March 1996)
  • Inwardly rectifying K channel subunits may form homomeric or heteromeric channels with distinct functional properties. Hyperpolarizing commands delivered to Xenopus oocytes expressing homomeric K 4.1Expand
  • Stephen J. Tucker, Paola Imbrici, Lorena Salvatore, Maria Cristina D’Adamo, Mauro Pessia
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • 2000 (First Publication: 2 June 2000)
  • The physiological role of the inwardly rectifying potassium channel, Kir5.1, is poorly understood, as is the molecular identity of many renal potassium channels. In this study we have usedExpand
  • Federico Sicca, Paola Imbrici, Maria Cristina D’Adamo, F Moro, Mauro Pessia
  • Biology, Medicine
  • Neurobiology of Disease
  • 2011 (First Publication: 1 July 2011)
  • The inwardly-rectifying potassium channel Kir4.1 is a major player in the astrocyte-mediated regulation of [K(+)](o) in the brain, which is essential for normal neuronal activity and synapticExpand
  • Maria Grazia Sacco Casamassima, Maria Cristina D’Adamo, Mauro Pessia, Stephen J. Tucker
  • Chemistry, Medicine
  • Journal of Biological Chemistry
  • 2003 (First Publication: 31 October 2003)
  • Heteromultimerization between different potassium channel subunits can generate channels with novel functional properties and thus contributes to the rich functional diversity of this gene family.Expand