Paolo Tammaro

• Mechanism of allosteric activation of TMEM16A/ANO1 channels by a commonly used chloride channel blocker.

  Ta CM. et al, (2016), Br J Pharmacol, 173, 511 - 528

• Corrigendum to "Disease-causing mutations associated with four bestrophinopathies exhibit disparate effects on the localization, but not the oligomerization, of Bestrophin-1" [Exp. Eye Res. 121 (2014) 74-85] DOI: 10.1016/j.exer.2014.02.006

  Johnson AA. et al, (2014), Experimental Eye Research, 127

• TMEM16A: A new therapeutic target for diseases of altered blood pressure

  Tammaro P., (2014), ACTA PHYSIOLOGICA, 211, 49 - 49

• Loss of TMEM16A function causes vascular abnormalities in mice

  Garnett H. et al, (2014), ACTA PHYSIOLOGICA, 211, 90 - 90

• Corrigendum to "Disease-causing mutations associated with four bestrophinopathies exhibit disparate effects on the localization, but not the oligomerization, of Bestrophin-1" [Exp. Eye Res. 121 (2014) 74-85] (DOI:10.1016/j.exer.2014.02.006)

  Johnson AA. et al, (2014), Experimental Eye Research

• Disease-causing mutations associated with four bestrophinopathies exhibit disparate effects on the localization, but not the oligomerization, of Bestrophin-1.

  Johnson AA. et al, (2014), Exp Eye Res, 121, 74 - 85

• Coronary spasm and acute myocardial infarction due to a mutation (V734I) in the nucleotide binding domain 1 of ABCC9

  Smith KJ. et al, (2013), International Journal of Cardiology, 168, 3506 - 3513

• Coronary spasm and acute myocardial infarction due to a mutation (V734I) in the nucleotide binding domain 1 of ABCC9.

  Smith KJ. et al, (2013), Int J Cardiol, 168, 3506 - 3513

• Putative pore-loops of TMEM16/anoctamin channels affect channel density in cell membranes.

  Adomaviciene A. et al, (2013), J Physiol, 591, 3487 - 3505

• Putative pore-loops of TMEM16/anoctamin channels affect channel density in cell membranes

  Adomaviciene A. et al, (2013), Journal of Physiology, 591, 3487 - 3505

• Parametrisation of the free energy of ATP binding to wild-type and mutant Kir6.2 potassium channels.

  Moran O. et al, (2013), Biophys Chem, 171, 76 - 83

• Autosomal dominant hypercalciuria in a mouse model due to a mutation of the epithelial calcium channel, TRPV5.

  Loh NY. et al, (2013), PLoS One, 8

• Molecular Modelling and Experimental Analysis of the ATP Sensitivity of Cloned Smooth Muscle KATP Channels

  Chadburn A. et al, (2012), BIOPHYSICAL JOURNAL, 102, 539A - 539A

• TMEM16A/anoctamin 1 protein mediates calcium-activated chloride currents in pulmonary arterial smooth muscle cells.

  Manoury B. et al, (2010), J Physiol, 588, 2305 - 2314

• Vascular K ATP channels: dephosphorylation and deactivation.

  Tammaro P., (2009), Br J Pharmacol, 157, 551 - 553

• A cytosolic factor that inhibits KATP channels expressed in Xenopus oocytes by impairing Mg-nucleotide activation by SUR1.

  Tammaro P. and Ashcroft FM., (2009), J Physiol, 587, 1649 - 1656

• Journal club. A physiologist notes the similarities between animal and plant electricity.

  Tammaro P., (2009), Nature, 458

• Variable phenotypic spectrum of diabetes mellitus in a family carrying a novel KCNJ11 gene mutation.

  D'Amato E. et al, (2008), Diabet Med, 25, 651 - 656

• A Kir6.2 mutation causing severe functional effects in vitro produces neonatal diabetes without the expected neurological complications.

  Tammaro P. et al, (2008), Diabetologia, 51, 802 - 810

• Xenopus oocytes as a heterologous expression system for studying ion channels with the patch-clamp technique.

  Tammaro P. et al, (2008), Methods Mol Biol, 491, 127 - 139

• Neonatal diabetes: The role of KCNJ11 (Kir6.2)

  Tammaro P., (2007), Endocrine Development, 11, 70 - 82

• Functional analysis of two Kir6.2 (KCNJ11) mutations, K170T and E322K, causing neonatal diabetes.

  Tarasov AI. et al, (2007), Diabetes Obes Metab, 9 Suppl 2, 46 - 55

• A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.

  Tammaro P. and Ashcroft FM., (2007), J Physiol, 584, 743 - 753

• The Kir6.2-F333I mutation differentially modulates K-ATP channels composed of SUR1 or SUR2 subunits

  Tammaro P. and Ashcroft F., (2007), JOURNAL OF PHYSIOLOGY-LONDON, 581, 1259 - 1269

• The Kir6.2-F333I mutation differentially modulates KATP channels composed of SUR1 or SUR2 subunits.

  Tammaro P. and Ashcroft F., (2007), J Physiol, 581, 1259 - 1269

• Neonatal diabetes.

  Tammaro P., (2007), Endocr Dev, 11, 70 - 82

• A mutation in the ATP-binding site of the K-ATP channel alters coupling with SUR2A

  Tammaro P. and Ashcroft F., (2007), BIOPHYSICAL JOURNAL, 106A - 106A

• Keeping the heart going: a new role for KATP channels.

  Tammaro P. and Ashcroft FM., (2006), J Physiol, 577

• Functional effects of naturally occurring KCNJ11 mutations causing neonatal diabetes on cloned cardiac KATP channels.

  Tammaro P. et al, (2006), J Physiol, 571, 3 - 14

• Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.

  Tammaro P. et al, (2005), EMBO J, 24, 2318 - 2330

• Modulation of the voltage-dependent K+ current by intracellular Mg2+ in rat aortic smooth muscle cells.

  Tammaro P. et al, (2005), Cardiovasc Res, 65, 387 - 396

• Effects of intracellular magnesium on Kv1.5 and Kv2.1 potassium channels.

  Tammaro P. et al, (2005), Eur Biophys J, 34, 42 - 51

• Two novel Kir6.2 mutations affecting the ATP sensitivity of the K-ATP channel are the cause of Permanent Neonatal Diabetes.

  Tammaro P. et al, (2005), BIOPHYSICAL JOURNAL, 88, 285A - 285A

• The functional effects of naturally occurring KNCJ11 mutations associated with neonatal diabetes on cloned cardiac K-ATP channels

  Tammaro P. and Ashcroft F., (2005), DIABETOLOGIA, 48, A394 - A394

• Modelling of the ATP-inhibitory mechanism in ATP-sensitive potassium (KATP) channels: Insights from computer simulations of wild-type and mutant channels.

  Shang LJ. et al, (2005), BIOPHYSICAL JOURNAL, 88, 284A - 284A

• Pharmacological evidence for a key role of voltage-gated K+ channels in the function of rat aortic smooth muscle cells.

  Tammaro P. et al, (2004), Br J Pharmacol, 143, 303 - 317

• Effect of intracellular magnesium on K-v currents in rat conduit pulmonary arterial myocytes (rPAMs) and K-v channels expressed in Xenopus oocytes

  Tammaro P. et al, (2004), BIOPHYSICAL JOURNAL, 86, 391A - 391A

• Induction of apoptosis by fenretinide in tumor cell lines correlates with DLX2, DLX3 and DLX4 gene expression.

  Ferrari N. et al, (2003), Oncol Rep, 10, 973 - 977

• Role of voltage-gated K+ (Kv) channels in vascular function

  Smirnov SV. et al, (2003), Neurophysiology, 35, 234 - 247

• Modulation of voltage-gated K+ (Kv) channel currents by intracellular Mg2+ in rat vasculature

  Tammaro P. and Smirnov SV., (2003), BIOPHYSICAL JOURNAL, 84, 419A - 419A

• Sodium channel heterologous expression in mammalian cells and the role of the endogenous beta1-subunits.

  Moran O. et al, (2003), Neurosci Lett, 336, 175 - 179

• Neurohormonal antagonism in heart failure; beneficial effects of vasopressin V(1a) and V(2) receptor blockade and ACE inhibition.

  Naitoh M. et al, (2002), Cardiovasc Res, 54, 51 - 57

• Developmental changes in the functional characteristics and expression of voltage-gated K+ channel currents in rat aortic myocytes.

  Belevych AE. et al, (2002), Cardiovasc Res, 54, 152 - 161

• Modulation of sodium current in mammalian cells by an epilepsy-correlated beta 1-subunit mutation.

  Tammaro P. et al, (2002), Biochem Biophys Res Commun, 291, 1095 - 1101

• Electrophysiologically distinct smooth muscle cell subtypes in rat conduit and resistance pulmonary arteries.

  Smirnov SV. et al, (2002), J Physiol, 538, 867 - 878

• Modulation of Kv channel currents by bisindolylmaleimide I (BIM), a selective PKC inhibitor, in rat aortic myocytes

  Tammaro P. and Smirnov SV., (2002), BIOPHYSICAL JOURNAL, 82, 285A - 285A

• Functional properties of sodium channels do not depend on the cytoskeleton integrity.

  Moran O. et al, (2000), Biochem Biophys Res Commun, 276, 204 - 209

• Functional properties of sodium channels do not depend on the cytoskeleton integrity.

  Moran O. et al, (2000), Biochem Biophys Res Commun, 275, 839 - 844

• Contrasting effects of phosphatidylinositol 4,5-bisphosphate (PIP2 ) on cloned TMEM16A and TMEM16B channels

  Ta C. et al, British Journal of Pharmacology

Recent Publications

• Mechanism of allosteric activation of TMEM16A/ANO1 channels by a commonly used chloride channel blocker.

  Ta CM. et al, (2016), Br J Pharmacol, 173, 511 - 528

• Corrigendum to "Disease-causing mutations associated with four bestrophinopathies exhibit disparate effects on the localization, but not the oligomerization, of Bestrophin-1" [Exp. Eye Res. 121 (2014) 74-85] DOI: 10.1016/j.exer.2014.02.006

  Johnson AA. et al, (2014), Experimental Eye Research, 127

• TMEM16A: A new therapeutic target for diseases of altered blood pressure

  Tammaro P., (2014), ACTA PHYSIOLOGICA, 211, 49 - 49

• Loss of TMEM16A function causes vascular abnormalities in mice

  Garnett H. et al, (2014), ACTA PHYSIOLOGICA, 211, 90 - 90

• Corrigendum to "Disease-causing mutations associated with four bestrophinopathies exhibit disparate effects on the localization, but not the oligomerization, of Bestrophin-1" [Exp. Eye Res. 121 (2014) 74-85] (DOI:10.1016/j.exer.2014.02.006)

  Johnson AA. et al, (2014), Experimental Eye Research