Outputs (5)

Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis (2007)
Journal Article

ATP-sensitive potassium (K(ATP)) channels couple cell metabolism to electrical activity by regulating K(+) fluxes across the plasma membrane. Channel closure is facilitated by ATP, which binds to the pore-forming subunit (Kir6.2). Conversely, channel... Read More about Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis.

Mechanism of action of a sulphonylurea receptor SUR1 mutation (F132L) that causes DEND syndrome (2007)
Journal Article

Activating mutations in the genes encoding the ATP-sensitive potassium (K(ATP)) channel subunits Kir6.2 and SUR1 are a common cause of neonatal diabetes. Here, we analyse the molecular mechanism of action of the heterozygous mutation F132L, which lie... Read More about Mechanism of action of a sulphonylurea receptor SUR1 mutation (F132L) that causes DEND syndrome.

Studies of the ATPase activity of the ABC protein SUR1 (2007)
Journal Article

The ATP-sensitive potassium (KATP) channel couples glucose metabolism to insulin secretion in pancreatic β-cells. It comprises regulatory sulfonylurea receptor 1 and pore-forming Kir6.2 subunits. Binding and/or hydrolysis of Mg-nucleotides at the nuc... Read More about Studies of the ATPase activity of the ABC protein SUR1.

A FAFLP system for the improved identification of plant-pathogenic and plant-associated species of the genus Pantoea (2007)
Journal Article

The majority of Pantoea species are either plant-pathogenic or plant-associated and cause a wide variety of symptoms on a range of hosts. Identification of Pantoea species is difficult due to minor differences in phenotypic characteristics between th... Read More about A FAFLP system for the improved identification of plant-pathogenic and plant-associated species of the genus Pantoea.

Phosphomimetic mutation of Ser-187 of SNAP-25 increases both syntaxin binding and highly Ca2+-sensitive exocytosis (2007)
Journal Article

The phosphorylation targets that mediate the enhancement of exocytosis by PKC are unknown. PKC phosporylates the SNARE protein SNAP-25 at Ser-187. We expressed mutants of SNAP-25 using the Semliki Forest Virus system in bovine adrenal chromaffin cell... Read More about Phosphomimetic mutation of Ser-187 of SNAP-25 increases both syntaxin binding and highly Ca2+-sensitive exocytosis.