about
Running out of time: the decline of channel activity and nucleotide activation in adenosine triphosphate-sensitive K-channelsThe Nucleotide-Binding Sites of SUR1: A Mechanistic ModelPlasma membrane-porating domain in poliovirus 2B protein. A short peptide mimics viroporin activity.Hypothermia-induced dystonia and abnormal cerebellar activity in a mouse model with a single disease-mutation in the sodium-potassium pump.The two C-terminal tyrosines stabilize occluded Na/K pump conformations containing Na or K ionsSuccessful transfer to sulfonylureas in KCNJ11 neonatal diabetes is determined by the mutation and duration of diabetes.Route, mechanism, and implications of proton import during Na+/K+ exchange by native Na+/K+-ATPase pumps.Neonatal Diabetes and the KATP Channel: From Mutation to Therapy.Neonatal diabetes caused by a homozygous KCNJ11 mutation demonstrates that tiny changes in ATP sensitivity markedly affect diabetes risk.Correction to 'Running out of time: the decline of channel activity and nucleotide activation in adenosine triphosphate-sensitive K-channels'Crystal Structure of a Spin-Labeled, Channel-Forming Alamethicin AnalogueRole of the C-terminus of SUR in the differential regulation of β-cell and cardiac KATP channels by MgADP and metabolism.Modulation of the reaction cycle of the Na+:Ca2+, K+ exchangerPore-forming properties of alamethicin F50/5 inserted in a biological membraneA novel technique to study pore-forming peptides in a natural membranePermanent neonatal diabetes: combining sulfonylureas with insulin may be an effective treatment
P50
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P50
description
researcher
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wetenschapper
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հետազոտող
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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Natascia Vedovato
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P108
P106
P31
P496
0000-0003-4462-5865