Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Natascia Vedovato"'
Publikováno v:
Frontiers in Pharmacology, Vol 13 (2022)
Externí odkaz:
https://doaj.org/article/ccd692a75aa0487dab92771af35baf81
Autor:
Malgorzata Cyranka, Thomas Monfeuga, Natascia Vedovato, Chelsea M Larabee, Anandhakumar Chandran, Enrique M Toledo, Heidi de Wet
Publikováno v:
Frontiers in Pharmacology, Vol 13 (2022)
Type 2 diabetes mellitus (T2DM) remains one of the most pressing health issues facing modern society. Several antidiabetic drugs are currently in clinical use to treat hyperglycaemia, but there is a need for new treatments that effectively restore pa
Externí odkaz:
https://doaj.org/article/c8783ab345114d4cb005c6e2be4c48d4
Publikováno v:
eLife, Vol 8 (2019)
The response of ATP-sensitive K+ channels (KATP) to cellular metabolism is coordinated by three classes of nucleotide binding site (NBS). We used a novel approach involving labeling of intact channels in a native, membrane environment with a non-cano
Externí odkaz:
https://doaj.org/article/7f916e61f8a14fc0a7f9a33162e35c07
Autor:
Toke Jost Isaksen, Lieke Kros, Natascia Vedovato, Thomas Hellesøe Holm, Ariel Vitenzon, David C Gadsby, Kamran Khodakhah, Karin Lykke-Hartmann
Publikováno v:
PLoS Genetics, Vol 13, Iss 5, p e1006763 (2017)
Mutations in the neuron-specific α3 isoform of the Na+/K+-ATPase are found in patients suffering from Rapid onset Dystonia Parkinsonism and Alternating Hemiplegia of Childhood, two closely related movement disorders. We show that mice harboring a he
Externí odkaz:
https://doaj.org/article/ff609b5902c742f1aa758dbcde00a063
Autor:
Tanadet Pipatpolkai, Samuel G. Usher, Natascia Vedovato, Frances M. Ashcroft, Phillip J. Stansfeld
Publikováno v:
Pipatpolkai, T, Usher, S G, Vedovato, N, Ashcroft, F M & Stansfeld, P J 2022, ' The dynamic interplay of PIP 2 and ATP in the regulation of the K ATP channel ', The Journal of Physiology, vol. 600, no. 20, pp. 4503-4519 . https://doi.org/10.1113/JP283345
KEY POINTS: The KATP channel is activated by the binding of phosphoinositol-bisphosphate (PIP2 ) lipids and inactivated by the binding of adenosine triphosphate (ATP). K39 has the potential to bind to both PIP2 and ATP. A mutation to this residue (K3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20f11a334096095b3567a7a9f7373d65
https://doi.org/10.1101/2021.05.06.442933
https://doi.org/10.1101/2021.05.06.442933
Autor:
Natascia Vedovato, Frances M. Ashcroft, Phillip J. Stansfeld, Samuel Usher, Tanadet Pipatpolkai
ATP-sensitive potassium (KATP) channels couple the intracellular ATP concentration to insulin secretion. KATP channel activity is inhibited by ATP binding to the Kir6.2 tetramer and activated by phosphatidylinositol-4,5-bisphosphate (PIP2). Here, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5da4b321350e7ce21720a58de343136b
https://doi.org/10.21203/rs.3.rs-445411/v1
https://doi.org/10.21203/rs.3.rs-445411/v1
Publikováno v:
The Journal of Physiology. 596:6205-6217
Key points β-Cell KATP channels are partially open in the absence of metabolic substrates, whereas cardiac KATP channels are closed. Using cloned channels heterologously expressed in Xenopus oocytes we measured the effect of MgADP on the MgATP conce
Autor:
Frances M. Ashcroft, Tarig Babiker, Roisin Finn, Sarah E. Flanagan, Maggie Shepherd, Andrew T. Hattersley, Natascia Vedovato, Nicholas J. Thomas, Sian Ellard, Ali J. Chakera, Roope Männikkö, Kashyap A. Patel
Publikováno v:
Diabetologia
Aims/hypothesis The finding that patients with diabetes due to potassium channel mutations can transfer from insulin to sulfonylureas has revolutionised the management of patients with permanent neonatal diabetes. The extent to which the in vitro cha
Publikováno v:
eLife
The response of ATP-sensitive K+ channels (KATP) to cellular metabolism is coordinated by three classes of nucleotide binding site (NBS). We used a novel approach involving labeling of intact channels in a native, membrane environment with a non-cano