Zobrazeno 1 - 10
of 101
pro vyhledávání: '"David C Gadsby"'
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
Publikováno v:
The Journal of General Physiology
Both the catalytically active and inactive interfacial ATP-binding sites open at least 8 Å during CFTR channel closure.
Cystic fibrosis transmembrane conductance regulator (CFTR) channel opening and closing are driven by cycles of adenosine tri
Cystic fibrosis transmembrane conductance regulator (CFTR) channel opening and closing are driven by cycles of adenosine tri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7e308149d44c3172a50a7d7f3f087b1
https://doi.org/10.1085/jgp.201411347
https://doi.org/10.1085/jgp.201411347
Autor:
David C. Gadsby, Natascia Vedovato
Publikováno v:
Journal of General Physiology. 143:449-464
A single Na+/K+-ATPase pumps three Na+ outwards and two K+ inwards by alternately exposing ion-binding sites to opposite sides of the membrane in a conformational sequence coupled to pump autophosphorylation from ATP and auto-dephosphorylation. The l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::985e22edae02610c82e4b8aa697ad508
https://doi.org/10.1085/jgp.201311148
https://doi.org/10.1085/jgp.201311148
Autor:
David C. Gadsby, Natascia Vedovato
Publikováno v:
Biophysical Journal. 110(3)
Na/K pumps incessantly extrude 3 Na and retrieve 2 K per ATPase cycle by coupling pump autophosphorylation and autodephosphorylation to conformational changes that alternately expose ion-binding sites to opposite membrane sides. The resulting net out
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::026c1b25cb013ddf2ef70eb568c07487
Autor:
Miguel Holmgren, Francisco Bezanilla, Joshua J. C. Rosenthal, Daniel Basilio, Daniela De Giorgis, Juan P. Castillo, David C. Gadsby, Ramon Latorre
Publikováno v:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
The Na + /K + pump is a nearly ubiquitous membrane protein in animal cells that uses the free energy of ATP hydrolysis to alternatively export 3Na + from the cell and import 2K + per cycle. This exchange of ions produces a steady-state outwardly dire
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4abeccc39239a9a67a0e776c0346f9db
https://doi.org/10.1073/pnas.1116439108
https://doi.org/10.1073/pnas.1116439108
Publikováno v:
Proceedings of the National Academy of Sciences. 107:1241-1246
CFTR, the ABC protein defective in cystic fibrosis, functions as an anion channel. Once phosphorylated by protein kinase A, a CFTR channel is opened and closed by events at its two cytosolic nucleotide binding domains (NBDs). Formation of a head-to-t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0cf2549c5853dd14d8fa31795e027fd
https://doi.org/10.1073/pnas.0911061107
https://doi.org/10.1073/pnas.0911061107
Publikováno v:
Channels. 3:383-386
The Na(+),K(+)-ATPase pump achieves thermodynamically uphill exchange of cytoplasmic Na(+) ions for extracellular K(+) ions by using ATP-mediated phosphorylation, followed by autodephosphorylation, to power conformational changes that allow ion acces
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93197d8841ddc5894f1975e00bd4f357
https://doi.org/10.4161/chan.3.6.9775
https://doi.org/10.4161/chan.3.6.9775
Publikováno v:
Philosophical Transactions of the Royal Society B: Biological Sciences. 364:229-238
In principle, an ion channel needs no more than a single gate, but a pump requires at least two gates that open and close alternately to allow ion access from only one side of the membrane at a time. In the Na + ,K + -ATPase pump, this alternating ga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::56e6ee3e70dae56e4c3687b8ed04859d
https://doi.org/10.1098/rstb.2008.0243
https://doi.org/10.1098/rstb.2008.0243
Publikováno v:
Nature
P-type ATPases pump ions across membranes, generating steep electrochemical gradients that are essential for the function of all cells. Access to the ion-binding sites within the pumps alternates between the two sides of the membrane to avoid the dis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8ace9a048290456c75b8c5653463743
https://doi.org/10.1038/nature07350
https://doi.org/10.1038/nature07350
Autor:
Miguel Holmgren, Francisco Palma, Pablo Artigas, Paul De Weer, R.F. Rakowski, David C. Gadsby
Publikováno v:
The Journal of General Physiology
Palytoxin binds to Na(+)/K(+) pumps in the plasma membrane of animal cells and opens an electrodiffusive cation pathway through the pumps. We investigated properties of the palytoxin-opened channels by recording macroscopic and microscopic currents i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cd706fbb48c3f65bca7281ab6e576ac
http://europepmc.org/articles/PMC2085370
http://europepmc.org/articles/PMC2085370