Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Wayland W L Cheng"'
Autor:
Zi-Wei Chen, John R Bracamontes, Melissa M Budelier, Allison L Germann, Daniel J Shin, Krishnan Kathiresan, Ming-Xing Qian, Brad Manion, Wayland W L Cheng, David E Reichert, Gustav Akk, Douglas F Covey, Alex S Evers
Publikováno v:
PLoS Biology, Vol 17, Iss 3, p e3000157 (2019)
Neurosteroids are endogenous modulators of neuronal excitability and nervous system development and are being developed as anesthetic agents and treatments for psychiatric diseases. While gamma amino-butyric acid Type A (GABAA) receptors are the prim
Externí odkaz:
https://doaj.org/article/a27cab63789b480aa2cf6c0a29f66e70
Autor:
Vikram Dalal, Mark J. Arcario, John T. Petroff, Brandon K. Tan, Noah M. Dietzen, Michael J. Rau, James A. J. Fitzpatrick, Grace Brannigan, Wayland W. L. Cheng
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-10 (2024)
Abstract Lipid nanodiscs have become a standard tool for studying membrane proteins, including using single particle cryo-electron microscopy (cryo-EM). We find that reconstituting the pentameric ligand-gated ion channel (pLGIC), Erwinia ligand-gated
Externí odkaz:
https://doaj.org/article/bb81c76ea0364e6bbfdacc3892a310a3
Autor:
Philipp A. M. Schmidpeter, John T. Petroff, Leila Khajoueinejad, Aboubacar Wague, Cheryl Frankfater, Wayland W. L. Cheng, Crina M. Nimigean, Paul M. Riegelhaupt
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Tandem pore (K2P) potassium channels set the cellular resting membrane potential in tissues throughout the body. Here, authors show how the composition of phospholipid within the bilayer may directly alter gating in this family of ion channels.
Externí odkaz:
https://doaj.org/article/c11664e1beb14494880bdba7127595cd
Autor:
Vikram Dalal, Mark J. Arcario, John T. Petroff, Noah M. Dietzen, Michael J. Rau, James A. J. Fitzpatrick, Grace Brannigan, Wayland W. L. Cheng
Lipid nanodiscs have become the standard reconstitution system for structural and biochemical studies of membrane proteins, especially using single particle cryo-EM. We find that reconstitution of the pentameric ligand-gated ion channel (pLGIC),Erwin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::588c027ecb5ec641b16e2bda8019f72f
https://doi.org/10.1101/2022.11.20.517256
https://doi.org/10.1101/2022.11.20.517256
Autor:
John T. Petroff, Noah M. Deitzen, Ezry Santiago-McRae, Brett Deng, Maya S. Washington, Lawrence J. Chen, K. Trent Moreland, Zengqin Deng, Michael Rau, James A. J. Fitzpatrick, Peng Yuan, Thomas T. Joseph, Jérôme Hénin, Grace Brannigan, Wayland W. L. Cheng
Pentameric ligand-gated ion channels (pLGICs) mediate synaptic transmission and are sensitive to their lipid environment. The mechanism of phospholipid modulation of any pLGIC is not well understood. We demonstrate that the model pLGIC, ELIC (Erwinia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d864e4b461367a9fb673545413db7b5e
https://doi.org/10.1101/2022.06.07.494883
https://doi.org/10.1101/2022.06.07.494883
Publikováno v:
Frontiers in Physiology, Vol 12 (2022)
Frontiers in Physiology
Frontiers in Physiology
Lipids modulate the function of many ion channels, possibly through direct lipid-protein interactions. The recent outpouring of ion channel structures by cryo-EM has revealed many lipid binding sites. Whether these sites mediate lipid modulation of i
Autor:
John T. Petroff, Noah M. Dietzen, Ezry Santiago-McRae, Brett Deng, Maya S. Washington, Lawrence J. Chen, K. Trent Moreland, Zengqin Deng, Michael Rau, James A. J. Fitzpatrick, Peng Yuan, Thomas T. Joseph, Jérôme Hénin, Grace Brannigan, Wayland W. L. Cheng
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Pentameric ligand-gated ion channels are modulated by anionic phospholipids. Here, by capturing an open-channel conformation of ELIC, the authors demonstrate the structural details of channel activation and a leaflet-specific mechanism for modulation
Externí odkaz:
https://doaj.org/article/d772e49e78fb4be7aa7a408b799d12f0