Zobrazeno 1 - 10
of 120
pro vyhledávání: '"Daniel L, Minor"'
Publikováno v:
STAR Protocols, Vol 5, Iss 1, Pp 102792- (2024)
Summary: Anuran saxiphilins (Sxphs) are “toxin sponge” proteins thought to prevent the lethal effects of small-molecule neurotoxins through sequestration. Here, we present a protocol for the expression, purification, and characterization of Sxphs
Externí odkaz:
https://doaj.org/article/31608f98045f4bf78d28744aa82a16b1
Autor:
Travis J. Morgenstern, Neha Nirwan, Erick O. Hernández-Ochoa, Hugo Bibollet, Papiya Choudhury, Yianni D. Laloudakis, Manu Ben Johny, Roger A. Bannister, Martin F. Schneider, Daniel L. Minor, Henry M. Colecraft
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-19 (2022)
Auxiliary subunit molecular diversity is an unexploited target for developing ion channel inhibitors. Here, the authors develop a general approach to inhibit ion channels based on the resident auxiliary subunit isoform to elucidate unique functions o
Externí odkaz:
https://doaj.org/article/6afcd6383eb345e8b49429eb383e8ae1
Autor:
Cristina Arrigoni, Marco Lolicato, David Shaya, Ahmed Rohaim, Felix Findeisen, Lam-Kiu Fong, Claire M. Colleran, Pawel Dominik, Sangwoo S. Kim, Jonathan P. Schuermann, William F. DeGrado, Michael Grabe, Anthony A. Kossiakoff, Daniel L. Minor
Publikováno v:
Nat Struct Mol Biol
Every voltage-gated ion channel (VGIC) has a pore domain (PD) made from four subunits, each comprising an antiparallel transmembrane helix pair bridged by a loop. The extent to which PD subunit structure requires quaternary interactions is unclear. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1228e10502809bafbfb88b46afc7f7d4
https://doi.org/10.1038/s41594-022-00775-x
https://doi.org/10.1038/s41594-022-00775-x
Autor:
Zhou Chen, Abhisek Mondal, Fayal Abderemane Ali, Seil Jang, Sangeeta Niranjan, José L. Montaño, Balyn W. Zaro, Daniel L. Minor
Publikováno v:
Nature.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7138149dd786ac71bc16647ab5ac6d3d
https://doi.org/10.1038/s41586-023-06175-5
https://doi.org/10.1038/s41586-023-06175-5
Autor:
Francisco Sepúlveda, Leigh D. Plant, Daniel L. Minor, Jr., Florian Lesage, Steve A.N. Goldstein, Péter Enyedi, Gábor Czirják, Douglas A. Bayliss, Austin M. Baggetta
Publikováno v:
IUPHAR/BPS Guide to Pharmacology CITE. 2023
The 4TM family of K channels mediate many of the background potassium currents observed in native cells. They are open across the physiological voltage-range and are regulated by a wide array of neurotransmitters and biochemical mediators. The pore-f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea7fde47c570d550bb1c3c79a91764bb
https://doi.org/10.2218/gtopdb/f79/2023.1
https://doi.org/10.2218/gtopdb/f79/2023.1
Publikováno v:
Nature Structural & Molecular Biology.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e5bffad0d6f422327c7b25ec376f5ab4
https://doi.org/10.1038/s41594-023-00951-7
https://doi.org/10.1038/s41594-023-00951-7
Gabapentinoid drugs for pain and anxiety act on the CaVα2δ-1 and CaVα2δ-2 subunits of high-voltage activated calcium channels (CaV1s and CaV2s). Here, we present the cryo-EM structure of the gabapentin-bound brain and cardiac CaV1.2/CaVβ3/CaVα2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a93d9e27a3c79bb1a9f047afa274cb6
https://doi.org/10.1101/2022.12.05.519047
https://doi.org/10.1101/2022.12.05.519047
Autor:
Zhou Chen, Sandra Zakrzewska, Holly S. Hajare, Aurora Alvarez-Buylla, Fayal Abderemane-Ali, Maximiliana Bogan, Dave Ramirez, Lauren A. O’Connell, J. Du Bois, Daniel L. Minor
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 119, iss 44
American bullfrog ( Rana castesbeiana ) saxiphilin ( Rc Sxph) is a high-affinity “toxin sponge” protein thought to prevent intoxication by saxitoxin (STX), a lethal bis-guanidinium neurotoxin that causes paralytic shellfish poisoning (PSP) by blo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::025c106450d858e7d469c2c41b558667
https://pubmed.ncbi.nlm.nih.gov/36279441
https://pubmed.ncbi.nlm.nih.gov/36279441
Voltage-gated ion channels (VGICs) comprise multiple structural units whose assembly is required for function1,2. There is scant structural understanding of how VGIC subunits assemble and whether chaperone proteins are required. High-voltage activate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5351e8acc6f96dd7a448b67413635499
https://doi.org/10.1101/2022.10.03.510667
https://doi.org/10.1101/2022.10.03.510667
Autor:
Lianne, Pope, Daniel L, Minor
Publikováno v:
Adv Exp Med Biol
K(2P) (KCNK) potassium channels form “back-ground” or “leak” currents that have critical roles in cell excitability control in the brain, cardiovascular system, and somatosensory neurons. Similar to many ion channel families, studies of K(2P)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f0c9efe9aa02ef894f1dd615fe83fb5e
https://pubmed.ncbi.nlm.nih.gov/35138610
https://pubmed.ncbi.nlm.nih.gov/35138610