Zobrazeno 1 - 10
of 137
pro vyhledávání: '"William N Zagotta"'
Autor:
William N Zagotta, Brandon S Sim, Anthony K Nhim, Marium M Raza, Eric GB Evans, Yarra Venkatesh, Chloe M Jones, Ryan A Mehl, E James Petersson, Sharona E Gordon
Publikováno v:
eLife, Vol 10 (2021)
With the recent explosion in high-resolution protein structures, one of the next frontiers in biology is elucidating the mechanisms by which conformational rearrangements in proteins are regulated to meet the needs of cells under changing conditions.
Externí odkaz:
https://doaj.org/article/93b61d38288c44e393a7774bb956124a
Publikováno v:
eLife, Vol 7 (2018)
Externí odkaz:
https://doaj.org/article/98b27b2cbb9446f3ad8c7917ef2cc95e
Publikováno v:
eLife, Vol 7 (2018)
Conformational dynamics underlie enzyme function, yet are generally inaccessible via traditional structural approaches. FRET has the potential to measure conformational dynamics in vitro and in intact cells, but technical barriers have thus far limit
Externí odkaz:
https://doaj.org/article/bfcbb8ec25cc4864913c6b989584adb9
Autor:
Gucan Dai, William N Zagotta
Publikováno v:
eLife, Vol 6 (2017)
EAG-like (ELK) voltage-gated potassium channels are abundantly expressed in the brain. These channels exhibit a behavior called voltage-dependent potentiation (VDP), which appears to be a specialization to dampen the hyperexitability of neurons. VDP
Externí odkaz:
https://doaj.org/article/8be9363a51484974bb1640e68d40ee40
Publikováno v:
PLoS ONE, Vol 5, Iss 9 (2010)
Ether-à-go-go (EAG) channels are expressed throughout the central nervous system and are also crucial regulators of cell cycle and tumor progression. The large intracellular amino- and carboxy- terminal domains of EAG1 each share similarity with kno
Externí odkaz:
https://doaj.org/article/7b459e9e41184f98a65b4cd218cec28c
Autor:
Subhashis Jana, Eric G. B. Evans, Hyo Sang Jang, Shuyang Zhang, Hui Zhang, Andrzej Rajca, Sharona E. Gordon, William N. Zagotta, Stefan Stoll, Ryan A. Mehl
Publikováno v:
bioRxiv
Studying protein structures and dynamics directly in the cellular environments in which they function is essential to fully understand the molecular mechanisms underlying cellular processes. Site-directed spin-labeling (SDSL)—in combination with do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a92a84e92edd5c1de181579c16ce6f1a
https://doi.org/10.1101/2023.01.26.525763
https://doi.org/10.1101/2023.01.26.525763
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Nature Communications
Nature Communications
Pacemaker hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channels exhibit a reversed voltage-dependent gating, activating by membrane hyperpolarization instead of depolarization. Sea urchin HCN (spHCN) channels also undergo inactivatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20ddfbf18313e27b6f869da87cfe4ba2
https://doaj.org/article/87335df92b7c4bdb83eb77f703536c2b
https://doaj.org/article/87335df92b7c4bdb83eb77f703536c2b
Publikováno v:
Biophysical Journal. 122:391a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e4ebec6d23827b7ea6a7d302ad8b2a0
https://doi.org/10.1016/j.bpj.2022.11.2137
https://doi.org/10.1016/j.bpj.2022.11.2137
Autor:
Eric G.B. Evans, William N. Zagotta
Publikováno v:
Neuron. 109:1245-1247
In this issue of Neuron, Xue et al. report high-resolution structures of the human cGMP-activated ion channel CNGA1 from rod photoreceptors. These structures provide valuable insights into the processes of cGMP-dependent activation and Ca2+ block and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d93a4ddff068cfb58bc4f3ff69adfd2
https://doi.org/10.1016/j.neuron.2021.03.034
https://doi.org/10.1016/j.neuron.2021.03.034
Autor:
Yarra Venkatesh, Eric G.B. Evans, William N. Zagotta, E. James Petersson, Anthony K Nhim, Marium M. Raza, Ryan A. Mehl, Chloe M. Jones, Brandon S Sim, Sharona E. Gordon
Publikováno v:
eLife, Vol 10 (2021)
eLife
eLife
With the recent explosion in high-resolution protein structures, one of the next frontiers in biology is elucidating the mechanisms by which conformational rearrangements in proteins are regulated to meet the needs of cells under changing conditions.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5e82c6c1482a9ca302b9ec7994b2d96
https://doi.org/10.7554/elife.70236
https://doi.org/10.7554/elife.70236