Zobrazeno 1 - 10
of 130
pro vyhledávání: '"Stuart J Edelstein"'
Publikováno v:
PLoS Computational Biology, Vol 16, Iss 2, p e1006991 (2020)
Calmodulin sits at the center of molecular mechanisms underlying learning and memory. Its complex and sometimes opposite influences, mediated via the binding to various proteins, are yet to be fully understood. Calcium/calmodulin-dependent protein ki
Externí odkaz:
https://doaj.org/article/21cc734feb2c417a81895733043ee415
Autor:
Anaïs Menny, Solène N Lefebvre, Philipp AM Schmidpeter, Emmanuelle Drège, Zaineb Fourati, Marc Delarue, Stuart J Edelstein, Crina M Nimigean, Delphine Joseph, Pierre-Jean Corringer
Publikováno v:
eLife, Vol 6 (2017)
Pentameric ligand-gated ion channels (pLGICs) mediate fast chemical signaling through global allosteric transitions. Despite the existence of several high-resolution structures of pLGICs, their dynamical properties remain elusive. Using the proton-ga
Externí odkaz:
https://doaj.org/article/5a8e01664d3d46f19fbee713e5512e76
Publikováno v:
PLoS Computational Biology, Vol 11, Iss 1, p e1004063 (2015)
Calmodulin is a calcium-binding protein ubiquitous in eukaryotic cells, involved in numerous calcium-regulated biological phenomena, such as synaptic plasticity, muscle contraction, cell cycle, and circadian rhythms. It exibits a characteristic dumbe
Externí odkaz:
https://doaj.org/article/d16416f4d43145f091dc8e02320dcf6b
Publikováno v:
PLoS ONE, Vol 10, Iss 1, p e0116616 (2015)
Modulation of the properties of AMPA receptors at the post-synaptic membrane is one of the main suggested mechanisms underlying fast synaptic transmission in the central nervous system of vertebrates. Electrophysiological recordings of single channel
Externí odkaz:
https://doaj.org/article/fba8d16c57794d3e9af6405ce963aece
Publikováno v:
PLoS ONE, Vol 5, Iss 1, p e8449 (2010)
Biological signal transduction commonly involves cooperative interactions in the binding of ligands to their receptors. In many cases, ligand concentrations in vivo are close to the value of the dissociation constant of their receptors, resulting in
Externí odkaz:
https://doaj.org/article/ea534886e7ac4ae2a0319fce685c8c6c
Calmodulin sits at the centre of molecular mechanisms underlying learning and memory. Its complex, and sometimes opposite influences, via the binding to various proteins, are yet to be fully understood. Calcium/calmodulin-dependent protein kinase II
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80f32918480eb6ca4cc693e13dfeb563
https://doi.org/10.1101/597278
https://doi.org/10.1101/597278
Publikováno v:
PLoS Computational Biology
PLoS Computational Biology, Vol 16, Iss 2, p e1006991 (2020)
PLoS Computational Biology, Vol 16, Iss 2, p e1006991 (2020)
Calmodulin sits at the center of molecular mechanisms underlying learning and memory. Its complex and sometimes opposite influences, mediated via the binding to various proteins, are yet to be fully understood. Calcium/calmodulin-dependent protein ki
Autor:
Solène N Lefebvre, Philipp A. M. Schmidpeter, Stuart J. Edelstein, Zaineb Fourati, Crina M. Nimigean, Emmanuelle Drège, Pierre-Jean Corringer, Anaïs Menny, Delphine Joseph, Marc Delarue
Publikováno v:
eLife
eLife, eLife Sciences Publication, 2017, 6, pp.e23955. ⟨10.7554/eLife.23955⟩
eLife, Vol 6 (2017)
eLife, 2017, 6, pp.e23955. ⟨10.7554/eLife.23955⟩
eLife, eLife Sciences Publication, 2017, 6, pp.e23955. ⟨10.7554/eLife.23955⟩
eLife, Vol 6 (2017)
eLife, 2017, 6, pp.e23955. ⟨10.7554/eLife.23955⟩
Pentameric ligand-gated ion channels (pLGICs) mediate fast chemical signaling through global allosteric transitions. Despite the existence of several high-resolution structures of pLGICs, their dynamical properties remain elusive. Using the proton-ga
Autor:
Philipp A. M. Schmidpeter, Emmanuelle Drège, Stuart J. Edelstein, Delphine Joseph, Solène N Lefebvre, Crina M. Nimigean, Zaineb Fourati, Pierre-Jean Corringer, Anaïs Menny, Marc Delarue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e720968242aa1edebee5a08da78a920b
https://doi.org/10.7554/elife.23955.029
https://doi.org/10.7554/elife.23955.029
Autor:
Stuart J. Edelstein
Publikováno v:
Journal of Molecular Biology
The MWC (Monod–Wyman–Changeux) allosteric model postulates concerted conformational changes between two states: the intrinsically more stable T state with relatively weak ligand binding and the R state with relatively strong ligand binding. The m