Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Rodolfo Briones"'
Gromaps: A Gromacs-Based Toolset to Analyse Density Maps Derived from Molecular Dynamics Simulations
Publikováno v:
Biophysical Journal. 116:142a-143a
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2015, 112 (40), pp.12390-12395. ⟨10.1073/pnas.1513782112⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2015, 112 (40), pp.12390-12395. ⟨10.1073/pnas.1513782112⟩
Proceedings of the National Academy of Sciences of the United States of America, 2015, 112 (40), pp.12390-12395. ⟨10.1073/pnas.1513782112⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2015, 112 (40), pp.12390-12395. ⟨10.1073/pnas.1513782112⟩
International audience; Regulated intramembrane proteolysis (RIP) is a conserved mechanism crucial for numerous cellular processes, including signaling, transcriptional regulation, axon guidance, cell adhesion, cellular stress responses, and transmem
Autor:
Mathilde Keck, Jacques Teulon, Stéphane Lourdel, Olga Andrini, Rodolfo Briones, Rosa Vargas-Poussou
Publikováno v:
AJP Renal Physiology
AJP Renal Physiology, American Physiological Society, 2015, 308 (12), pp.F1324-F1334. ⟨10.1152/ajprenal.00004.2015⟩
American Journal of Physiology-Renal Physiology
AJP Renal Physiology, American Physiological Society, 2015, 308 (12), pp.F1324-F1334. ⟨10.1152/ajprenal.00004.2015⟩
American Journal of Physiology-Renal Physiology
International audience; The mutations in the CLCNKB gene encoding the ClC-Kb chloride channel are responsible for Bartter syndrome type 3, one of the four variants of Bartter syndrome in the genetically based nomenclature. All forms of Bartter syndro
Publikováno v:
Biophysical Journal
Electrical cell signaling requires adjustment of ion channel, receptor, or transporter function in response to changes in membrane potential. For the majority of such membrane proteins, the molecular details of voltage sensing remain insufficiently u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d80c608254139c2dc5915ba46daca6d
https://hdl.handle.net/11858/00-001M-0000-002D-339B-511858/00-001M-0000-002D-339C-311858/00-001M-0000-002D-3399-911858/00-001M-0000-002D-3396-F11858/00-001M-0000-002D-3398-B11858/00-001M-0000-002D-339A-7
https://hdl.handle.net/11858/00-001M-0000-002D-339B-511858/00-001M-0000-002D-339C-311858/00-001M-0000-002D-3399-911858/00-001M-0000-002D-3396-F11858/00-001M-0000-002D-3398-B11858/00-001M-0000-002D-339A-7
Publikováno v:
Frontiers in Physiology
Hydrophobic matching, lipid sorting, and protein oligomerization are key principles by which lipids and proteins organize in biological membranes. The Aquaporin-0 channel (AQP0), solved by electron crystallography (EC) at cryogenic temperatures, is o
Gating Charge Calculations: Probing Voltage-Sensing Proteins through Computational Electrophysiology
Publikováno v:
Biophysical Journal. 110(3)
Sensitivity to voltage stimuli is a defining property of electrical excitability and is found in ion channels with dedicated voltage sensors, but also in other channels, transporters and even metabotropic receptors. Voltage dependence is conferred by
Autor:
Adam Lange, Claudia Steinem, Markus Zweckstetter, Ingo Mey, Bert L. de Groot, Conrad Weichbrodt, Saskia Villinger, Rodolfo Briones, Stefan Becker, Licia Paltrinieri, Christian Griesinger, Karin Giller
Publikováno v:
Biophysical journal 111(6), 1223-1234 (2016). doi:10.1016/j.bpj.2016.08.007
Biophysical Journal
Biophysical Journal
The voltage-dependent anion channel 1 (VDAC-1) is an important protein of the outer mitochondrial membrane that transports energy metabolites and is involved in apoptosis. The available structures of VDAC proteins show a wide β -stranded barrel pore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26e7174414787a982cd64ff7cb1e4cce
https://pub.dzne.de/record/138791
https://pub.dzne.de/record/138791
Autor:
Roland Benz, Stefan Becker, Ulrich Zachariae, Bert L. de Groot, Christian Griesinger, Markus Zweckstetter, Jean-Philippe Demers, Robert Schneider, Adam Lange, Zrinka Gattin, Elke Maier, Rodolfo Briones, Karin Giller
Publikováno v:
Structure
The voltage-dependent anion channel (VDAC) is the major protein in the outer membrane of mitochondria, where it mediates efficient transport of ATP and ADP. Changes in its conformation and permeability, induced by voltage or apoptosis-related protein
Publikováno v:
The Journal of Physiology. 587:1387-1400
The ClC transport protein family comprises both Cl(-) ion channel and H(+)/Cl(-) and H(+)/NO(3)(-) exchanger members. Structural studies on a bacterial ClC transporter reveal a pore obstructed at its external opening by a glutamate side-chain which a
Publikováno v:
Journal of Molecular Structure: THEOCHEM. 764:187-194
The electronic structure and the spectroscopic properties of [ M ( CN ) 2 ] n − n (M=Au(I), Ag(I); n=1–3) were studied using density functional theory (DFT) at the B3LYP level. The absorption spectrums in these complexes were calculated by single