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Thematische Bibliographien / Gating mechanism

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Auswahl der wissenschaftlichen Literatur zum Thema „Gating mechanism“

Autor: Grafiati

Veröffentlicht am 25. Mai 2024

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Zeitschriftenartikel zum Thema "Gating mechanism"

1

Ulbricht, Mathias. "Gating mechanism under pressure." Nature 519, no. 7541 (2015): 41–42. http://dx.doi.org/10.1038/519041a.

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2

Csanády, László. "Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms." Journal of General Physiology 134, no. 2 (2009): 129–36. http://dx.doi.org/10.1085/jgp.200910268.

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Rate-equilibrium free energy relationship (REFER) analysis provides information on transition-state structures and has been applied to reveal the temporal sequence in which the different regions of an ion channel protein move during a closed–open conformational transition. To date, the theory used to interpret REFER relationships has been developed only for equilibrium mechanisms. Gating of most ion channels is an equilibrium process, but recently several ion channels have been identified to have retained nonequilibrium traits in their gating cycles, inherited from transporter-like ancestors.

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3

Enkvetchakul, D., and C. G. Nichols. "Gating Mechanism of KATP Channels." Journal of General Physiology 122, no. 5 (2003): 471–80. http://dx.doi.org/10.1085/jgp.200308878.

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4

Fu, Tianmin. "Molecular Mechanism of TRPM2 Gating." Biophysical Journal 116, no. 3 (2019): 299a—300a. http://dx.doi.org/10.1016/j.bpj.2018.11.1624.

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5

Zhao, Piao, Cheng Tang, Yuqin Yang, et al. "A new polymodal gating model of the proton-activated chloride channel." PLOS Biology 21, no. 9 (2023): e3002309. http://dx.doi.org/10.1371/journal.pbio.3002309.

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The proton–activated chloride (PAC) channel plays critical roles in ischemic neuron death, but its activation mechanisms remain elusive. Here, we investigated the gating of PAC channels using its novel bifunctional modulator C77304. C77304 acted as a weak activator of the PAC channel, causing moderate activation by acting on its proton gating. However, at higher concentrations, C77304 acted as a weak inhibitor, suppressing channel activity. This dual function was achieved by interacting with 2 modulatory sites of the channel, each with different affinities and dependencies on the channel’s sta

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6

Elinder, Fredrik, and Peter Århem. "Metal ion effects on ion channel gating." Quarterly Reviews of Biophysics 36, no. 4 (2003): 373–427. http://dx.doi.org/10.1017/s0033583504003932.

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1. Introduction 3742. Metals in biology 3783. The targets: structure and function of ion channels 3804. General effects of metal ions on channels 3824.1 Three types of general effect 3824.2 The main regulators 3835. Effects on gating: mechanisms and models 3845.1 Screening surface charges (Mechanism A) 3875.1.1 The classical approach 3875.1.1.1 Applying the Grahame equation 3885.1.2 A one-site approach 3915.2 Binding and electrostatically modifying the voltage sensor (Mechanism B) 3915.2.1 The classical model 3915.2.1.1 The classical model as state diagram – introducing basic channel kinetics

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7

Navarro, Marco A., Lorin S. Milescu, and Mirela Milescu. "Unlocking the gating mechanism of Kv2.1 using guangxitoxin." Journal of General Physiology 151, no. 3 (2018): 275–78. http://dx.doi.org/10.1085/jgp.201812254.

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8

Lopez, William, Jayalakshmi Ramachandran, Abdelaziz Alsamarah, Yun Luo, Andrew L. Harris, and Jorge E. Contreras. "Mechanism of gating by calcium in connexin hemichannels." Proceedings of the National Academy of Sciences 113, no. 49 (2016): E7986—E7995. http://dx.doi.org/10.1073/pnas.1609378113.

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Aberrant opening of nonjunctional connexin hemichannels at the plasma membrane is associated with many diseases, including ischemia and muscular dystrophy. Proper control of hemichannel opening is essential to maintain cell viability and is achieved by physiological levels of extracellular Ca2+, which drastically reduce hemichannel activity. Here we examined the role of conserved charged residues that form electrostatic networks near the extracellular entrance of the connexin pore, a region thought to be involved in gating rearrangements of hemichannels. Molecular dynamics simulations indicate

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9

Bompadre, Silvia G., Tomohiko Ai, Jeong Han Cho, et al. "CFTR Gating I." Journal of General Physiology 125, no. 4 (2005): 361–75. http://dx.doi.org/10.1085/jgp.200409227.

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The CFTR chloride channel is activated by phosphorylation of serine residues in the regulatory (R) domain and then gated by ATP binding and hydrolysis at the nucleotide binding domains (NBDs). Studies of the ATP-dependent gating process in excised inside-out patches are very often hampered by channel rundown partly caused by membrane-associated phosphatases. Since the severed ΔR-CFTR, whose R domain is completely removed, can bypass the phosphorylation-dependent regulation, this mutant channel might be a useful tool to explore the gating mechanisms of CFTR. To this end, we investigated the reg

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10

Tiffner, Adéla, Lena Maltan, Sarah Weiß, and Isabella Derler. "The Orai Pore Opening Mechanism." International Journal of Molecular Sciences 22, no. 2 (2021): 533. http://dx.doi.org/10.3390/ijms22020533.

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Cell survival and normal cell function require a highly coordinated and precise regulation of basal cytosolic Ca2+ concentrations. The primary source of Ca2+ entry into the cell is mediated by the Ca2+ release-activated Ca2+ (CRAC) channel. Its action is stimulated in response to internal Ca2+ store depletion. The fundamental constituents of CRAC channels are the Ca2+ sensor, stromal interaction molecule 1 (STIM1) anchored in the endoplasmic reticulum, and a highly Ca2+-selective pore-forming subunit Orai1 in the plasma membrane. The precise nature of the Orai1 pore opening is currently a topi

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