Relevant bibliographies by topics / Gating mechanism

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Gating mechanism'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Gating mechanism"

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

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Csanády, László. "Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms." Journal of General Physiology 134, no. 2 (July 27, 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. So far it has not been examined to what extent REFER analysis is applicable to such systems. By deriving the REFER relationships for a simple nonequilibrium mechanism, this paper addresses whether an equilibrium mechanism can be distinguished from a nonequilibrium one by the characteristics of their REFER plots, and whether information on the transition-state structures can be obtained from REFER plots for gating mechanisms that are known to be nonequilibrium cycles. The results show that REFER plots do not carry information on the equilibrium nature of the underlying gating mechanism. Both equilibrium and nonequilibrium mechanisms can result in linear or nonlinear REFER plots, and complementarity of REFER slopes for opening and closing transitions is a trivial feature true for any mechanism. Additionally, REFER analysis provides limited information about the transition-state structures for gating schemes that are known to be nonequilibrium cycles.
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Enkvetchakul, D., and C. G. Nichols. "Gating Mechanism of KATP Channels." Journal of General Physiology 122, no. 5 (October 27, 2003): 471–80. http://dx.doi.org/10.1085/jgp.200308878.

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

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Zhao, Piao, Cheng Tang, Yuqin Yang, Zhen Xiao, Samantha Perez-Miller, Heng Zhang, Guoqing Luo, et al. "A new polymodal gating model of the proton-activated chloride channel." PLOS Biology 21, no. 9 (September 15, 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 state. Moreover, we discovered a protonation–independent voltage activation of the PAC channel that appears to operate through an ion–flux gating mechanism. Through scanning–mutagenesis and molecular dynamics simulation, we confirmed that E181, E257, and E261 in the human PAC channel serve as primary proton sensors, as their alanine mutations eliminated the channel’s proton gating while sparing the voltage–dependent gating. This proton–sensing mechanism was conserved among orthologous PAC channels from different species. Collectively, our data unveils the polymodal gating and proton–sensing mechanisms in the PAC channel that may inspire potential drug development.
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Elinder, Fredrik, and Peter Århem. "Metal ion effects on ion channel gating." Quarterly Reviews of Biophysics 36, no. 4 (November 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 3925.2.2 A one-site approach 3955.2.2.1 Explaining state-dependent binding – a simple electrostatic mechanism 3955.2.2.2 The relation between models assuming binding to smeared and to discrete charges 3965.2.2.3 The special case of Zn2+ – no binding in the open state 3965.2.2.4 Opposing effects of Cd2+ on hyperpolarization-activated channels 3985.3 Binding and interacting non-electrostatically with the voltage sensor (Mechanism C) 3985.3.1 Combining mechanical slowing of opening and closing with electrostatic modification of voltage sensor 4005.4 Binding to the pore – a special case of one-site binding models (Mechanism D) 4005.4.1 Voltage-dependent pore-block – adding extra gating 4015.4.2 Coupling pore block to gating 4025.4.2.1 The basic model again 4025.4.2.2 A special case – Ca2+ as necessary cofactor for closing 4035.4.2.3 Expanding the basic model – Ca2+ affecting a voltage-independent step 4045.5 Summing up 4056. Quantifying the action: comparing the metal ions 4076.1 Steady-state parameters are equally shifted 4076.2 Different metal ions cause different shifts 4086.3 Different metal ions slow gating differently 4106.4 Block of ion channels 4127. Locating the sites of action 4127.1 Fixed surface charges involved in screening 4137.2 Binding sites 4137.2.1 Group 2 ions 4147.2.2 Group 12 ions 4148. Conclusions and perspectives 4159. Appendix 41610. Acknowledgements 41811. References 418Metal ions affect ion channels either by blocking the current or by modifying the gating. In the present review we analyse the effects on the gating of voltage-gated channels. We show that the effects can be understood in terms of three main mechanisms. Mechanism A assumes screening of fixed surface charges. Mechanism B assumes binding to fixed charges and an associated electrostatic modification of the voltage sensor. Mechanism C assumes binding and an associated non-electrostatic modification of the gating. To quantify the non-electrostatic effect we introduced a slowing factor, A. A fourth mechanism (D) is binding to the pore with a consequent pore block, and could be a special case of Mechanisms B or C. A further classification considers whether the metal ion affects a single site or multiple sites. Analysing the properties of these mechanisms and the vast number of studies of metal ion effects on different voltage-gated ion channels we conclude that group 2 ions mainly affect channels by classical screening (a version of Mechanism A). The transition metals and the Zn group ions mainly bind to the channel and electrostatically modify the gating (Mechanism B), causing larger shifts of the steady-state parameters than the group 2 ions, but also different shifts of activation and deactivation curves. The lanthanides mainly bind to the channel and both electrostatically and non-electrostatically modify the gating (Mechanisms B and C). With the exception of the ether-à-go-go-like channels, most channel types show remarkably similar ion-specific sensitivities.
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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 (December 18, 2018): 275–78. http://dx.doi.org/10.1085/jgp.201812254.

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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 (November 21, 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 discrete sites for Ca2+ interaction and consequent disruption of salt bridges in the open hemichannels. Experimentally, we found that disruption of these salt bridges by mutations facilitates hemichannel closing. Two negatively charged residues in these networks are putative Ca2+ binding sites, forming a Ca2+-gating ring near the extracellular entrance of the pore. Accessibility studies showed that this Ca2+-bound gating ring does not prevent access of ions or small molecules to positions deeper into the pore, indicating that the physical gate is below the Ca2+-gating ring. We conclude that intra- and intersubunit electrostatic networks at the extracellular entrance of the hemichannel pore play critical roles in hemichannel gating reactions and are tightly controlled by extracellular Ca2+. Our findings provide a general mechanism for Ca2+ gating among different connexin hemichannel isoforms.
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Bompadre, Silvia G., Tomohiko Ai, Jeong Han Cho, Xiaohui Wang, Yoshiro Sohma, Min Li, and Tzyh-Chang Hwang. "CFTR Gating I." Journal of General Physiology 125, no. 4 (March 14, 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 regulation and gating of the ΔR-CFTR expressed in Chinese hamster ovary cells. In the cell-attached mode, basal ΔR-CFTR currents were always obtained in the absence of cAMP agonists. Application of cAMP agonists or PMA, a PKC activator, failed to affect the activity, indicating that the activity of ΔR-CFTR channels is indeed phosphorylation independent. Consistent with this conclusion, in excised inside-out patches, application of the catalytic subunit of PKA did not affect ATP-induced currents. Similarities of ATP-dependent gating between wild type and ΔR-CFTR make this phosphorylation-independent mutant a useful system to explore more extensively the gating mechanisms of CFTR. Using the ΔR-CFTR construct, we studied the inhibitory effect of ADP on CFTR gating. The Ki for ADP increases as the [ATP] is increased, suggesting a competitive mechanism of inhibition. Single channel kinetic analysis reveals a new closed state in the presence of ADP, consistent with a kinetic mechanism by which ADP binds at the same site as ATP for channel opening. Moreover, we found that the open time of the channel is shortened by as much as 54% in the presence of ADP. This unexpected result suggests another ADP binding site that modulates channel closing.
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Tiffner, Adéla, Lena Maltan, Sarah Weiß, and Isabella Derler. "The Orai Pore Opening Mechanism." International Journal of Molecular Sciences 22, no. 2 (January 7, 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 topic of intensive research. This review describes how Orai1 gating checkpoints in the middle and cytosolic extended transmembrane regions act together in a concerted manner to ensure an opening-permissive Orai1 channel conformation. In this context, we highlight the effects of the currently known multitude of Orai1 mutations, which led to the identification of a series of gating checkpoints and the determination of their role in diverse steps of the Orai1 activation cascade. The synergistic action of these gating checkpoints maintains an intact pore geometry, settles STIM1 coupling, and governs pore opening. We describe the current knowledge on Orai1 channel gating mechanisms and summarize still open questions of the STIM1–Orai1 machinery.
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Dissertations / Theses on the topic "Gating mechanism"

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Yoluk, Özge. "Elucidating the Gating Mechanism of Cys-Loop Receptors." Doctoral thesis, KTH, Teoretisk biologisk fysik, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-187230.

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Cys-loop receptors are membrane proteins that are key players for the fast synaptic neurotransmission. Their ion transport initiates new nerve signals after activation by small agonist molecules, but this function is also highly sensitive to allosteric modulation by a number of compounds such as anesthetics, alcohol or anti-parasitic agents. For a long time, these modulators were believed to act primarily on the membrane, but the availability of high- resolution structures has made it possible to identify several binding sites in the transmembrane domains of the ion channels. It is known that ligand binding in the extracellular domain causes a conformational earthquake that interacts with the transmembrane domain, which leads to channel opening. The investigations carried out in this thesis aim at understanding the connection between ligand binding and channel opening. I present new models of the mammalian GABAA receptor based on the eukaryotic structure GluCl co-crystallized with an anti-parasitic agent, and show how these models can be used to study receptor-modulator interactions. I also show how removal of the bound modulator leads to gradual closing of the channel in molecular dynamics simulations. In contrast, simulations of the receptor with both the agonist and the modulator remain stable in an open-like conformation. This makes it possible to extract several key interactions, and I propose mechanisms for how the extracellular domain motion is initiated. The rapid increase in the number of cys-loop receptor structures the last few years has further made it possible to use principal component analysis (PCA) to create low-dimensional descriptions of the conformational landscape. By performing PCA on the crystal structure ensemble, I have been able to divide the structures into functional clusters and sample the transitions between them using various sampling methods. The studies presented in this thesis contribute to our understanding of the gating mechanism and the functional clustering of the cys-loop receptor structures, which both are important to design new allosteric modulator drugs that influence the channel function, in particular to treat neurological disorders.

QC 20160518

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Lee, Lori WaiHang Dougherty Dennis A. Dougherty Dennis A. "Chemical scale investigations of the gating mechanism of ion channels /." Diss., Pasadena, Calif. : California Institute of Technology, 2007. http://resolver.caltech.edu/CaltechETD:etd-01152007-080704.

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Krishnamoorthy, Gayathri. "MECHANISM OF CALCIUM DEPENDENT GATING OF BKCa CHANNELS: RELATING PROTEIN STRUCTURE TO FUNCTION." online version, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=case1144444855.

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Schulte, Uwe. "pH-Gating of inward-rectifier K+ channels (Kir) molecular mechanism and structural implications /." [S.l. : s.n.], 2000. http://www.bsz-bw.de/cgi-bin/xvms.cgi?SWB8385910.

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Chiang, Chien-Sung. "The gating mechanism of the large mechanosensitive channel in Escherichia coli and effects of gain-of-function mutations." College Park, Md. : University of Maryland, 2005. http://hdl.handle.net/1903/2332.

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Thesis (Ph. D.) -- University of Maryland, College Park, 2005.
Thesis research directed by: Biology. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.
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Nematian, Ardestani Ehsanollah [Verfasser]. "Identification and Characterization of a Novel Voltage Gating Mechanism in Extracellular-pH-sensitive K2P Channels / Ehsanollah Nematian Ardestani." Kiel : Universitätsbibliothek Kiel, 2019. http://d-nb.info/118038766X/34.

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Zhang, Yingyi [Verfasser], Inga [Gutachter] Hänelt, and Mikhail [Gutachter] Kudryashev. "Cryo electron microscopy study on gating mechanism of the lipid-modulated serotonin receptor / Yingyi Zhang ; Gutachter: Inga Hänelt, Mikhail Kudryashev." Frankfurt am Main : Universitätsbibliothek Johann Christian Senckenberg, 2020. http://d-nb.info/1221669222/34.

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Fernandez, Jose A. "Gating mechanisms of the TRPM* ion channel." Thesis, Queen's University Belfast, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.534741.

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Schmidt, Matthias Rene. "K+ channels : gating mechanisms and lipid interactions." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:51dc4149-d943-4dcd-bf5b-f04130456d84.

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Computational methods, including homology modelling, in-silico dockings, and molecular dynamics simulations have been used to study the functional dynamics and interactions of K+ channels. Molecular models were built of the inwardly rectifying K+ channel Kir2.2, the bacterial homolog K+ channel KirBac3.1, and the twin pore (K2P) K+ channels TREK-1 and TRESK. To investigate the electrostatic energy profile of K+ permeating through these homology models, continuum electrostatic calculations were performed. The primary mechanism of KirBac3.1 gating is believed to involve an opening at the helix bundle crossing (HBC). However, simulations of Kir channels have not yet revealed opening at the HBC. Here, in simulations of the new KirBac3.1-S129R X-ray crystal structure, in which the HBC was trapped open by the S129R mutation in the inner pore-lining helix (TM2), the HBC was found to exhibit considerable mobility. In a simulation of the new KirBac3.1-S129R-S205L double mutant structure, if the S129R and the S205L mutations were converted back to the wild-type serine, the HBC would close faster than in the simulations of the KirBac3.1-S129R single mutant structure. The double mutant structure KirBac3.1-S129R-S205L therefore likely represents a higher-energy state than the single mutant KirBac3.1-S129R structure, and these simulations indicate a staged pathway of gating in KirBac channels. Molecular modelling and MD simulations of the Kir2.2 channel structure demonstrated that the HBC would tend to open if the C-linker between the transmembrane and cytoplasmic domain was modelled helical. The electrostatic energy barrier for K+ permeation at the helix bundle crossing was found to be sensitive to subtle structural changes in the C-linker. Charge neutralization or charge reversal of the PIP2-binding residue R186 on the C-linker decreased the electrostatic barrier for K+ permeation through the HBC, suggesting an electrostatic contribution to the PIP2-dependent gating mechanism. Multi-scale simulations determined the PIP2 binding site in Kir2.2, in good agreement with crystallographic predictions. A TREK-1 homology model was built, based on the TRAAK structure. Two PIP2 binding sites were found in this TREK-1 model, at the C-terminal end, in line with existing functional data, and between transmembrane helices TM2 and TM3. The TM2-TM3 site is in reasonably good agreement with electron density attributed to an acyl tail in a recently deposited TREK-2 structure.
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Winch, Tom J. "Current based models for Markov ion channel gating mechanisms." Thesis, University of Nottingham, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.311750.

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Books on the topic "Gating mechanism"

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Yue, David, Manu Ben-Johny, and Ivy E. Dick. Ion Channel Gating and Mechanisms. Iop Publishing Ltd, 2021.

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Loussouarn, Gildas, and Mounir Tarek, eds. Molecular Mechanisms of Voltage-Gating in Ion Channels. Frontiers Media SA, 2021. http://dx.doi.org/10.3389/978-2-88971-588-6.

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Thursfield, Rebecca, Chris Orchard, Rosanna Featherstone, and Jane C. Davies. Future treatments. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780198702948.003.0013.

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There are only a relatively limited armoury of drugs, the majority of which are aimed at downstream symptoms of cystic fibrosis. Therapies targeting the basic defect in CF as well as continued availability of more conventional drugs are required. Progress in gene therapy has been limited by the significant barriers to gene transfer of the CF lung, but the UK is hosting a large repeated dose trial of nebulized non-viral gene therapy designed around clinically meaningful outcomes. The UK CF Gene Therapy Consortium is also seeking to develop a promising modified lentiviral approach, although this is some years off. Perhaps the exciting development of recent decades has come from small molecule CFTR modulators, driven by an understanding of basic pathophysiological mechanisms. Ivacaftor is the first drug to be licensed, having proved itself highly clinically efficacious in patients with the class-3 gating mutation G551D. The trial pipeline seeks to expand indications for this and to explore the potential of Phe508del correctors. Finally, a number of anti-inflammatory and anti-infective strategies are being pursued. The emerging global problem of antibiotic resistance is leading to exciting alternatives such as biofilm disruption and bacteriophage to be explored.
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(Editor), V. Frolov, ed. Quantum Gravity: Proceedings of the 4th Seminar on Quantum Gravity. Moscow,USSR May 25-29, 1987. World Scientific Pub Co Inc, 1988.

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Book chapters on the topic "Gating mechanism"

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Gu, Min, Xiaosong Gan, and Xiaoyuan Deng. "Angle-Gating Mechanism." In Microscopic Imaging Through Turbid Media, 57–89. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46397-0_5.

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Gu, Min, Xiaosong Gan, and Xiaoyuan Deng. "Polarization-Gating Mechanism." In Microscopic Imaging Through Turbid Media, 91–119. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46397-0_6.

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Gu, Min, Xiaosong Gan, and Xiaoyuan Deng. "Fluorescence-Gating Mechanism." In Microscopic Imaging Through Turbid Media, 121–43. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46397-0_7.

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Zagotta, William N. "Ligand-Dependent Gating Mechanism." In Textbook of Ion Channels Volume I, 45–60. Boca Raton: CRC Press, 2023. http://dx.doi.org/10.1201/9781003096214-4.

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Miller, A. G., C. A. Warren, and R. W. Aldrich. "Inward Rectification by an Activation Gating Mechanism." In From Ion Channels to Cell-to-Cell Conversations, 21–34. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4899-1795-9_2.

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Malmström, Bo G. "The Mechanism of Electron Gating in Cytochrome c Oxidase." In Cytochrome Systems, 733–41. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_102.

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Willegems, Katrien, and Rouslan G. Efremov. "Structural Details of the Ryanodine Receptor Calcium Release Channel and Its Gating Mechanism." In Advances in Experimental Medicine and Biology, 179–204. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-55858-5_8.

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Zhu, Liangliang, Qiang Cui, Yilun Liu, Yuan Yan, Hang Xiao, and Xi Chen. "Molecular Dynamics-Decorated Finite Element Method (MDeFEM): Application to the Gating Mechanism of Mechanosensitive Channels." In Handbook of Nonlocal Continuum Mechanics for Materials and Structures, 1–52. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-22977-5_46-1.

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Zhu, Liangliang, Qiang Cui, Yilun Liu, Yuan Yan, Hang Xiao, and Xi Chen. "Molecular Dynamics-Decorated Finite Element Method (MDeFEM): Application to the Gating Mechanism of Mechanosensitive Channels." In Handbook of Nonlocal Continuum Mechanics for Materials and Structures, 77–128. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-58729-5_46.

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Schwarz, M., S. Nill, and R. Bendl. "Combination of External/Image-Based Detection of Respiratory Induced Motion and Adaption with a Gating Mechanism." In IFMBE Proceedings, 772–75. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-03474-9_218.

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Conference papers on the topic "Gating mechanism"

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Salman, Shaeke, and Xiuwen Liu. "Sparsity as the Implicit Gating Mechanism for Residual Blocks." In 2019 International Joint Conference on Neural Networks (IJCNN). IEEE, 2019. http://dx.doi.org/10.1109/ijcnn.2019.8851903.

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Mirzadeh, Seyed Iman, Mehrdad Farajtabar, and Hassan Ghasemzadeh. "Dropout as an Implicit Gating Mechanism For Continual Learning." In 2020 IEEE/CVF Conference on Computer Vision and Pattern Recognition Workshops (CVPRW). IEEE, 2020. http://dx.doi.org/10.1109/cvprw50498.2020.00124.

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Xia, Haifeng, Zengmao Wang, Bo Du, Lefei Zhang, Shuai Chen, and Gang Chun. "Leveraging Ratings and Reviews with Gating Mechanism for Recommendation." In CIKM '19: The 28th ACM International Conference on Information and Knowledge Management. New York, NY, USA: ACM, 2019. http://dx.doi.org/10.1145/3357384.3357919.

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Cao, Kun, and Zongxia Xie. "Uncertainty prediction and calibration using multi-expert gating mechanism." In 2022 International Joint Conference on Neural Networks (IJCNN). IEEE, 2022. http://dx.doi.org/10.1109/ijcnn55064.2022.9891958.

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Wang, Yongheng, Detian Huang, Yifan Shi, Liqing Chen, and Longtao Chen. "Online Multi-Object Tracking with Generalized IoU Gating Mechanism." In 2022 China Automation Congress (CAC). IEEE, 2022. http://dx.doi.org/10.1109/cac57257.2022.10055877.

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Venien- Bryan, Catherine. "Gating mechanism of a potassium channel, experimental and theoretical studies." In European Microscopy Congress 2020. Royal Microscopical Society, 2021. http://dx.doi.org/10.22443/rms.emc2020.741.

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Yang, Binbin, Xinchi Deng, Han Shi, Changlin Li, Gengwei Zhang, Hang Xu, Shen Zhao, Liang Lin, and Xiaodan Liang. "Continual Object Detection via Prototypical Task Correlation Guided Gating Mechanism." In 2022 IEEE/CVF Conference on Computer Vision and Pattern Recognition (CVPR). IEEE, 2022. http://dx.doi.org/10.1109/cvpr52688.2022.00904.

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She, Jingke, Shanshan Gong, Suyuan Yang, Hantao Yang, and Shaofei Lu. "Xigmoid: An Approach to Improve the Gating Mechanism of RNN." In 2022 International Joint Conference on Neural Networks (IJCNN). IEEE, 2022. http://dx.doi.org/10.1109/ijcnn55064.2022.9892346.

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Chang, Junwei, and Li Jin. "Gating Mechanism Based Feature Fusion Networks for Time Series Classification." In 2022 5th International Conference on Advanced Electronic Materials, Computers and Software Engineering (AEMCSE). IEEE, 2022. http://dx.doi.org/10.1109/aemcse55572.2022.00037.

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Bavi, Navid, Qinghua Qin, and Boris Martinac. "Finite element simulation of the gating mechanism of mechanosensitive ion channels." In Fourth International Conference on Smart Materials and Nanotechnology in Engineering, edited by Jayantha A. Epaarachchi, Alan Kin-tak Lau, and Jinsong Leng. SPIE, 2013. http://dx.doi.org/10.1117/12.2030203.

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Reports on the topic "Gating mechanism"

1

Routtenberg, Aryeh. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, February 1987. http://dx.doi.org/10.21236/ada179463.

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Routtenberg, A. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, March 1985. http://dx.doi.org/10.21236/ada154511.

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3

Routtenberg, Aryeh. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, April 1985. http://dx.doi.org/10.21236/ada217196.

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