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Titlebook: Ionotropic Glutamate Receptor Technologies; Gabriela K. Popescu Book 2016 Springer Science+Business Media New York 2016 atomic organizatio

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發(fā)表于 2025-3-21 18:03:48 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Ionotropic Glutamate Receptor Technologies
編輯Gabriela K. Popescu
視頻videohttp://file.papertrans.cn/476/475249/475249.mp4
概述Includes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts
叢書名稱Neuromethods
圖書封面Titlebook: Ionotropic Glutamate Receptor Technologies;  Gabriela K. Popescu Book 2016 Springer Science+Business Media New York 2016 atomic organizatio
描述This detailed volume explores key technologies that are used currently to investigate iGluR structure, function and physiology.? Chapters in this book cover methods to help illuminate the assembly, trafficking, molecular composition and subcellular location of iGluRs;?approaches used to understand the atomic organization of iGluRs; and techniques to monitor receptor activity in real time. Written in the popular .Neuromethods. series style, chapters include the kind of detail and key advice from the specialists needed to get successful results in your own laboratory..Concise and easy-to-use, .Ionotropic Glutamate Receptor Technologies. aims to facilitate the implementation of specific methods to iGluR investigations..
出版日期Book 2016
關(guān)鍵詞atomic organization; iGluR physiology; iGluR function; iGluR structure; intramolecular motions; receptor
版次1
doihttps://doi.org/10.1007/978-1-4939-2812-5
isbn_softcover978-1-4939-4895-6
isbn_ebook978-1-4939-2812-5Series ISSN 0893-2336 Series E-ISSN 1940-6045
issn_series 0893-2336
copyrightSpringer Science+Business Media New York 2016
The information of publication is updating

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Assessing The Effects of Ligand-Binding Mutations to AMPA and Kainate Receptor Kineticss measures of channel function have yet to be fully elucidated. In this chapter I describe our approach to making single-point mutations in the ligand-binding domain and assessing the functional consequences of those mutations on critical measures of receptor-channel function.
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Timing AMPA Receptor Activation with Laser-Pulse Photolysised to characterize the mechanism of channel regulation by modulatory agents, and the structure-function relationship. Here, I describe the instrumentation of laser-pulse photolysis, data analysis, and advantages as well as limitations of this technique.
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Electrophysiological Tagging of Ionotropic Glutamate Receptorsdetection using standard whole-cell current recordings. This method is highly sensitive and specific to detect the incorporation of recombinant ionotropic glutamate receptors into functional synapses.
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NMR Approaches to Functional Dynamics of Genetically Separated iGluR Domainse ligand-binding domain of an AMPA receptor (GluA2) to permit studies of protein dynamics by NMR. The strategies for resonance assignment and the experiments used to study dynamics are also described.
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Analysis of Whole-Cell NMDA Receptor Currentssensitization/resensitization, and the probability of channel opening are determined. Besides the kinetic parameters of the receptor, the number of ion channels in the cell membrane and single-channel conductance are estimated from whole-cell recordings.
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