ReviewBiophysical journal2015
Structure, Dynamics, and Allosteric Potential of Ionotropic Glutamate Receptor N-Terminal Domains.
Review in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed.
- InSty: A ProDy Module for Evaluating Protein Interactions and Stability.Journal of molecular biology · 2025Article
- Molecular Insights Into the Sensory Adaption of the Cave-Dwelling LeechEcology and evolution · 2025Article
- Tuning synaptic strength by regulation of AMPA glutamate receptor localization.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
- Glutamate and excitotoxicity in central nervous system disorders: ionotropic glutamate receptors as a target for neuroprotection.Neuroprotection (Chichester, England) · 2024Review
- The Concise Guide to PHARMACOLOGY 2023/24: Ion channels.British journal of pharmacology · 2023Article
- Scipion-EM-ProDy: A Graphical Interface for the ProDy Python Package within the Scipion Workflow Engine Enabling Integration of Databases, Simulations and Cryo-Electron Microscopy Image Processing.International journal of molecular sciences · 2023Article
- Delving into the significance of the His289Tyr single-nucleotide polymorphism in the glutamate ionotropic receptor kainate-1 (Frontiers in molecular neuroscience · 2023Article
- Protein dynamics developments for the large scale and cryoEM: case study of ProDy 2.0.Acta crystallographica. Section D, Structural biology · 2022Review
- GluN2A and GluN2B NMDA receptors use distinct allosteric routes.Nature communications · 2021Article
- Depolarization-dependent Induction of Site-specific Changes in Sialylation onMolecular & cellular proteomics : MCP · 2020Article
- Shared Signature Dynamics Tempered by Local Fluctuations Enables Fold Adaptability and Specificity.Molecular biology and evolution · 2019Article
- The structural arrangement at intersubunit interfaces in homomeric kainate receptors.Scientific reports · 2019Article
- Activation and desensitization of ionotropic glutamate receptors by selectively triggering pre-existing motions.Neuroscience letters · 2019Review
- Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain.Structure (London, England : 1993) · 2019Article
- An inter-dimer allosteric switch controls NMDA receptor activity.The EMBO journal · 2019Article
- Design of Elastic Networks with Evolutionary Optimized Long-Range Communication as Mechanical Models of Allosteric Proteins.Biophysical journal · 2017Article
- Synaptic transmission and plasticity require AMPA receptor anchoring via its N-terminal domain.eLife · 2017Article
- Dependence of prevalence of contiguous pathways in proteins on structural complexity.PloS one · 2017Article
- Pharmacological characterisation of S 47445, a novel positive allosteric modulator of AMPA receptors.PloS one · 2017Article
- Review on the role of AMPA receptor nano-organization and dynamic in the properties of synaptic transmission.Neurophotonics · 2016Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Ionotropic glutamate receptors (iGluRs) are tetrameric cation channels that mediate synaptic transmission and plasticity. They have a unique modular architecture with four domains: the intracellular C-terminal domain (CTD) that is involved in synaptic targeting, the transmembrane domain (TMD) that forms the ion channel, the membrane-proximal ligand-binding domain (LBD) that binds agonists such as L-glutamate, and the distal N-terminal domain (NTD), whose function is the least clear. The extracellular portion, comprised of the LBD and NTD, is loosely arranged, mediating complex allosteric regulation and providing a rich target for drug development. Here, we briefly review recent work on iGluR NTD structure and dynamics, and further explore the allosteric potential for the NTD in AMPA-type iGluRs using coarse-grained simulations. We also investigate mechanisms underlying the established NTD allostery in NMDA-type iGluRs, as well as the fold-related metabotropic glutamate and GABAB receptors. We show that the clamshell motions intrinsically favored by the NTD bilobate fold are coupled to dimeric and higher-order rearrangements that impact the iGluR LBD and ultimately the TMD. Finally, we explore the dynamics of intact iGluRs and describe how it might affect receptor operation in a synaptic environment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.