Hille, B. Ion Channels of Excitable Membranes 3rd edn (Sinauer, 2001).<\/p>\n
Jahr, C. E. & Stevens, C. F. Glutamate activates multiple single channel conductances in hippocampal neurons. Nature 325, 522\u2013525 (1987).<\/p>\n
Article<\/a>\u00a0 Cull-Candy, S. G. & Usowicz, M. M. Multiple-conductance channels activated by excitatory amino acids in cerebellar neurons. Nature 325, 525\u2013528 (1987).<\/p>\n Article<\/a>\u00a0 Schneggenburger, R. & Ascher, P. Coupling of permeation and gating in an NMDA-channel pore mutant. Neuron 18, 167\u2013177 (1997).<\/p>\n Article<\/a>\u00a0 Banke, T. G. & Traynelis, S. F. Activation of NR1\/NR2B NMDA receptors. Nat. Neurosci. 6, 144\u2013152 (2003).<\/p>\n Article<\/a>\u00a0 Popescu, G. & Auerbach, A. Modal gating of NMDA receptors and the shape of their synaptic response. Nat. Neurosci. 6, 476\u2013483 (2003).<\/p>\n Article<\/a>\u00a0 Bliss, T. V. P. & Collingridge, G. L. A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361, 31\u201339 (1993).<\/p>\n Article<\/a>\u00a0 Malenka, R. C. & Bear, M. F. LTP and LTD: an embarrassment of riches. Neuron 44, 5\u201321 (2004).<\/p>\n Article<\/a>\u00a0 Hansen, K. B. et al. Structure, function, and pharmacology of glutamate receptor ion channels. Pharmacol. Rev. 73, 298\u2013487 (2021).<\/p>\n Article<\/a>\u00a0 Karakas, E. & Furukawa, H. Crystal structure of a heterotetrameric NMDA receptor ion channel. Science 344, 992\u2013997 (2014).<\/p>\n Article<\/a>\u00a0 Lee, C. H. et al. NMDA receptor structures reveal subunit arrangement and pore architecture. Nature 511, 191\u2013197 (2014).<\/p>\n Article<\/a>\u00a0 Wang, J. X. & Furukawa, H. Dissecting diverse functions of NMDA receptors by structural biology. Curr. Opin. Struct. Biol. 54, 34\u201342 (2019).<\/p>\n Article<\/a>\u00a0 Mony, L. & Paoletti, P. Mechanisms of NMDA receptor regulation. Curr. Opin. Neurobiol. 83, 102815 (2023).<\/p>\n Article<\/a>\u00a0 Zhou, C. & Tajima, N. Structural insights into NMDA receptor pharmacology. Biochem. Soc. Trans. 51, 1713\u20131731 (2023).<\/p>\n Article<\/a>\u00a0 Wu, E., Zhang, J., Zhang, J. & Zhu, S. Structural insights into gating mechanism and allosteric regulation of NMDA receptors. Curr. Opin. Neurobiol. 83, 102806 (2023).<\/p>\n Article<\/a>\u00a0 Hansen, K. B. et al. Structure, function, and allosteric modulation of NMDA receptors. J. Gen. Physiol. 150, 1081\u20131105 (2018).<\/p>\n Article<\/a>\u00a0 Ratner, M. H., Kumaresan, V. & Farb, D. H. Neurosteroid actions in memory and neurologic\/neuropsychiatric disorders. Front. Endocrinol. 10, 169 (2019).<\/p>\n Article<\/a>\u00a0 Hanson, J. E. et al. Therapeutic potential of N-methyl-D-aspartate receptor modulators in psychiatry. Neuropsychopharmacology 49, 51\u201366 (2024).<\/p>\n Article<\/a>\u00a0 Zorumski, C. F. et al. New directions in neurosteroid therapeutics in neuropsychiatry. Neurosci. Biobehav. Rev. 172, 106119 (2025).<\/p>\n Article<\/a>\u00a0 Hrcka Krausova, B. et al. Site of action of brain neurosteroid pregnenolone sulfate at the N-methyl-D-aspartate receptor. J. Neurosci. 40, 5922 (2020).<\/p>\n Article<\/a>\u00a0 Perszyk, R. E. et al. Biased modulators of NMDA receptors control channel opening and ion selectivity. Nat. Chem. Biol. 16, 188\u2013196 (2020).<\/p>\n Article<\/a>\u00a0 Chou, T. H. et al. Molecular mechanism of ligand gating and opening of NMDA receptor. Nature 632, 209\u2013217 (2024).<\/p>\n Article<\/a>\u00a0 Ullman, E. Z. et al. Mechanisms of action underlying conductance-modifying positive allosteric modulators of the NMDA receptor. Mol. Pharmacol. 106, 334\u2013353 (2024).<\/p>\n Article<\/a>\u00a0 Paul, S. M. et al. The major brain cholesterol metabolite 24(S)-hydroxycholesterol is a potent allosteric modulator of N-methyl-D-aspartate receptors. J. Neurosci. 33, 17290\u201317300 (2013).<\/p>\n Article<\/a>\u00a0 Wu, F. S., Gibbs, T. T. & Farb, D. H. Pregnenolone sulfate: a positive allosteric modulator at the N-methyl-D-aspartate receptor. Mol. Pharmacol. 40, 333\u2013336 (1991).<\/p>\n Article<\/a>\u00a0 Fritzemeier, R. G. et al. Thienopyrimidinone derivatives as a GluN2B\/C\/D biased, positive allosteric modulator of the N-methyl-d-aspartate receptor. J. Med. Chem. 68, 9303\u20139322 (2025).<\/p>\n Article<\/a>\u00a0 Premkumar, L. S., Qin, F. & Auerbach, A. Subconductance States of a mutant NMDA receptor channel kinetics, calcium, and voltage dependence. J. Gen. Physiol. 109, 181\u2013189 (1997).<\/p>\n Article<\/a>\u00a0 Stern, P., B\u00e9h\u00e9, P., Schoepfer, R. & Colquhoun, D. Single-channel conductances of NMDA receptors expressed from cloned cDNAs: comparison with native receptors. Proc. R. Soc. Lond. B 250, 271\u2013277 (1997).<\/p>\n ADS<\/a>\u00a0 Banke, T. G., Dravid, S. M. & Traynelis, S. F. Protons trap NR1\/NR2B NMDA receptors in a nonconducting state. J. Neurosci. 25, 42\u201351 (2005).<\/p>\n Article<\/a>\u00a0 Huang, Z. & Gibb, A. J. Mg2+ block properties of triheteromeric GluN1\u2013GluN2B\u2013GluN2D NMDA receptors on neonatal rat substantia nigra pars compacta dopaminergic neurones. J. Physiol. 592, 2059\u20132078 (2014).<\/p>\n Article<\/a>\u00a0 Kang, H. et al. Structural basis for channel gating and blockade in tri-heteromeric GluN1-2B-2D NMDA receptor. Neuron https:\/\/doi.org\/10.1016\/j.neuron.2025.01.013<\/a> (2025).<\/p>\n Article<\/a>\u00a0 Chou, T. H., Tajima, N., Romero-Hernandez, A. & Furukawa, H. Structural basis of functional transitions in mammalian NMDA receptors. Cell 182, 357\u2013371 (2020).<\/p>\n Article<\/a>\u00a0 Tajima, N. et al. Activation of NMDA receptors and the mechanism of inhibition by ifenprodil. Nature 534, 63\u201368 (2016).<\/p>\n Article<\/a>\u00a0 Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A. & Sansom, M. S. P. HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graphics 14, 354\u2013360 (1996).<\/p>\n Article<\/a>\u00a0 Amin, J. B. et al. Two gates mediate NMDA receptor activity and are under subunit-specific regulation. Nat. Commun. 14, 1623 (2023).<\/p>\n Article<\/a>\u00a0 Twomey, E. C., Yelshanskaya, M. V., Grassucci, R. A., Frank, J. & Sobolevsky, A. I. Channel opening and gating mechanism in AMPA-subtype glutamate receptors. Nature 549, 60\u201365 (2017).<\/p>\n Article<\/a>\u00a0 Gangwar, S. P. et al. Kainate receptor channel opening and gating mechanism. Nature 630, 762\u2013768 (2024).<\/p>\n Article<\/a>\u00a0 Swanson, G. T., Kamboj, S. K. & Cull-Candy, S. G. Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition. J. Neurosci. 17, 58 (1997).<\/p>\n Article<\/a>\u00a0 Zhang, W. et al. A transmembrane accessory subunit that modulates kainate-type glutamate receptors. Neuron 61, 385\u2013396 (2009).<\/p>\n Article<\/a>\u00a0 Watanabe, J., Beck, C., Kuner, T., Premkumar, L. S. & Wollmuth, L. P. DRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels. J. Neurosci. 22, 10209\u201310216 (2002).<\/p>\n Article<\/a>\u00a0 Perszyk, R. E. et al. Hodgkin-Huxley-Katz Prize Lecture: genetic and pharmacological control of glutamate receptor channel through a highly conserved gating motif. J. Physiol. https:\/\/doi.org\/10.1113\/JP278086<\/a> (2020).<\/p>\n Article<\/a>\u00a0 Rosenmund, C., Stern-Bach, Y. & Stevens, C. F. The tetrameric structure of a glutamate receptor channel. Science 280, 1596\u20131599 (1998).<\/p>\n Article<\/a>\u00a0 Yelshanskaya, M. V., Patel, D. S., Kottke, C. M., Kurnikova, M. G. & Sobolevsky, A. I. Opening of glutamate receptor channel to subconductance levels. Nature 605, 172\u2013178 (2022).<\/p>\n Article<\/a>\u00a0 Coombs, I. D. & Cull-Candy, S. G. Single-channel mechanisms underlying the function, diversity and plasticity of AMPA receptors. Neuropharmacology 198, 108781 (2021).<\/p>\n Article<\/a>\u00a0 Benveniste, M. & Mayer, M. L. Kinetic analysis of antagonist action at N-methyl-D-aspartic acid receptors. Two binding sites each for glutamate and glycine. Biophys. J. 59, 560\u2013573 (1991).<\/p>\n Article<\/a>\u00a0 Hale, W. D., Huganir, R. L. & Twomey, E. C. Architecture, activation, and conformational plasticity in the GluA4 AMPA receptor. Preprint at bioRxiv https:\/\/doi.org\/10.1101\/2025.06.12.659357<\/a> (2025).<\/p>\n Furukawa, H., Simorowski, N. & Michalski, K. Effective production of oligomeric membrane proteins by EarlyBac-insect cell system. Methods Enzymol. 653, 3\u201319 (2021).<\/p>\n Article<\/a>\u00a0 Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290\u2013296 (2017).<\/p>\n Article<\/a>\u00a0 Rubinstein, J. L. & Brubaker, M. A. Alignment of cryo-EM movies of individual particles by optimization of image translations. J. Struct. Biol. 192, 188\u2013195 (2015).<\/p>\n Article<\/a>\u00a0 Punjani, A., Zhang, H. & Fleet, D. J. Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction. Nat. Methods 17, 1214\u20131221 (2020).<\/p>\n Article<\/a>\u00a0 Chou, T. H. et al. Structural insights into binding of therapeutic channel blockers in NMDA receptors. Nat. Struct. Mol. Biol. 29, 507\u2013518 (2022).<\/p>\n Article<\/a>\u00a0 Meng, E. C. et al. UCSF ChimeraX: tools for structure building and analysis. Protein Sci. 32, e4792 (2023).<\/p>\n Article<\/a>\u00a0 Liebschner, D. et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallogr. D 75, 861\u2013877 (2019).<\/p>\n Article<\/a>\u00a0 Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486\u2013501 (2010).<\/p>\n Article<\/a>\u00a0 Lewis, C. A. Ion-concentration dependence of the reversal potential and the single channel conductance of ion channels at the frog neuromuscular junction. J. Physiol. 286, 417\u2013445 (1979).<\/p>\n Article<\/a>\u00a0 Jatzke, C., Hernandez, M. & Wollmuth, L. P. Extracellular vestibule determinants of Ca2+ influx in Ca2+-permeable AMPA receptor channels. J. Physiol. 549, 439\u2013452 (2003).<\/p>\n Article<\/a>\u00a0 Webb, B. & Sali, A. Comparative protein structure modeling using MODELLER. Curr. Protoc.Bioinform. 2016, 5.6.1\u20135.6.37 (2016).<\/p>\n Lindorff-Larsen, K. et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins 78, 1950\u20131958 (2010).<\/p>\n Article<\/a>\u00a0 Joung, I. S. & Cheatham, T. E. III Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations. J. Phys. Chem. B 112, 9020\u20139041 (2008).<\/p>\n Article<\/a>\u00a0 Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W. & Klein, M. L. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79, 926\u2013935 (1983).<\/p>\n Article<\/a>\u00a0 Darden, T., York, D. & Pedersen, L. Particle mesh Ewald: an N\u00b7log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089\u201310092 (1993).<\/p>\n Article<\/a>\u00a0 Hess, B., Bekker, H., Berendsen, H. J. C. & Fraaije, J. G. E. M. LINCS: a linear constraint solver for molecular simulations. J. Comput. Chem. 18, 1463\u20131472 (1997).<\/p>\n Article<\/a>\u00a0 Nos\u00e9, S. A unified formulation of the constant temperature molecular dynamics methods. J. Chem. Phys. 81, 511\u2013519 (1984).<\/p>\n Article<\/a>\u00a0 Abraham, M. J. et al. GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX 1\u20132, 19\u201325 (2015).<\/p>\n Article<\/a>\u00a0
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n PubMed<\/a>\u00a0
\n PubMed Central<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n
\n ADS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n","protected":false},"excerpt":{"rendered":"Hille, B. Ion Channels of Excitable Membranes 3rd edn (Sinauer, 2001). Jahr, C. E. & Stevens, C. F.…\n","protected":false},"author":2,"featured_media":260638,"comment_status":"","ping_status":"","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[34],"tags":[140574,97,1159,140723,1160,79],"class_list":{"0":"post-260637","1":"post","2":"type-post","3":"status-publish","4":"format-standard","5":"has-post-thumbnail","7":"category-health","8":"tag-cryoelectron-microscopy","9":"tag-health","10":"tag-humanities-and-social-sciences","11":"tag-ion-channels-in-the-nervous-system","12":"tag-multidisciplinary","13":"tag-science"},"_links":{"self":[{"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/posts\/260637","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/comments?post=260637"}],"version-history":[{"count":0,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/posts\/260637\/revisions"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/media\/260638"}],"wp:attachment":[{"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/media?parent=260637"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/categories?post=260637"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/tags?post=260637"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}