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Presynaptic Neuronal Pentraxin Receptor Organizes Excitatory and Inhibitory Synapses
Open accessAbstract
Three neuronal pentraxins are expressed in brain, the membrane-bound “neuronal pentraxin receptor” (NPR) and the secreted proteins NP1 and NARP (i.e., NP2). Neuronal pentraxins bind to AMPARs at excitatory synapses and play important, well-documented roles in the activity-dependent regulation of neural circuits via this binding activity. However, it is unknown whether neuronal pentraxins perform roles in synapses beyond modulating postsynaptic AMPAR-dependent plasticity, and whether they may even act in inhibitory synapses. Here, we show that NPR expressed in non-neuronal cells potently induces formation of both excitatory and inhibitory postsynaptic specializations in cocultured hippocampal neurons. Knockdown of NPR in hippocampal neurons, conversely, dramatically decreased assembly and function of both excitatory and inhibitory postsynaptic specializations. Overexpression of NPR rescued the NPR knockdown phenotype but did not in itself change synapse numbers or properties. However, the NPR knockdown decreased the levels of NARP, whereas NPR overexpression produced a dramatic increase in the levels of NP1 and NARP, suggesting that NPR recruits and stabilizes NP1 and NARP on the presynaptic plasma membrane. Mechanistically, NPR acted in excitatory synapse assembly by binding to the N-terminal domain of AMPARs; antagonists of AMPA and GABA receptors selectively inhibited NPR-induced heterologous excitatory and inhibitory synapse assembly, respectively, but did not affect neurexin-1β-induced synapse assembly as a control. Our data suggest that neuronal pentraxins act as signaling complexes that function as general trans-synaptic organizers of both excitatory and inhibitory synapses by a mechanism that depends, at least in part, on the activity of the neurotransmitter receptors at these synapses. SIGNIFICANCE STATEMENT Neuronal pentraxins comprise three neuronal proteins, neuronal pentraxin receptor (NPR) which is a type-II transmembrane protein on the neuronal surface, and secreted neuronal pentraxin-1 and NARP. The general functions of neuronal pentraxins at synapses have not been explored, except for their basic AMPAR binding properties. Here, we examined the functional role of NPR at synapses because it is the only neuronal pentraxin that is anchored to the neuronal cell-surface membrane. We find that NPR is a potent inducer of both excitatory and inhibitory heterologous synapses, and that knockdown of NPR in cultured neurons decreases the density of both excitatory and inhibitory synapses. Our data suggest that NPR performs a general, previously unrecognized function as a universal organizer of synapses.
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“Neuronal pentraxins have been found to be involved in synapse formation and plasticity [37, 38]”
In the citing paper
“The three NPTXs interact, directly or indirectly, with the N-terminal extracellular domain of AMPAR subunits (GluA1, GluA2, GluA3 and GluA4), via their conserved pentraxin domain (Chang et al. 2010; Cho et al. 2008; Lee et al. 2017; Sia et al. 2007; Suzuki et al. 2020).”
From Neuronal pentraxins as biomarkers of synaptic activity: from physiological functions to pathological changes in neurodegeneration (2022) · cites this paper as Lee et al. 2017
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“A potential role of NPTXR as universal organizer of both excitatory and inhibitory synapses was observed in in vitro studies (Lee et al. 2017).”
From Neuronal pentraxins as biomarkers of synaptic activity: from physiological functions to pathological changes in neurodegeneration (2022) · cites this paper as Lee et al. 2017
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Citations
Cites
High-Efficiency Transformation of Mammalian Cells by Plasmid DNA
Chen, C., & Okayama, H. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.8.2745 · Cited by 5,327
Neuroligin Expressed in Nonneuronal Cells Triggers Presynaptic Development in Contacting Axons
Scheiffele, P., Fan, J., Choih, J., Fetter, R., & Serafini, T. (2000) · Cell · doi:10.1016/s0092-8674(00)80877-6 · Cited by 1,218
Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms
Chen, L., Chetkovich, D. M., Petralia, R. S., Sweeney, N. T., Kawasaki, Y., Wenthold, R. J., Bredt, D. S., & Nicoll, R. A. (2000) · Nature · doi:10.1038/35050030 · Cited by 1,111
Definition of the readily releasable pool of vesicles at hippocampal synapses.
Rosenmund, C., & Stevens, C. (1996) · Neuron · doi:10.1016/s0896-6273(00)80146-4 · Cited by 1,084
Neurexins Induce Differentiation of GABA and Glutamate Postsynaptic Specializations via Neuroligins
Graf, E. R., Zhang, X., Jin, S., Linhoff, M. W., & Craig, A. M. (2004) · Cell · doi:10.1016/j.cell.2004.11.035 · Cited by 1,029
Neuroligins Determine Synapse Maturation and Function
Varoqueaux, F., Aramuni, G., Rawson, R. L., Mohrmann, R., Missler, M., Gottmann, K., Zhang, W., Südhof, T. C., & Brose, N. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.003 · Cited by 837
Self-citationα-Neurexins couple Ca2+ channels to synaptic vesicle exocytosis
Missler, M., Zhang, W., Rohlmann, A., Kattenstroth, G., Hammer, R. E., Gottmann, K., & Südhof, T. C. (2003) · Nature · doi:10.1038/nature01755 · Cited by 699
Self-citationNeurexins: Synaptic Cell Surface Proteins Related to the α-Latrotoxin Receptor and Laminin
Ushkaryov, Y. A., Petrenko, A. G., Geppert, M., & Südhof, T. C. (1992) · Science · doi:10.1126/science.1621094 · Cited by 682
Self-citationChubykin, A. A., Atasoy, D., Etherton, M. R., Brose, N., Kavalali, E. T., Gibson, J. R., & Südhof, T. C. (2007) · Neuron · doi:10.1016/j.neuron.2007.05.029 · Cited by 594
Self-citationSynaptic clustering of AMPA receptors by the extracellular immediate-early gene product narp.
O’Brien, R. J., Xu, D., Petralia, R. S., Steward, O., Huganir, R. L., & Worley, P. (1999) · Neuron · doi:10.1016/s0896-6273(00)80782-5 · Cited by 471
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Diering, G. H., & Huganir, R. L. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.018 · Cited by 844
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686
Towards an Understanding of Synapse Formation
Südhof, T. C. (2018) · Neuron · doi:10.1016/j.neuron.2018.09.040 · Cited by 698
Self-citationThe roles of perineuronal nets and the perinodal extracellular matrix in neuronal function
Fawcett, J. W., Oohashi, T., & Pizzorusso, T. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0196-3 · Cited by 589
Structural and Functional Architecture of AMPA-Type Glutamate Receptors and Their Auxiliary Proteins
Greger, I. H., Watson, J. F., & Cull-Candy, S. G. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.009 · Cited by 392
The cell biology of synapse formation
Südhof, T. C. (2021) · Journal of Cell Biology · doi:10.1083/jcb.202103052 · Cited by 358
Self-citationTranscellular Nanoalignment of Synaptic Function
Biederer, T., Kaeser, P. S., & Blanpied, T. A. (2017) · Neuron · doi:10.1016/j.neuron.2017.10.006 · Cited by 352
NPTX2 and cognitive dysfunction in Alzheimer’s Disease
Xiao, M.-F., Xu, D., Craig, M. T., Pelkey, K. A., Chien, C.-C., Shi, Y., Zhang, J., Resnick, S., Pletnikova, O., Salmon, D., et al. (2017) · eLife · doi:10.7554/elife.23798 · Cited by 316
Goetzl, E. J., Abner, E. L., Jicha, G. A., Kapogiannis, D., & Schwartz, J. B. (2018) · The FASEB Journal · doi:10.1096/fj.201700731r · Cited by 219
Farhy-Tselnicker, I., van Casteren, A. C. M., Lee, A., Chang, V. T., Aricescu, A. R., & Allen, N. J. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.053 · Cited by 199
Fluid Biomarkers for Synaptic Dysfunction and Loss
Camporesi, E., Nilsson, J., Brinkmalm, A., Becker, B., Ashton, N. J., Blennow, K., & Zetterberg, H. (2020) · Biomarker Insights · doi:10.1177/1177271920950319 · Cited by 165
Functional organization of postsynaptic glutamate receptors
Scheefhals, N., & MacGillavry, H. D. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.05.002 · Cited by 166
Zhou, J., Wade, S. D., Graykowski, D., Xiao, M.-F., Zhao, B., Giannini, L. A. A., Hanson, J. E., van Swieten, J. C., Sheng, M., Worley, P. F., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.adf0141 · Cited by 152
Galasko, D., Xiao, M., Xu, D., Smirnov, D., Salmon, D. P., Dewit, N., Vanbrabant, J., Jacobs, D., Vanderstichele, H., Vanmechelen, E., et al. (2019) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2019.11.002 · Cited by 133
Longitudinal CSF proteomics identifies NPTX2 as a prognostic biomarker of Alzheimer's disease
Libiger, O., Shaw, L. M., Watson, M. H., Nairn, A. C., Umaña, K. L., Biarnes, M. C., Canet‐Avilés, R. M., Jack, C. R., Breton, Y., Cortes, L., et al. (2021) · Alzheimer's & Dementia · doi:10.1002/alz.12353 · Cited by 108
Two Classes of Secreted Synaptic Organizers in the Central Nervous System
Yuzaki, M. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021317-121322 · Cited by 125
A synthetic synaptic organizer protein restores glutamatergic neuronal circuits
Suzuki, K., Elegheert, J., Song, I., Sasakura, H., Senkov, O., Matsuda, K., Kakegawa, W., Clayton, A. J., Chang, V. T.-C., Ferrer-Ferrer, M., et al. (2020) · Science · doi:10.1126/science.abb4853 · Cited by 128
Cell adhesion and matricellular support by astrocytes of the tripartite synapse
Hillen, A. E. J., Burbach, J. P. H., & Hol, E. M. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.02.002 · Cited by 108
Gómez de San José, N., Massa, F., Halbgebauer, S., Oeckl, P., Steinacker, P., & Otto, M. (2022) · Journal of Neural Transmission · doi:10.1007/s00702-021-02411-2 · Cited by 112
Siedlecki‐Wullich, D., Català-Solsona, J., Fábregas, C., Hernández, I., Clarimón, J., Lleó, A., Boada, M., Saura, C. A., Rodrı́guez-Álvarez, J., & Miñano-Molina, A. J. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0501-4 · Cited by 117
Subunit-specific role for the amino-terminal domain of AMPA receptors in synaptic targeting
Díaz-Alonso, J., Sun, Y. J., Granger, A. J., Levy, J. M., Blankenship, S. M., & Nicoll, R. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707472114 · Cited by 89
Cerebrospinal fluid biomarker panel for synaptic dysfunction in Alzheimer's disease
Nilsson, J., Gobom, J., Sjödin, S., Brinkmalm, G., Ashton, N. J., Svensson, J., Johansson, P., Portelius, E., Zetterberg, H., Blennow, K., et al. (2021) · Alzheimer's & Dementia: Diagnosis, Assessment & Disease Monitoring · doi:10.1002/dad2.12179 · Cited by 82
Nilsson, J., Binette, A. P., Palmqvist, S., Brum, W. S., Janelidze, S., Ashton, N. J., Spotorno, N., Stomrud, E., Gobom, J., Zetterberg, H., et al. (2024) · Brain · doi:10.1093/brain/awae032 · Cited by 90
The Basic Characteristics of the Pentraxin Family and Their Functions in Tumor Progression
Wang, Z., Wang, X., Zou, H., Dai, Z., Feng, S., Zhang, M., Xiao, G., Liu, Z., & Cheng, Q. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01757 · Cited by 73
AMPA receptor trafficking and LTP: Carboxy-termini, amino-termini and TARPs
Díaz-Alonso, J., & Nicoll, R. A. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108710 · Cited by 66
Fossati, G., Pozzi, D., Canzi, A., Mirabella, F., Valentino, S., Morini, R., Ghirardini, E., Filipello, F., Moretti, M., Gotti, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201899529 · Cited by 67
Kanda, M., Shimizu, D., Sawaki, K., Nakamura, S., Umeda, S., Miwa, T., Tanaka, H., Tanaka, C., Hayashi, M., Iguchi, Y., et al. (2020) · Molecular Cancer · doi:10.1186/s12943-020-01251-0 · Cited by 67
Nilsson, J., Cousins, K. A. Q., Gobom, J., Portelius, E., Chen‐Plotkin, A. S., Shaw, L. M. J., Grossman, M., Irwin, D. J., Trojanowski, J. Q., Zetterberg, H., et al. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12809 · Cited by 62
A model of human neural networks reveals NPTX2 pathology in ALS and FTLD
Hruška-Plocháň, M., Wiersma, V. I., Betz, K. M., Mallona, I., Ronchi, S., Maniecka, Z., Hock, E., Tantardini, E., Laferrière, F., Sahadevan, S., et al. (2024) · Nature · doi:10.1038/s41586-024-07042-7 · Cited by 73
Mackmull, M., Nagel, L., Sesterhenn, F., Muntel, J., Großbach, J., Stalder, P., Bruderer, R., Reiter, L., van de Berg, W. D. J., de Souza, N., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00837-0 · Cited by 47
Begcevic, I., Tsolaki, M., Brinc, D., Brown, M., Martinez-Morillo, E., Lazarou, I., Kozori, M., Tagaraki, F., Nenopoulou, S., Gkioka, M., et al. (2018) · F1000Research · doi:10.12688/f1000research.15095.1 · Cited by 51
Moreno‐Rodríguez, M., Perez, S. E., Nadeem, M., Malek‐Ahmadi, M. H., & Mufson, E. J. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-1723-x · Cited by 53
Spatiotemporal patterns of gene expression around implanted silicon electrode arrays
Thompson, C. H., Saxena, A., Heelan, N., Salatino, J. W., & Purcell, E. K. (2021) · Journal of Neural Engineering · doi:10.1088/1741-2552/abf2e6 · Cited by 47
van Oostrum, M., Campbell, B., Seng, C., Müller, M., tom Dieck, S., Hammer, J., Pedrioli, P. G. A., Földy, C., Tyagarajan, S. K., & Wollscheid, B. (2020) · Nature Communications · doi:10.1038/s41467-020-18494-6 · Cited by 46
The Role of Neuronal Pentraxin 2 (NP2) in Regulating Glutamatergic Signaling and Neuropathology
Chapman, G., Shanmugalingam, U., & Smith, P. D. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00575 · Cited by 48
Poulsen, L. L. C., Plá, I., Sánchez, A., Grøndahl, M. L., Marko‐Varga, G., Andersen, C. Y., Englund, A. L. M., & Malm, J. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.110522 · Cited by 47
Jiang, X., Sando, R. C., & Südhof, T. C. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000173118 · Cited by 47
Self-citationde Bartolomeis, A., Buonaguro, E. F., Latte, G., Rossi, R., Marmo, F., Iasevoli, F., & Tomasetti, C. (2017) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2017.00240 · Cited by 44
Barschke, P., Oeckl, P., Steinacker, P., Al Shweiki, M. R., Weishaupt, J. H., Landwehrmeyer, G. B., Anderl-Straub, S., Weydt, P., Diehl-Schmid, J., Danek, A., et al. (2020) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2019-322476 · Cited by 45
Jiang, W., Wei, M., Liu, M., Pan, Y., Cao, D., Yang, X., & Zhang, C. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.0729-17.2017 · Cited by 47
Self-citationAstrocytic Factors Controlling Synaptogenesis: A Team Play
Fossati, G., Matteoli, M., & Menna, E. (2020) · Cells · doi:10.3390/cells9102173 · Cited by 46
Higginbotham, L. A., Carter, E. K., Dammer, E. B., Haque, R. U., Johnson, E. C. B., Duong, D. M., Yin, L., Jager, P. L. D., Bennett, D. A., Felsky, D., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106286 · Cited by 41
The interplay between electrical and chemical synaptogenesis
Jabeen, S., & Thirumalai, V. (2018) · Journal of Neurophysiology · doi:10.1152/jn.00398.2018 · Cited by 44
Lim, B., Sando, S. B., Grøntvedt, G. R., Bråthen, G., & Diamandis, E. P. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.03.013 · Cited by 39
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Yang, L., Wei, M., Xing, B., & Zhang, C. (2022) · Bioscience Reports · doi:10.1042/bsr20212411 · Cited by 42
Self-citationAlamro, H., Bajić, V., Mačvanin, M., Isenović, E. R., Gojobori, T., Essack, M., & Gao, X. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.1084656 · Cited by 43
AMPA receptor anchoring at CA1 synapses is determined by N-terminal domain and TARP γ8 interactions
Watson, J. F., Pinggera, A., Ho, H., & Greger, I. H. (2021) · Nature Communications · doi:10.1038/s41467-021-25281-4 · Cited by 38
Wang, Z., Jin, T., Le, Q., Liu, C., Wang, X., Wang, F., & Ma, L. (2019) · Biological Psychiatry · doi:10.1016/j.biopsych.2019.10.009 · Cited by 32
Bolsewig, K., Hok-A-Hin, Y. S., Sepe, F. N., Boonkamp, L., Jacobs, D., Bellomo, G., Paoletti, F. P., Vanmechelen, E., Teunissen, C. E., Parnetti, L., et al. (2022) · Journal of Alzheimer's Disease · doi:10.3233/jad-220318 · Cited by 36
Sanfilippo, P., Kim, A. J., Bhukel, A., Yoo, J., Mirshahidi, P. S., Pandey, V., Bevir, H., Yuen, A., Mirshahidi, P. S., Guo, P., et al. (2024) · Neuron · doi:10.1016/j.neuron.2023.12.014 · Cited by 36
Ju, L.-S., Yang, J., Zhu, T., Liu, P., & Yang, J. (2022) · BMC Psychiatry · doi:10.1186/s12888-022-03838-x · Cited by 35
Ramesh, V., Liu, F., Minto, M. S., Chan, U., & West, A. E. (2023) · eLife · doi:10.7554/elife.86273 · Cited by 37
Boudkkazi, S., Schwenk, J., Nakaya, N., Brechet, A., Kollewe, A., Harada, H., Bildl, W., Kulik, A., Dong, L., Sultana, A., et al. (2023) · Neuron · doi:10.1016/j.neuron.2023.07.013 · Cited by 33
Neuronal pentraxin 1: A synaptic-derived plasma biomarker in Alzheimer's disease
Ma, Q., Teng, E., Zuo, X., Jones, M. R., Teter, B., Zhao, E. Y., Zhu, C., Bilousova, T. V., Gylys, K. H., Apostolova, L. G., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.02.014 · Cited by 34
Compartment-Specific Neurexin Nanodomains Orchestrate Tripartite Synapse AssemblyPreprint
Trotter, J. H., Dargaei, Z., Sclip, A., Essayan-Perez, S., Liakath‐Ali, K., Raju, K., Nabet, A., Liu, X., Wöhr, M., & Südhof, T. C. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.21.262097 · Cited by 35
Self-citationAssociation between serum NPTX2 and cognitive function in patients with vascular dementia
Shao, K., Shan, S., Ru, W., & Ma, C. (2020) · Brain and Behavior · doi:10.1002/brb3.1779 · Cited by 25
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Differential nanoscale organization of excitatory synapses onto excitatory vs. inhibitory neurons
Dharmasri, P. A., Levy, A. D., & Blanpied, T. A. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315379121 · Cited by 23
Molecular signatures of cortical expansion in the human foetal brain
Ball, G., Oldham, S., Kyriakopoulou, V., Williams, L. Z. J., Karolis, V. R., Price, A. N., Hutter, J. M., Seal, M. L., Alexander‐Bloch, A. F., Hajnal, J. V., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54034-2 · Cited by 28
Biology of AMPA receptor interacting proteins - From biogenesis to synaptic plasticity
Matthews, P. M., Pinggera, A., Kampjut, D., & Greger, I. H. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108709 · Cited by 25
Revealing NOTCH-dependencies in synaptic targets associated with Alzheimer's disease
Perna, A., Marathe, S. V., Dreos, R., Falquet, L., Akarsu, H., & Auber, L. A. (2021) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2021.103657 · Cited by 25
Gulyássy, P., Völgyi, K., Tóth, V., Györffy, B. A., Puska, G., Simor, A., Juhász, G. D., Drahos, L., & Kékesi, K. A. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02699-x · Cited by 28
Lim, B., Tsolaki, M., Soosaipillai, A., Brown, M., Zilakaki, M., Tagaraki, F., Fotiou, D., Koutsouraki, E., Grosi, E., Prassas, I., et al. (2019) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2019-0428 · Cited by 25
Dulewicz, M., Kulczyńska-Przybik, A., Słowik, A., Borawska, R., & Mroczko, B. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10194575 · Cited by 22
Shantaraman, A., Dammer, E. B., Ugochukwu, O., Duong, D. M., Yin, L., Carter, E. K., Gearing, M., Chen‐Plotkin, A. S., Lee, E. B., Trojanowski, J. Q., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00749-1 · Cited by 23
Photoaffinity Probes for the Identification of Sequence-Specific Glycosaminoglycan-Binding Proteins
Joffrin, A. M., & Hsieh‐Wilson, L. C. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c06046 · Cited by 22
Wang, R., Man, Y., Zhou, M., Zhu, Y., Wang, L., & Yang, J. (2021) · Neuroreport · doi:10.1097/wnr.0000000000001584 · Cited by 20
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Ning, L., Shen, R., Xie, B., Jiang, Y., Geng, X., & Dong, W. (2024) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlae093 · Cited by 19
Carmel, M., Michaelovsky, E., Weinberger, R., Frisch, A., Mekori‐Domachevsky, E., Gothelf, D., & Weizman, A. (2020) · The World Journal of Biological Psychiatry · doi:10.1080/15622975.2020.1747113 · Cited by 19
Lee, J. S., Sun, Y., Soares, A. R., Fai, C., Picciotto, M. R., & Guo, J. U. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.08.032 · Cited by 19
Liu, J., Wang, M., Sun, L., Pan, N. C., Zhang, C., Zhang, J., Zuo, Z., He, S., Wu, Q., & Wang, X. (2020) · Protein & Cell · doi:10.1007/s13238-020-00720-y · Cited by 18
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Nowacka, A., Getz, A. M., Bessa‐Neto, D., & Choquet, D. (2024) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2023.0220 · Cited by 21
Podvin, S., Jones, A. C., Liu, Q., Aulston, B. D., Mosier, C., Ames, J., Winston, C. N., Lietz, C. B., Jiang, Z., O’Donoghue, A. J., et al. (2021) · ACS Omega · doi:10.1021/acsomega.1c00660 · Cited by 16
Hao, Y., Liu, H.-W., Zeng, X.-T., Wang, Y., Zeng, W.-X., Qian, K.-Y., Li, L., Chi, M.-X., Gao, S.-B., Hu, Z.-T., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37137-0 · Cited by 14
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Saunders, T. S., Gadd, D. A., Spires‐Jones, T. L., King, D., Ritchie, C. W., & Terrera, G. M. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15656 · Cited by 12
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Metadata
- Authors
- Lee, S.-J., Wei, M., Zhang, C., Maxeiner, S., Pak, C., Calado Botelho, S., Trotter, J., Sterky, F. H., & Südhof, T. C.
- Affiliations
- Stanford Medicine (US)
- Peking University (CN)
- Howard Hughes Medical Institute (US)
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2016-12-16
- Volume
- 37
- Issue
- 5
- Pages
- 1062-1080
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC5296791
- OpenAlex
- W2562584466
- Cited by
- 146
- References
- 36
- Citations by year
- 2026: 9 · 2025: 12 · 2024: 28 · 2023: 13 · 2022: 18 · 2021: 21 · 2020: 21 · 2019: 6 · 2018: 9 · 2017: 9
- FWCI
- 4.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Mental Health (R01MH052804, R37MH052804)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (F32HD078051)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Immunology and Microbiology › Immunology › Biomarkers in Disease Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- NARP, excitatory synapses, inhibitory synapses, AMPA receptors, GABA receptors, trans-synaptic signaling, postsynaptic specialization, hippocampal neurons, synaptic plasticity, presynaptic plasma membrane
- MeSH terms
- Pentraxins, Animals, C-Reactive Protein, Hippocampus, Humans, Nerve Tissue Proteins, Neurons, Receptors, Cell Surface, Synapses, Receptors, AMPA, Patch-Clamp Techniques, Excitatory Amino Acid Antagonists, GABA Antagonists, Coculture Techniques, Excitatory Postsynaptic Potentials, RNA, Small Interfering, Mice, Gene Knockdown Techniques, HEK293 Cells
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