The DOI matches its Crossref record; 77 of the 79 references it cites were found in a registry or an index.
Postsynaptic Scaffolds of Excitatory and Inhibitory Synapses in Hippocampal Neurons: Maintenance of Core Components Independent of Actin Filaments and Microtubules
Open accessAbstract
The mechanisms responsible for anchoring molecular components of postsynaptic specializations in the mammalian brain are not well understood but are presumed to involve associations with cytoskeletal elements. Here we build on previous studies of neurotransmitter receptors (Allison et al., 1998) to analyze the modes of attachment of scaffolding and signal transducing proteins of both glutamate and GABA postsynaptic sites to either the microtubule or microfilament cytoskeleton. Hippocampal pyramidal neurons in culture were treated with latrunculin A to depolymerize actin, with vincristine to depolymerize microtubules, or with Triton X-100 to extract soluble proteins. The synaptic clustering of PSD-95, a putative NMDA receptor anchoring protein and a core component of the postsynaptic density (PSD), was unaffected by actin depolymerization, microtubule depolymerization, or detergent extraction. The same was largely true for GKAP, a PSD-95-interacting protein. In contrast, the synaptic clustering of Ca(2+)/calmodulin-dependent protein kinase II (CaMKII)alpha, another core component of the PSD, was completely dependent on an intact actin cytoskeleton and was partially disrupted by detergent. Drebrin and alpha-actinin-2, actin-binding proteins concentrated in spines, were also dependent on F-actin for synaptic localization but were unaffected by detergent extraction. Surprisingly, the subcellular distributions of the inhibitory synaptic proteins GABA(A)R and gephyrin, which has a tubulin-binding motif, were unaffected by depolymerization of microtubules or actin or by detergent extraction. These studies reveal an unsuspected heterogeneity in the modes of attachment of postsynaptic proteins to the cytoskeleton and support the idea that PSD-95 and gephyrin may be core scaffolding components independent of the actin or tubulin cytoskeleton.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Lastly, the actin cytoskeleton is known to mediate receptor positioning (Gudheti et al., 2013) and its depolymerization was shown to reduce glutamate receptor accumulations in spines (Allison et al., 2000).”
From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Allison et al., 2000
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Domain Interaction Between NMDA Receptor Subunits and the Postsynaptic Density Protein PSD-95
Kornau, H., Schenker, L. T., Kennedy, M. B., & Seeburg, P. H. (1995) · Science · doi:10.1126/science.7569905 · Cited by 1,916
(1991) · Medical Entomology and Zoology · Cited by 1,512
Dendritic spine changes associated with hippocampal long-term synaptic plasticity
Engert, F., & Bonhoeffer, T. (1999) · Nature · doi:10.1038/19978 · Cited by 1,412
Rat hippocampal neurons in dispersed cell culture.
Banker, G. A., & Cowan, W. M. (1977) · Brain Research · doi:10.1016/0006-8993(77)90594-7 · Cited by 1,110
Harris, K. M., & Kater, S. B. (1994) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.17.030194.002013 · Cited by 1,020
Naisbitt, S., Kim, E., Tu, J. C., Xiao, B., Sala, C., Valtschanoff, J., Weinberg, R. J., Worley, P. F., & Sheng, M. (1999) · Neuron · doi:10.1016/s0896-6273(00)80809-0 · Cited by 1,009
Postsynaptic clustering of major GABAA receptor subtypes requires the γ2 subunit and gephyrin
Essrich, C., Lorez, M., Benson, J. A., Fritschy, J., & Lüscher, B. (1998) · Nature Neuroscience · doi:10.1038/2798 · Cited by 856
GABAA-receptor-associated protein links GABAA receptors and the cytoskeleton
Wang, H.-B., Bedford, F., Brandon, N., Moss, S., & Olsen, R. (1999) · Nature · doi:10.1038/16264 · Cited by 754
Shen, K., & Meyer, T. (1999) · Science · doi:10.1126/science.284.5411.162 · Cited by 673
Competitive binding of α-actinin and calmodulin to the NMDA receptor
Wyszynski, M., Lin, J., Rao, A., Nigh, E., Beggs, A. H., Craig, A. M., & Sheng, M. (1997) · Nature · doi:10.1038/385439a0 · Cited by 596
Self-citation
Cited by
Sorted by citations
Items 101–200 of 243
Grossman, S. D., Futter, M., Snyder, G. L., Allen, P. B., Nairn, A. C., Greengard, P., & Hsieh‐Wilson, L. C. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02491.x · Cited by 62
Synaptic structure and diffusion dynamics of synaptic receptors
Triller, A., & Choquet, D. (2003) · Biology of the Cell · doi:10.1016/j.biolcel.2003.07.001 · Cited by 67
MacGillavry, H. D., Kerr, J. M., Kassner, J. D., Frost, N. A., & Blanpied, T. A. (2015) · European Journal of Neuroscience · doi:10.1111/ejn.13129 · Cited by 63
Li, X., Serwanski, D. R., Miralles, C. P., Bahr, B. A., & Blas, A. L. D. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04635.x · Cited by 54
Enhanced Vulnerability to NMDA Toxicity in Sublethal Traumatic Neuronal Injury In Vitro
Arundine, M., Chopra, G. K., Wrong, A., Lei, S., Aarts, M. M., MacDonald, J. F., & Tymianski, M. (2003) · Journal of Neurotrauma · doi:10.1089/089771503322686166 · Cited by 51
Silverman, M. A., Johnson, S., Gurkins, D., Farmer, M., Lochner, J. E., Rosa, P., & Scalettar, B. A. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4694-04.2005 · Cited by 52
Glutamate-induced δ-catenin redistribution and dissociation from postsynaptic receptor complexes
Jones, S. B., Lanford, G. W., Chen, Y., Moribito, M., Kim, K., & Lu, Q. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00532-8 · Cited by 50
Hodges, J., Martín‐Vílchez, S., Asmussen, H., Whitmore, L. A., & Horwitz, A. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101770 · Cited by 50
Cytoskeletal makeup of the synapse: Shaft versus spine
Bucher, M., Fanutza, T., & Mikhaylova, M. (2019) · Cytoskeleton · doi:10.1002/cm.21583 · Cited by 51
Potentiation of GABA A Currents after Mechanical Injury of Cortical Neurons
Kao, C.-Q., Goforth, P. B., Ellis, E. F., & Satin, L. S. (2004) · Journal of Neurotrauma · doi:10.1089/089771504322972059 · Cited by 50
Peitsch, W. K., Hofmann, I., Prätzel, S., Gründ, C., Kuhn, C., Moll, I., Langbein, L., & Franke, W. W. (2001) · European Journal of Cell Biology · doi:10.1078/0171-9335-00194 · Cited by 47
Bausen, M., Fuhrmann, J. C., Betz, H., & O’Sullivan, G. A. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.11.004 · Cited by 47
Cellular transport and membrane dynamics of the glycine receptor
Dumoulin, A. (2009) · Frontiers in Molecular Neuroscience · doi:10.3389/neuro.02.028.2009 · Cited by 45
Cdk5 in Neuroskeletal Dynamics
Smith, D. S. (2003) · Neurosignals · doi:10.1159/000074626 · Cited by 45
Substrate-selective and Calcium-independent Activation of CaMKII by α-Actinin
Jalan‐Sakrikar, N., Bartlett, R. K., Baucum, A. J., & Colbran, R. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.351817 · Cited by 47
Chapter 13 Synaptic and extrasynaptic GABAA receptor and gephyrin clusters
Christie, S. B., Li, R.-W., Miralles, C. P., Riquelme, R., Yang, B. Y., Charych, E. I., Yu, W., Daniels, S. B., Cantino, M. E., & Blas, A. L. D. (2002) · Progress in brain research · doi:10.1016/s0079-6123(02)36015-1 · Cited by 43
Neurons: The Interplay between Cytoskeleton, Ion Channels/Transporters and Mitochondria
Alberti, P., Semperboni, S., Cavaletti, G., & Scuteri, A. (2022) · Cells · doi:10.3390/cells11162499 · Cited by 42
Accelerators, Brakes, and Gears of Actin Dynamics in Dendritic Spines
Pontrello, C. G., & Ethell, I. M. (2009) · The Open Neuroscience Journal · doi:10.2174/1874082000903020067 · Cited by 45
Peitsch, W. K., Hofmann, I., Endlich, N., Prätzel, S., Kuhn, C., Spring, H., Gröne, H., Kriz, W., & Franke, W. W. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000069222.63700.de · Cited by 42
Actin and Actin-Binding Proteins: Masters of Dendritic Spine Formation, Morphology, and Function
Lin, W., & Webb, D. J. (2009) · The Open Neuroscience Journal · doi:10.2174/1874082000903020054 · Cited by 42
Fredj, N. B., Grange, J., Sadoul, R., Richard, S., Goldberg, Y., & Boyer, V. (2004) · Journal of Cell Science · doi:10.1242/jcs.00927 · Cited by 40
Stress-Induced Thermoprotection of Neuromuscular Transmission
Klose, M. K. (2004) · Integrative and Comparative Biology · doi:10.1093/icb/44.1.14 · Cited by 40
Zhang, W., & Benson, D. L. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10313 · Cited by 38
Modification of AMPA receptor clustering regulates cerebellar synaptic plasticity
Hirai, H. (2001) · Neuroscience Research · doi:10.1016/s0168-0102(00)00237-6 · Cited by 40
EPHB receptor signaling in dendritic spine development
Irie, F. (2004) · Frontiers in bioscience · doi:10.2741/1325 · Cited by 40
van Zundert, B., Álvarez, F. J., Tapia, J. C., Yeh, H. H., Diaz, E., & Aguayo, L. G. (2004) · Journal of Neurophysiology · doi:10.1152/jn.00364.2003 · Cited by 38
A Pictorial History of the Neuronal Cytoskeleton
Leterrier, C. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.2872-20.2020 · Cited by 31
Photodynamic sensitizers modulate cytoskeleton structural dynamics in neuronal cells
Dubey, T., & Chinnathambi, S. (2021) · Cytoskeleton · doi:10.1002/cm.21655 · Cited by 36
Seizures Induced by in Vivo Latrunculin A and Jasplakinolide Microperfusion in the Rat Hippocampus
Sierra‐Paredes, G., Oreiro-García, T., Núñez-Rodriguez, A., Vázquez-López, A., & Sierra‐Marcuño, G. (2006) · Journal of Molecular Neuroscience · doi:10.1385/jmn:28:2:151 · Cited by 38
Cardin, V., Lezama, R. A., Torres-Márquez, M. E., & Pasantes‐Morales, H. (2003) · Glia · doi:10.1002/glia.10271 · Cited by 36
Puchkov, D., Leshchyns’ka, I., Nikonenko, A. G., Schachner, M., & Sytnyk, V. (2011) · Cerebral Cortex · doi:10.1093/cercor/bhq283 · Cited by 35
Kwak, S., Kim, J., Kim, S. C., Kwon, O., Choi, S., & Kang, T. (2008) · Brain Research · doi:10.1016/j.brainres.2008.04.026 · Cited by 35
Regulation of synapse composition by protein acetylation: the role of acetylated cortactin
Catarino, T., Ribeiro, L. F., Santos, S. D., & Carvalho, A. L. (2012) · Journal of Cell Science · doi:10.1242/jcs.110742 · Cited by 36
Viltono, L., Patrizi, A., Fritschy, J., & Sassoé‐Pognetto, M. (2008) · The Journal of Comparative Neurology · doi:10.1002/cne.21713 · Cited by 33
Compatibility between itinerant synaptic receptors and stable postsynaptic structure
Sekimoto, K., & Triller, A. (2009) · Physical Review E · doi:10.1103/physreve.79.031905 · Cited by 37
Colocalization of -actinin and Synaptopodin in the Pyramidal Cell Axon Initial Segment
Sánchez-Ponce, D., Blázquez‐Llorca, L., DeFelipe, J., Garrido, J. J., & Muñoz, A. (2011) · Cerebral Cortex · doi:10.1093/cercor/bhr251 · Cited by 34
Gephyrin Palmitoylation in Basolateral Amygdala Mediates the Anxiolytic Action of Benzodiazepine
Shen, Z., Wu, P., Wang, F., Xia, Z., Deng, Q., Nie, T., Zhang, S.-Q., Zheng, H., Liu, W., Lu, J.-J., et al. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2018.09.024 · Cited by 32
Synaptic and Nuclear Localization of Brain-Enriched Guanylate Kinase-Associated Protein
Yao, I., Iida, J., Nishimura, W., & Hata, Y. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-13-05354.2002 · Cited by 32
Regulation of postsynaptic gephyrin cluster size by protein phosphatase 1
Bausen, M., Weltzien, F., Betz, H., & O’Sullivan, G. A. (2010) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.02.007 · Cited by 30
Shiraishi, Y., Mizutani, A., Yuasa, S., Mikoshiba, K., & Furuichi, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02003.x · Cited by 30
Lambert, M., Velasco, P., Viola, K., & Klein, W. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601876 · Cited by 29
Role of Ca2+ and calmodulin‐dependent enzymes in the regulation of glycine transport in Müller glia
Gadea, A., López, E., Hernández‐Cruz, A., & López-Colomé, A. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00735.x · Cited by 27
Fujisawa, S., Shirao, T., & Aoki, C. J. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.03.009 · Cited by 27
Mitigation of synaptic and memory impairments via F-actin stabilization in Alzheimer’s disease
Haseena, P. A., Basavaraju, N., Chandran, M., Jaleel, A., Bennett, D. A., & Kommaddi, R. P. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01558-w · Cited by 26
General Introduction to Drebrin
Shirao, T., & Sekino, Y. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-4-431-56550-5_1 · Cited by 25
SIPA1L1/SPAR1 Interacts with the Neurabin Family of Proteins and is Involved in GPCR Signaling
Matsuura, K., Kobayashi, S., Konno, K., Yamasaki, M., Horiuchi, T., Senda, T., Hayashi, T., Satoh, K., Arima-Yoshida, F., Iwasaki, K., et al. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.0569-21.2022 · Cited by 25
Nonaka, M., Doi, T., Fujiyoshi, Y., Takemoto‐Kimura, S., & Bito, H. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2489-05.2006 · Cited by 25
van Zundert, B., Álvarez, F. J., Yévenes, G. E., Cárcamo, J. G., Vera, J. C., & Aguayo, L. G. (2002) · Journal of Neurophysiology · doi:10.1152/jn.00455.2001 · Cited by 25
Fast interaction between AMPA and NMDA receptors by intracellular calcium
Rozov, A. V., & Burnashev, N. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.09.005 · Cited by 24
Lahiri, D. K., & Greig, N. H. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.002 · Cited by 26
White matter disturbances in phenylketonuria: Possible underlying mechanisms
Ferreira, B. K., Rodrigues, M. T., STRECK, E. L., Ferreira, G. C., & Schuck, P. F. (2020) · Journal of Neuroscience Research · doi:10.1002/jnr.24598 · Cited by 25
Klein, W. L., Lacor, P. N., Felice, F. G. D., & Ferreira, S. T. (2007) · Research and perspectives in neurosciences · doi:10.1007/978-3-540-45702-2_11 · Cited by 23
"MEMORY BYTES" — MOLECULAR MATCH FOR CaMKII PHOSPHORYLATION ENCODING OF MICROTUBULE LATTICES
Hameroff, S. R., Craddock, T. J. A., & Tuszyński, J. A. (2010) · Journal of Integrative Neuroscience · doi:10.1142/s0219635210002482 · Cited by 23
Lee, C., Wu, D., Chen, S., Lin, Y., & Lee, T. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16816 · Cited by 21
Wu, L., Sun, C., Zhang, Y., Fan, M., Xu, J., Ma, H., & Jian, Z. (2007) · Brain Research · doi:10.1016/j.brainres.2007.06.082 · Cited by 21
Klose, M. K., Armstrong, G. A. B., & Robertson, R. M. (2004) · Journal of Neurobiology · doi:10.1002/neu.20058 · Cited by 21
Modulation of the NMDA Receptor Through Secreted Soluble Factors
Cerpa, W. F., Ramos‐Fernández, E., & Inestrosa, N. C. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-9009-x · Cited by 20
Kim, J., Kim, Y.-J., Lee, D.-S., Kim, J. Y., Ko, A.-R., Hyun, H.-W., Kim, M. J., & Kang, T. (2016) · Scientific Reports · doi:10.1038/srep26576 · Cited by 21
Olah, S. S., Kareemo, D. J., Buchta, W. C., Sinnen, B. L., Miller, C. N., Actor-Engel, H. S., Gookin, S. E., Winborn, C. S., Kleinjan, M. S., Crosby, K. C., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113331 · Cited by 19
LIS1-dependent retrograde translocation of excitatory synapses in developing interneuron dendrites
Kawabata, I., Kashiwagi, Y., Obashi, K., Ohkura, M., Nakai, J., Wynshaw-Boris, A. J., Yanagawa, Y., & Okabe, S. (2012) · Nature Communications · doi:10.1038/ncomms1736 · Cited by 19
Ahmed, R., Zha, X., Green, S. H., & Dailey, M. E. (2005) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.08.020 · Cited by 18
Vickers, C. A., & Wyllie, D. J. A. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707314 · Cited by 18
Freire‐Cobo, C., Sierra‐Paredes, G., Freire, M., & Sierra‐Marcuño, G. (2014) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-014-9558-9 · Cited by 17
Linking the synapse to the cytoskeleton: a breath-taking role for microfilaments
Jockusch, B. M., Rothkegel, M., & Schwarz, G. (2004) · Neuroreport · doi:10.1097/01.wnr.0000131673.92694.58 · Cited by 14
Vázquez-López, A., Sierra‐Paredes, G., & Sierra‐Marcuño, G. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.06.063 · Cited by 14
Network, Cellular, and Molecular Mechanisms Underlying Long-Term Memory Formation
Carasatorre, M., & Ramı́rez-Amaya, V. (2012) · Current topics in behavioral neurosciences · doi:10.1007/7854_2012_229 · Cited by 14
Lee, T., Lee, C.-C., Harn, H., Chiou, T., Chuang, M., Chen, C., Chuang, C., Lin, P., & Lin, S. (2021) · Journal of Molecular Medicine · doi:10.1007/s00109-021-02135-6 · Cited by 12
Leshchyns’ka, I., Tanaka, M. M., Schachner, M., & Sytnyk, V. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.252098 · Cited by 11
Kim, J., Lee, D.-S., Kim, T. H., Park, H., Kim, M.-J., & Kang, T. (2021) · Cell Death and Disease · doi:10.1038/s41419-020-03325-9 · Cited by 11
Klein, W. L. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_4 · Cited by 11
Subcellular localization and regulation of GABAA receptors and associated proteins
Lüscher, B., & Fritschy, J. (2001) · International review of neurobiology · doi:10.1016/s0074-7742(01)48013-5 · Cited by 10
Binding of gephyrin to microtubules is regulated by its phosphorylation at Ser270
Zhou, L., Kiss, É., Demmig, R., Kirsch, J., Nawrotzki, R., & Kuhse, J. (2021) · Histochemistry and Cell Biology · doi:10.1007/s00418-021-01973-2 · Cited by 10
Takahashi, H., & Naito, Y. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-4-431-56550-5_10 · Cited by 10
Changes in cytoskeletal gene expression linked to MPTP-treatment in Mice
Cuadrado‐Tejedor, M., Sesma, M. T., Giménez‐Amaya, J. M., & Ortíz, L. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.05.014 · Cited by 9
Sbai, O., Soussi, R., Bôle, A., Khrestchatisky, M., Esclapez, M., & Ferhat, L. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113512 · Cited by 8
Septin 6 localizes to microtubules in neuronal dendrites
Moon, I. S., Lee, H., & Walikonis, R. S. (2012) · Cytotechnology · doi:10.1007/s10616-012-9477-7 · Cited by 8
Actin Cytoskeleton at the Synapse: An Alzheimer's Disease Perspective
Haseena, P. A., Basavaraju, N., Gupta, A., & Kommaddi, R. P. (2025) · Cytoskeleton · doi:10.1002/cm.21993 · Cited by 9
Melišková, V., Havránek, T., Bačová, Z., & Bakoš, J. (2021) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2004106 · Cited by 7
Huang, C., Wang, Y., Chen, P., Shan, Q., Wang, H., Ding, L., Bi, G., & Zhou, J. (2022) · Communications Biology · doi:10.1038/s42003-022-03260-9 · Cited by 7
Tsai, Y.-C., Huang, S., Peng, H., Lin, S., Lin, S., Chin, T., & Huang, S. (2023) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2023.12.006 · Cited by 7
Drebrin expression is increased in spinal motoneurons of rats after axotomy
Kobayashi, S., Shirao, T., & Sasaki, T. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02155-3 · Cited by 7
Network features and pathway analyses of a signal transduction cascade
Yamashima, R. (2009) · Frontiers in Neuroinformatics · doi:10.3389/neuro.11.013.2009 · Cited by 7
Why Alzheimer’s is a Disease of Memory: Synaptic Targeting by Pathogenic Aβ Oligomers (ADDLs)
Klein, W. L., Felice, F. G. D., Lacor, P. N., Lambert, M. P., & Zhao, W.-Q. (2008) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-540-76330-7_9 · Cited by 7
Surakul, P., Weerachatyanukul, W., & Chutabhakdikul, N. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.02.060 · Cited by 7
PTBP-dependent PSD-95 and CamKIIα alternative splicing in the lens.
Frederikse, P. H., Nandanoor, A., & Kasinathan, C. (2014) · Europe PMC (PubMed Central) · Cited by 6
Berry, C. B., & McBean, G. J. (2003) · Brain Research · doi:10.1016/s0006-8993(03)02565-4 · Cited by 6
Petralia, R. S., & Wenthold, R. J. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-055-3_2 · Cited by 7
Pivovarov, A. S., Murzina, G. B., Makhnovsky, D. A., Tret’yakova, M. S., & Vasil’yeva, N. A. (2013) · Invertebrate Neuroscience · doi:10.1007/s10158-013-0155-z · Cited by 4
Subunit-Specific NMDA Receptor Trafficking to Synapses
Barría, A. (2007) · Elsevier eBooks · doi:10.1016/b978-012369437-9/50015-3 · Cited by 4
Pivovarov, A. S., Васильева, Н. А., Murzina, G. B., & Makhnovsky, D. A. (2013) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-013-9771-7 · Cited by 3
Jing, D., Li, D., Cheng, P., Chen, Y., & Behnisch, T. (2019) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2019.107038 · Cited by 3
Hade, I., & Zenia, T. A. (2011) · Diyala Journal for Pure Science · Cited by 3
Luccardini, C., Casagrande, S., Cupello, A., Pellistri, F., Ramoino, P., & Robello, M. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.01.067 · Cited by 3
Luk, C., Schmold, N., Lee, T. K. M., & Syed, N. I. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07428.x · Cited by 3
The Role of the Postsynaptic Density and the Spine Cytoskeleton in Synaptic Plasticity
Marcora, E. M., Carlisle, H. J., & Kennedy, M. B. (2008) · Elsevier eBooks · doi:10.1016/b978-012370509-9.00036-x · Cited by 4
Antibodies in Stiff-Person Spectrum Disorders and Their Correlations with Clinical Phenotypes
Termsarasab, P., Thammongkolchai, T., & Katirji, B. (2020) · Springer eBooks · doi:10.1007/978-3-030-43059-7_8 · Cited by 2
Disrupting Protein-Protein Interaction: Therapeutic Tools Against Brain Damage
Aarts, M. M., & Tymianski, M. (2005) · Springer eBooks · doi:10.1007/0-387-24532-4_12 · Cited by 2
(2015) · Molecular & Cellular Epilepsy · doi:10.14800/mce.608 · Cited by 2
Peptide action in stroke therapy
Aarts, M. M., & Tymianski, M. (2003) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.3.7.1093 · Cited by 2
Influence of receptor lateral diffusion on depression of neuronal cholinosensitivity
Murzina, G. B. (2013) · BIOPHYSICS · doi:10.1134/s000635091303010x · Cited by 2
Metadata
- Authors
- Allison, D. W., Chervin, A. S., Gelfand, V. I., & Craig, A. M.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2000-06-15
- Volume
- 20
- Issue
- 12
- Pages
- 4545-4554
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6772458
- OpenAlex
- W2148256023
- Cited by
- 245
- References
- 79
- Citations by year
- 2025: 5 · 2024: 3 · 2023: 2 · 2022: 4 · 2021: 10 · 2020: 4 · 2019: 3 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 5 · 2014: 12 · 2013: 8 · 2012: 7
- FWCI
- 8.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- National Institutes of Health (GM-52111)
- National Institute of General Medical Sciences (R01GM052111, GM52111-01)
- National Institute of Neurological Disorders and Stroke (NS33184, R01NS033184)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Keywords
- postsynaptic scaffolds, postsynaptic density, actin cytoskeleton, microtubules, PSD-95, GKAP, CaMKIIα, drebrin, ACTN2, GABAA receptor, gephyrin, glutamatergic synapses, inhibitory synapses, hippocampal pyramidal neurons, latrunculin A, vincristine, detergent extraction, dendritic spines
- MeSH terms
- Disks Large Homolog 4 Protein, Actins, Animals, Cells, Cultured, Evoked Potentials, Hippocampus, Marine Toxins, Membrane Proteins, Microtubules, Nerve Tissue Proteins, Neurons, Synapses, Thiazoles, Vincristine, Octoxynol, Bridged Bicyclo Compounds, Heterocyclic, Excitatory Postsynaptic Potentials, Intracellular Signaling Peptides and Proteins, Rats, Thiazolidines
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review