The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
C‐terminal synaptic targeting elements for postsynaptic density proteins ProSAP1/Shank2 and ProSAP2/Shank3
Open accessAbstract
Synapses are specialized contact sites mediating communication between neurons. Synaptogenesis requires the specific assembly of protein clusters at both sides of the synaptic contact by mechanisms that are barely understood. We studied the synaptic targeting of multi‐domain proteins of the ProSAP/Shank family thought to serve as master scaffolding molecules of the postsynaptic density. In contrast to Shank1, expression of green‐fluorescent protein (GFP)‐tagged ProSAP1/Shank2 and ProSAP2/Shank3 deletion constructs in hippocampal neurons revealed that their postsynaptic localization relies on the integrity of the C‐termini. The shortest construct that was perfectly targeted to synaptic sites included the last 417 amino acids of ProSAP1/Shank2 and included the C‐terminal sterile alpha motif (SAM) domain. Removal of 54 residues from the N‐terminus of this construct resulted in a diffuse distribution in the cytoplasm. Altogether, our data delineate a hitherto unknown targeting signal in both ProSAP1/Shank2 and ProSAP2/Shank3 and provide evidence for an implication of these proteins and their close homologue, Shank1, in distinct molecular pathways.
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?
In the citing paper
“These results are consistent with previous data showing that the Homer-binding site is involved in the synaptic localization of Shank3.22, 31”
From SHANK3 mutations identified in autism lead to modification of dendritic spine morphology via an actin-dependent mechanism (2012) · cites this paper as [31]
In the citing paper
“Shank3WT overexpression led to an accumulation of the protein in dendritic spines (Figure 2a), as previously reported.31”
From SHANK3 mutations identified in autism lead to modification of dendritic spine morphology via an actin-dependent mechanism (2012) · cites this paper as [31]
In the citing paper
“Shank3 forms multimers via its C terminal SAM domain (Boeckers et al., 2005; Hayashi et al., 2009; Naisbitt et al., 1999) as well as its PDZ domain (Iskenderian-Epps and Imperiali, 2010).”
From Modeling Autism by SHANK Gene Mutations in Mice (2013) · cites this paper as Boeckers et al., 2005
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
PDZ Domains and the Organization of Supramolecular Complexes
Sheng, M., & Sala, C. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1 · Cited by 1,211
Coupling of mGluR/Homer and PSD-95 Complexes by the Shank Family of Postsynaptic Density Proteins
Tu, J. C., Xiao, B., Naisbitt, S. R., Yuan, J. P., Petralia, R. S., Brakeman, P., Doan, A., Aakalu, V. K., Lanahan, A. A., Sheng, M., et al. (1999) · Neuron · doi:10.1016/s0896-6273(00)80810-7 · Cited by 1,079
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
Regulation of Dendritic Spine Morphology and Synaptic Function by Shank and Homer
Sala, C., Piëch, V., Wilson, N. R., Passafaro, M., Liu, G., & Sheng, M. (2001) · Neuron · doi:10.1016/s0896-6273(01)00339-7 · Cited by 716
The Shank family of scaffold proteins
Sheng, M., & Kim, E. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.11.1851 · Cited by 578
Dieck, S., Sanmartí-Vila, L., Langnaese, K., Richter, K., Kindler, S., Soyke, A., Wex, H., Smalla, K.-H., Kämpf, U., Fränzer, J.-T., et al. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.2.499 · Cited by 482
Self-citationThe postsynaptic density at glutamatergic synapses
Kennedy, M. B. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)01033-8 · Cited by 475
Enlightening the Postsynaptic Density
Ziff, E. B. (1997) · Neuron · doi:10.1016/s0896-6273(00)80409-2 · Cited by 384
Boeckers, T. M., Bockmann, J., Kreutz, M. R., & Gundelfinger, E. D. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00931.x · Cited by 349
Self-citationCharacterization of the Shank Family of Synaptic Proteins
Lim, S., Naisbitt, S., Yoon, J., Hwang, J.-I., Suh, P.-G., Sheng, M., & Kim, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.29510 · Cited by 295
Research works printed but not linked: 1
- Goslin K., 1991, Culturing Nerve Cells, 251
Cited by
Sorted by citations
SHANK proteins: roles at the synapse and in autism spectrum disorder
Monteiro, P., & Feng, G. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.183 · Cited by 681
Mutations in the SHANK2 synaptic scaffolding gene in autism spectrum disorder and mental retardation
Berkel, S., Marshall, C. R., Weiss, B., Howe, J., Roeth, R., Moog, U., Endris, V., Roberts, W., Szatmari, P., Pinto, D., et al. (2010) · Nature Genetics · doi:10.1038/ng.589 · Cited by 563
Modeling Autism by SHANK Gene Mutations in Mice
Jiang, Y.-H., & Ehlers, M. D. (2013) · Neuron · doi:10.1016/j.neuron.2013.03.016 · Cited by 488
Leblond, C. S., Heinrich, J., Delorme, R., Proepper, C., Betancur, C., Huguet, G., Konyukh, M., Chaste, P., Ey, E., Rastam, M., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002521 · Cited by 429
Self-citationThe postsynaptic density proteins Homer and Shank form a polymeric network structure
Hayashi, M. K., Tang, C., Verpelli, C., Narayanan, R., Stearns, M. H., Xu, R.-M., Li, H., Sala, C., & Hayashi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.01.050 · Cited by 356
Durand, C. M., Perroy, J., Loll, F., Perrais, D., Fagni, L., Bourgeron, T., Montcouquiol, M., & Sans, N. (2012) · Molecular Psychiatry · doi:10.1038/mp.2011.57 · Cited by 316
An Architectural Framework That May Lie at the Core of the Postsynaptic Density
Baron, M. K., Boeckers, T. M., Vaida, B., Faham, S., Gingery, M., Sawaya, M. R., Salyer, D., Gundelfinger, E. D., & Bowie, J. U. (2006) · Science · doi:10.1126/science.1118995 · Cited by 292
Self-citationBoeckers, T. M. (2006) · Cell and Tissue Research · doi:10.1007/s00441-006-0274-5 · Cited by 263
Self-citationPrevalence of SHANK3 variants in patients with different subtypes of autism spectrum disorders
Boccuto, L., Lauri, M., Sarasua, S. M., Skinner, C. D., Buccella, D., Dwivedi, A., Orteschi, D., Collins, J. S., Zollino, M., Visconti, P., et al. (2013) · European Journal of Human Genetics · doi:10.1038/ejhg.2012.175 · Cited by 240
Postsynaptic ProSAP/Shank scaffolds in the cross-hair of synaptopathies
Grabrucker, A. M., Schmeisser, M. J., Schoen, M., & Boeckers, T. M. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.07.003 · Cited by 233
Self-citationConcerted action of zinc and ProSAP/Shank in synaptogenesis and synapse maturation
Grabrucker, A. M., Knight, M. J., Proepper, C., Bockmann, J., Joubert, M., Rowan, M., Nienhaus, G. U., Garner, C. C., Bowie, J. U., Kreutz, M. R., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.336 · Cited by 228
Self-citationVerpelli, C., Dvoretskova, E., Vicidomini, C., Rossi, F., Chiappalone, M., Schoen, M., Di Stefano, B., Mantegazza, R., Broccoli, V., Böckers, T. M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.258384 · Cited by 197
Sala, C., Vicidomini, C., Bigi, I., Mossa, A., & Verpelli, C. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13232 · Cited by 182
Berkel, S., Tang, W., Treviño, M., Vogt, M., Obenhaus, H. A., Gass, P., Scherer, S. W., Sprengel, R., Schratt, G., & Rappold, G. A. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr470 · Cited by 162
Jaramillo, T. C., Speed, H. E., Xuan, Z., Reimers, J. M., Liu, S., & Powell, C. M. (2015) · Autism Research · doi:10.1002/aur.1529 · Cited by 160
Cerebellar associative sensory learning defects in five mouse autism models
Kloth, A. D., Badura, A., Li, A., Cherskov, A., Connolly, S. G., Giovannucci, A., Bangash, M. A., Grasselli, G., Peñagarikano, O., Piochon, C., et al. (2015) · eLife · doi:10.7554/elife.06085 · Cited by 148
Speed, H. E., Kouser, M., Xuan, Z., Reimers, J. M., Ochoa, C. F., Gupta, N. M., Liu, S., & Powell, C. M. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.3125-14.2015 · Cited by 148
Abelson interacting protein 1 (Abi‐1) is essential for dendrite morphogenesis and synapse formation
Proepper, C., Johannsen, S., Liebau, S., Dahl, J., Vaida, B., Bockmann, J., Kreutz, M. R., Gundelfinger, E. D., & Boeckers, T. M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601569 · Cited by 124
Self-citationPhelan–McDermid Syndrome and SHANK3: Implications for Treatment
Costales, J. L., & Kolevzon, A. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0352-z · Cited by 130
Scaffolding proteins at the postsynaptic density: shank as the architectural framework
Kreienkamp, H. J. (2008) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-72843-6_15 · Cited by 105
A role for synaptic zinc in ProSAP/Shank PSD scaffold malformation in autism spectrum disorders
Grabrucker, A. M. (2013) · Developmental Neurobiology · doi:10.1002/dneu.22089 · Cited by 105
A role for zinc in postsynaptic density asSAMbly and plasticity?
Gundelfinger, E. D., Boeckers, T. M., Baron, M. K., & Bowie, J. U. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.05.007 · Cited by 98
Self-citationTemporal-spatial expression and novel biochemical properties of the memory-related protein KIBRA
Johannsen, S., Duning, K., Pavenstädt, H., Kremerskothen, J., & Boeckers, T. M. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.06.054 · Cited by 91
Self-citationIdentification and functional characterization of rare SHANK2 variants in schizophrenia
Peykov, S. Z., Berkel, S., Schoen, M., Weiss, K., Degenhardt, F., Strohmaier, J., Weiss, B., Proepper, C., Schratt, G. M., Nöthen, M. M., et al. (2015) · Molecular Psychiatry · doi:10.1038/mp.2014.172 · Cited by 100
Self-citationScaffold Proteins at the Postsynaptic Density
Verpelli, C., Schmeisser, M. J., Sala, C., & Boeckers, T. M. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-7091-0932-8_2 · Cited by 92
Self-citationDelling, J. P., & Boeckers, T. M. (2021) · Journal of Neurodevelopmental Disorders · doi:10.1186/s11689-021-09397-8 · Cited by 104
Self-citationMosca, S. J., Langevin, L. M., Dewey, D., Innes, A. M., Lionel, A. C., Marshall, C. R., Scherer, S. W., Parboosingh, J. S., & Bernier, F. P. (2016) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2016-103818 · Cited by 90
Cochoy, D. M., Kolevzon, A. L., Kajiwara, Y., Schoen, M., Pascual‐Lucas, M., Lurie, S., Buxbaum, J. D., Boeckers, T. M., & Schmeißer, M. J. (2015) · Molecular Autism · doi:10.1186/s13229-015-0020-5 · Cited by 89
Self-citationSchoen, M., Reichel, J. M., Demestre, M., Putz, S., Deshpande, D., Proepper, C., Liebau, S., Schmeißer, M. J., Ludolph, A. C., Michaelis, J., et al. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00496 · Cited by 80
Self-citationHolder, J. L., & Quach, M. M. (2016) · Epilepsia · doi:10.1111/epi.13506 · Cited by 78
Fourie, C., Vyas, Y., Lee, K., Jung, Y., Garner, C. C., & Montgomery, J. M. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00374 · Cited by 78
Shank and Zinc Mediate an AMPA Receptor Subunit Switch in Developing Neurons
Ha, H., Leal‐Ortiz, S., Lalwani, K., Kiyonaka, S., Hamachi, I., Mysore, S. P., Montgomery, J. M., Garner, C. C., Huguenard, J. R., & Kim, S. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00405 · Cited by 69
Luo, P., Fei, F., Zhang, L., Qu, Y., & Fei, Z. (2011) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.05.004 · Cited by 69
Shank3 Is Part of a Zinc-Sensitive Signaling System That Regulates Excitatory Synaptic Strength
Arons, M. H., Lee, K. C., Thynne, C. J., Kim, S. A., Schob, C., Kindler, S., Montgomery, J. M., & Garner, C. C. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0116-16.2016 · Cited by 71
Grabrucker, S., Proepper, C., Mangus, K., Eckert, M., Chhabra, R., Schmeißer, M. J., Boeckers, T. M., & Grabrucker, A. M. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2013.12.015 · Cited by 66
Self-citationBacolla, A., Collins, J., Gold, B., Chuzhanova, N. A., Yi, M., Stephens, R. M., Stefanov, S. A., Olsh, A., Jakupciak, J. P., Dean, M. C., et al. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl354 · Cited by 62
Activity induced changes in the distribution of Shanks at hippocampal synapses
Tao-Cheng, J. H., Dosemeci, A., Gallant, P. E., Smith, C., & Reese, T. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.03.041 · Cited by 61
Eltokhi, A., Rappold, G., & Sprengel, R. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00240 · Cited by 63
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
Wendholt, D., Spilker, C., Schmitt, A., Dolnik, A., Smalla, K., Proepper, C., Bockmann, J., Sobue, K., Gundelfinger, E. D., Kreutz, M. R., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601101200 · Cited by 61
Self-citationNeuronal L-Type Calcium Channel Signaling to the Nucleus Requires a Novel CaMKIIα-Shank3 Interaction
Perfitt, T. L., Wang, X., Dickerson, M. T., Stephenson, J. R., Nakagawa, T., Jacobson, D. A., & Colbran, R. J. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.0893-19.2020 · Cited by 54
Mameza, M. G., Dvoretskova, E., Bamann, M., Hönck, H., Güler, T., Boeckers, T. M., Schoen, M., Verpelli, C., Sala, C., Barsukov, I., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.424747 · Cited by 54
Self-citationAn SK3 Channel/nWASP/Abi-1 Complex Is Involved in Early Neurogenesis
Liebau, S., Steinestel, J., Linta, L., Kleger, A., Storch, A., Schoen, M., Steinestel, K., Proepper, C., Bockmann, J., Schmeißer, M. J., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018148 · Cited by 50
Self-citationShank Proteins Differentially Regulate Synaptic Transmission
Shi, R., Redman, P. T., Ghose, D., Hwang, H., Liu, Y., Ren, X., Ding, L. J., Liu, M., Jones, K. J., & Xu, W. (2017) · eNeuro · doi:10.1523/eneuro.0163-15.2017 · Cited by 50
Differential Distribution of Shank and GKAP at the Postsynaptic Density
Tao-Cheng, J.-H., Yang, Y., Reese, T. S., & Döṣemeci, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118750 · Cited by 46
Hagmeyer, S., Sauer, A. K., & Grabrucker, A. M. (2018) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2018.00011 · Cited by 43
Altered synaptic ultrastructure in the prefrontal cortex of Shank3-deficient rats
Jacot-Descombes, S., Keshav, N. U., Dickstein, D. L., Wicinski, B., Janssen, W. G. M., Hiester, L. L., Sarfo, E. K., Warda, T., Fam, M. M., Harony-Nicolas, H., et al. (2020) · Molecular Autism · doi:10.1186/s13229-020-00393-8 · Cited by 41
Selective Localization of Shanks to VGLUT1-Positive Excitatory Synapses in the Mouse Hippocampus
Heise, C., Schroeder, J. C., Schoen, M., Halbedl, S., Reim, D., Woelfle, S., Kreutz, M. R., Schmeißer, M. J., & Boeckers, T. M. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00106 · Cited by 42
Self-citationXu, N., Lv, H., Yang, T., Du, X., Sun, Y., Xiao, B., Fan, Y., Luo, X., Zhan, Y., Wang, L., et al. (2020) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-020-01592-5 · Cited by 42
Shankopathies in the Developing Brain in Autism Spectrum Disorders
Vyas, Y., Cheyne, J. E., Lee, K., Jung, Y., Cheung, P. Y., & Montgomery, J. M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.775431 · Cited by 46
SHANK genes in autism: Defining therapeutic targets
Mossa, A., Giona, F., Pagano, J., Sala, C., & Verpelli, C. (2017) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.11.019 · Cited by 40
The Role of Zinc and NMDA Receptors in Autism Spectrum Disorders
Lee, K. C., Mills, Z., Cheung, P. Y., Cheyne, J. E., & Montgomery, J. M. (2022) · Pharmaceuticals · doi:10.3390/ph16010001 · Cited by 42
Eltokhi, A., Gonzalez-Lozano, M. A., Oettl, L.-L., Rozov, A., Pitzer, C., Röth, R., Berkel, S., Hüser, M., Harten, A., Kelsch, W., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01140-y · Cited by 38
Lutz, A.-K., Arévalo, A. P., Ioannidis, V., Stirmlinger, N., Demestre, M., Delorme, R., Bourgeron, T., & Boeckers, T. M. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.773571 · Cited by 38
Self-citationProepper, C., Steinestel, K., Schmeißer, M. J., Heinrich, J., Steinestel, J., Bockmann, J., Liebau, S., & Boeckers, T. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027045 · Cited by 38
Self-citationSPAR2, a novel SPAR‐related protein with GAP activity for Rap1 and Rap2
Spilker, C., Sanhueza, G. A., Böckers, T. M., Kreutz, M. R., & Gundelfinger, E. D. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04991.x · Cited by 37
Self-citationMaturation of Synaptic Contacts in Differentiating Neural Stem Cells
Liebau, S., Vaida, B., Storch, A., & Boeckers, T. M. (2007) · Stem Cells · doi:10.1634/stemcells.2006-0823 · Cited by 34
Self-citationDosage-sensitive genes in autism spectrum disorders: From neurobiology to therapy
Javed, S., Selliah, T., Lee, Y., & Huang, W. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.08.009 · Cited by 32
Bucher, M., Niebling, S., Han, Y., Molodenskiy, D., Hassani Nia, F., Kreienkamp, H.-J., Svergun, D., Kim, E., Kostyukova, A. S., Kreutz, M. R., et al. (2021) · eLife · doi:10.7554/elife.66165 · Cited by 33
Self-citationAssociation study of SHANK3 gene polymorphisms with autism in Chinese Han population
Qin, J., Jia, M., Wang, L., Lu, T., Ruan, Y., Liu, J., Guo, Y., Zhang, J., Yang, X., Yue, W., et al. (2009) · BMC Medical Genetics · doi:10.1186/1471-2350-10-61 · Cited by 32
Ultrastructural analyses in the hippocampus CA1 field in Shank3-deficient mice
Uppal, N., Puri, R., Yuk, F., Janssen, W. G. M., Bozdagi-Gunal, O., Harony‐Nicolas, H., Dickstein, D. L., Buxbaum, J. D., & Hof, P. R. (2015) · Molecular Autism · doi:10.1186/s13229-015-0036-x · Cited by 33
Prenatal Zinc Deficient Mice as a Model for Autism Spectrum Disorders
Sauer, A. K., Hagmeyer, S., & Grabrucker, A. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116082 · Cited by 35
Molecular architecture of postsynaptic Interactomes
Wilkinson, B., & Coba, M. P. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109782 · Cited by 25
Neurodevelopmental Consequences of Dietary Zinc Deficiency: A Status Report
Ross, M. M., Hernández-Espinosa, D. R., & Aizenman, E. (2023) · Biological Trace Element Research · doi:10.1007/s12011-023-03630-2 · Cited by 31
A bidirectional switch in the Shank3 phosphorylation state biases synapses toward up- or downscaling
Wu, C.-H., Tatavarty, V., Beltran, P. M., Guerrero, A., Keshishian, H., Krug, K., MacMullan, M. A., Li, L., Carr, S. A., Cottrell, J. R., et al. (2022) · eLife · doi:10.7554/elife.74277 · Cited by 29
Dolnik, A., Kanwal, N., Mackert, S., Halbedl, S., Proepper, C., Bockmann, J., Schoen, M., Boeckers, T. M., Kühl, S. J., & Schmeißer, M. J. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13353 · Cited by 29
Self-citationGrabrucker, S., Pagano, J., Schweizer, J., Urrutia‐Ruiz, C., Schön, M., Thome, K., Ehret, G., Grabrucker, A. M., Zhang, R., Hengerer, B., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2019104267 · Cited by 28
Self-citationRaab, M., Boeckers, T. M., & Neuhuber, W. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.08.041 · Cited by 27
Self-citationA Presynaptic Function of Shank Protein inDrosophila
Wu, S. H., Gan, G., Zhang, Z., Sun, J. Y., Wang, Q., Gao, Z., Li, M., Jin, S., Huang, J., Thomas, U., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.0893-17.2017 · Cited by 27
Activity and circadian rhythm influence synaptic Shank3 protein levels in mice
Sarowar, T., Chhabra, R., Vilella, A., Boeckers, T. M., Zoli, M., & Grabrucker, A. M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13709 · Cited by 29
Self-citationNia, F. H., Woike, D., Kloth, K., Kortüm, F., & Kreienkamp, H. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15014 · Cited by 26
Structural basis for PDZ domain interactions in the post‐synaptic density scaffolding protein Shank3
Ponna, S. K., Ruskamo, S., Myllykoski, M., Keller, C., Boeckers, T. M., & Kursula, P. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14322 · Cited by 25
Self-citationLee, K., Jung, Y., Vyas, Y., Skelton, I., Abraham, W. C., Hsueh, Y., & Montgomery, J. M. (2022) · Molecular Autism · doi:10.1186/s13229-022-00494-6 · Cited by 24
Identification of two novel Shank3 transcripts in the developing mouse neocortex
Waga, C., Asano, H., Sanagi, T., Suzuki, E., Nakamura, Y., Tsuchiya, A., Itoh, M., Goto, Y., Kohsaka, S., & Uchino, S. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12505 · Cited by 25
Sasaki, K., Kojitani, N., Hirose, H., Yoshihama, Y., Suzuki, H., Shimada, M., Takayanagi, A., Yamashita, A., Nakaya, M., Hirano, H., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.088 · Cited by 23
Shank2 identifies a subset of glycinergic neurons involved in altered nociception in an autism model
Heuvel, F. O., Alami, N. O., Aousji, O., Pogatzki-Zahn, E. M., Zahn, P. K., Wilhelm, H., Deshpande, D., Khatamsaz, E., Catanese, A., Woelfle, S., et al. (2023) · Molecular Autism · doi:10.1186/s13229-023-00552-7 · Cited by 24
Self-citationSam Domains in Multiple Diseases
Vincenzi, M., Mercurio, F. A., & Leone, M. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666181009114445 · Cited by 23
POSH regulates assembly of the NMDAR/PSD-95/Shank complex and synaptic function
Yao, M., Meng, M., Yang, X., Wang, S., Zhang, H., Zhang, F., Shi, L., Zhang, Y., Zhang, X., & Xu, Z. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110642 · Cited by 21
Defective Synapse Maturation and Enhanced Synaptic Plasticity in Shank2 Δex7 –/– Mice
Wegener, S., Buschler, A., Stempel, A. V., Kang, S. J., Lim, C., Kaang, B., Shoichet, S. A., Manahan‐Vaughan, D., & Schmitz, D. (2018) · eNeuro · doi:10.1523/eneuro.0398-17.2018 · Cited by 25
ProSAPiP2, a novel postsynaptic density protein that interacts with ProSAP2/Shank3
Liebau, S., Proepper, C., Schmidt, T., Schoen, M., Bockmann, J., & Boeckers, T. M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.05.098 · Cited by 20
Self-citationKawasawa, Y. I., Mohammad, S., Son, A. I., Morizono, H., Basha, A., Salzberg, A. C., Torii, M., & Hashimoto‐Torii, K. (2017) · Alcohol · doi:10.1016/j.alcohol.2017.05.001 · Cited by 20
SHANK family on stem cell fate and development
Liu, X., Yuan, M., Lau, B. W.-M., & Li, Y. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05325-3 · Cited by 21
SHANK1 and autism spectrum disorders
Gong, X., & Wang, H. (2015) · Science China Life Sciences · doi:10.1007/s11427-015-4892-6 · Cited by 22
Wan, L., Liu, D., Xiao, W., Zhang, B., Yan, X., Luo, Z., & Xiao, B. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-021-01054-x · Cited by 20
Nia, F. H., Woike, D., Bento, I., Niebling, S., Tibbe, D., Schulz, K., Hirnet, D., Skiba, M., Hönck, H., Veith, K., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01882-3 · Cited by 18
Lutz, A.-K., Bauer, H. F., Ioannidis, V., Schön, M., & Boeckers, T. M. (2022) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2022.890231 · Cited by 15
Self-citationSchaz, U., Föhr, K. J., Liebau, S., Fulda, S., Kölch, M. G., Fegert, J. M., Boeckers, T. M., & Ludolph, A. G. (2010) · The World Journal of Biological Psychiatry · doi:10.3109/15622975.2010.506927 · Cited by 16
Self-citationJin, C., Kang, H., Yoo, T., Ryu, J. R., Yoo, Y.-E., Ma, R., Zhang, Y., Kang, H. R., Kim, Y., Seong, H., et al. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.614435 · Cited by 14
The Kohlschütter-Tönz syndrome associated gene Rogdi encodes a novel presynaptic protein
Riemann, D., Wallrafen, R., & Dresbach, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-16004-1 · Cited by 14
Self-citationA blueprint for research on Shankopathies: A view from research on autism spectrum disorder
Carbonetto, S. (2013) · Developmental Neurobiology · doi:10.1002/dneu.22150 · Cited by 13
Ray, S., & Hewitt, K. J. (2023) · BioEssays · doi:10.1002/bies.202300022 · Cited by 11
Grabrucker, A. M., Vaida, B., Bockmann, J., & Boeckers, T. M. (2009) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2009.05.008 · Cited by 11
Self-citationnArgBP2-SAPAP-SHANK, the core postsynaptic triad associated with psychiatric disorders
Lee, S., Kim, J. A., & Chang, S. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-017-0018-5 · Cited by 13
Zhu, W., Li, J., Chen, S., Zhang, J., Vetrini, F., Braxton, A. A., Eng, C. M., Yang, Y., Xia, F., Keller, K. L., et al. (2018) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.38622 · Cited by 10
SHANK Mutations in Intellectual Disability and Autism Spectrum Disorder
Schmeißer, M. J., & Verpelli, C. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-800109-7.00010-8 · Cited by 7
GluA1-Shank3 interaction decreases in response to chronic neuronal depolarization
Ross, M. M., & Aizenman, E. (2023) · Neuroscience Letters · doi:10.1016/j.neulet.2023.137305 · Cited by 6
Abnormal Function of Metalloproteins Underlies Most Neurodegenerative Diseases
Kanninen, K. M., & White, A. R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804562-6.00021-x · Cited by 6
Woike, D., Tibbe, D., Nia, F. H., Martens, V., Wang, E. Q., Barsukov, I., & Kreienkamp, H. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03611-5 · Cited by 8
Kalarani, I. B., Vajagathali, M., & Veerabathiran, R. (2022) · Advances in Neurodevelopmental Disorders · doi:10.1007/s41252-022-00251-z · Cited by 3
POSH undergoes phase separation and co-condensation with SHANK2/3 to regulate spine development
Yao, M., Yuan, L., Zheng, Y., & Xu, Z. (2025) · Protein & Cell · doi:10.1093/procel/pwaf066 · Cited by 2
Metadata
- Authors
- Boeckers, T. M., Liedtke, T., Spilker, C., Dresbach, T., Bockmann, J., Kreutz, M. R., & Gundelfinger, E. D.
- Affiliations
- Universität Ulm (DE)
- University of Münster (DE)
- Leibniz Institute for Neurobiology (DE)
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2004-12-23
- Volume
- 92
- Issue
- 3
- Pages
- 519-524
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2099448375
- Cited by
- 113
- References
- 20
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 7 · 2022: 9 · 2021: 9 · 2020: 9 · 2019: 1 · 2018: 9 · 2017: 8 · 2016: 8 · 2015: 12 · 2014: 1 · 2013: 5 · 2012: 4
- FWCI
- 1.05
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Centre National de la Recherche Scientifique
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- Shank1, postsynaptic density, synaptic targeting, sterile alpha motif domain, synaptic scaffolding proteins, synaptogenesis, hippocampal neurons, protein localization
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cells, Cultured, Molecular Sequence Data, Nerve Tissue Proteins, Recombinant Fusion Proteins, Synapses, Transfection, Sequence Deletion, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Rats
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
