The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Homer Binds a Novel Proline-Rich Motif and Links Group 1 Metabotropic Glutamate Receptors with IP3 Receptors
Open accessAbstract
Group I metabotropic glutamate receptors (mGluRs) activate PI turnover and thereby trigger intracellular calcium release. Previously, we demonstrated that mGluRs form natural complexes with members of a family of Homer-related synaptic proteins. Here, we present evidence that Homer proteins form a physical tether linking mGluRs with the inositol trisphosphate receptors (IP3R). A novel proline-rich "Homer ligand" (PPXXFr) is identified in group 1 mGluRs and IP3R, and these receptors coimmunoprecipitate as a complex with Homer from brain. Expression of the IEG form of Homer, which lacks the ability to cross-link, modulates mGluR-induced intracellular calcium release. These studies identify a novel mechanism in calcium signaling and provide evidence that an IEG, whose expression is driven by synaptic activity, can directly modify a specific synaptic function.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“For example, a gene that encodes a synaptic scaffolding protein, HOMER132, was engaged in NeuN+ specific peaks and loops and its expression was significantly higher in NeuN+ cells compared with NeuN− cells (Fig. 2b).”
From Neuronal and glial 3D chromatin architecture informs the cellular etiology of brain disorders (2021) · cites this paper as [32]
Citations
Cites
PHARMACOLOGY AND FUNCTIONS OF METABOTROPIC GLUTAMATE RECEPTORS
Conn, P. J., & Pin, J. (1997) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.37.1.205 · Cited by 3,083
Sequence and expression of a metabotropic glutamate receptor
Masu, M., Tanabe, Y., Tsuchida, K., Shigemoto, R., & Nakanishi, S. (1991) · Nature · doi:10.1038/349760a0 · Cited by 1,216
Homer: a protein that selectively binds metabotropic glutamate receptors
Brakeman, P., Lanahan, A. A., O’Brien, R., Roche, K. W., Barnes, C. A., Huganir, R. L., & Worley, P. F. (1997) · Nature · doi:10.1038/386284a0 · Cited by 1,115
Self-citationStructural basis for the binding of proline-rich peptides to SH3 domains
Yu, H., Chen, J., Feng, S., Dalgarno, D. C., Brauer, A. W., & Schrelber, S. L. (1994) · Cell · doi:10.1016/0092-8674(94)90367-0 · Cited by 1,003
A family of metabotropic glutamate receptors
Tanabe, Y., Masu, M., Ishii, T., Shigemoto, R., & Nakanishi, S. (1992) · Neuron · doi:10.1016/0896-6273(92)90118-w · Cited by 940
The role of excitatory amino acids in behavioral sensitization to psychomotor stimulants
Wolf, M. E. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(97)00090-7 · Cited by 934
Baude, A., Nusser, Z., Roberts, J. D. B., Mulvihill, E., Jeffrey Mcllhinney, R. A., & Somogyi, P. (1993) · Neuron · doi:10.1016/0896-6273(93)90086-7 · Cited by 927
A family of metabotropic glutamate receptors
Tanabe, Y. (1992) · Medical Entomology and Zoology · doi:10.11501/3061113 · Cited by 879
Symons, M. H., Derry, J. M. J., Karlak, B., Jiang, S., Lemahieu, V., McCormick, F. P., Francke, U., & Abo, A. (1996) · Cell · doi:10.1016/s0092-8674(00)81050-8 · Cited by 830
Abe, T., Sugihara, H., Nawa, H., Shigemoto, R., Mizuno, N., & Nakanishi, S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42219-3 · Cited by 815
Cited by
Sorted by citations
Items 301–400 of 859
Holst, S. C., Sousek, A., Hefti, K., Saberi-Moghadam, S., Buck, A., Ametamey, S. M., Scheidegger, M., Franken, P., Henning, A., Seifritz, E., et al. (2017) · eLife · doi:10.7554/elife.28751 · Cited by 66
Polese, D. (2002) · Neuropsychopharmacology · doi:10.1016/s0893-133x(02)00371-8 · Cited by 66
The Evolutionary Assembly of Neuronal Machinery
Arendt, D. (2020) · Current Biology · doi:10.1016/j.cub.2020.04.008 · Cited by 72
Mizutani, A., Kuroda, Y., Futatsugi, A., Furuichi, T., & Mikoshiba, K. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4738-07.2008 · Cited by 65
Chen, T., Yang, Y., Luo, P., Liu, W., Dai, S., Zheng, X.-R., Zhou, F., & Jiang, X. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.09.004 · Cited by 65
Ary, A. W., & Szumlinski, K. K. (2007) · Brain Research · doi:10.1016/j.brainres.2007.09.035 · Cited by 64
Regulation of Endothelial Cell Barrier Function by Store‐Operated Calcium Entry
Cioffi, D. L., & Stevens, T. (2006) · Microcirculation · doi:10.1080/10739680600930354 · Cited by 64
Soloviev, M., Ciruela, F., Chan, W., & McIlhinney, R. A. J. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3436 · Cited by 64
Tappe‐Theodor, A., & Kuner, R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505900103 · Cited by 66
Molecular constituents and phosphorylation‐dependent regulation of the post‐synaptic density
Yamauchi, T. (2002) · Mass Spectrometry Reviews · doi:10.1002/mas.10033 · Cited by 63
Group I Metabotropic Glutamate Receptors: A Role in Neurodevelopmental Disorders?
Catania, M. V., D’Antoni, S., Bonaccorso, C. M., Aronica, E., Bear, M. F., & Nicoletti, F. (2007) · Molecular Neurobiology · doi:10.1007/s12035-007-0022-1 · Cited by 61
Lesage, A., & Steckler, T. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.12.043 · Cited by 63
Fukaya, M., Uchigashima, M., Nomura, S., Hasegawa, Y., Kikuchi, H., & Watanabe, M. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06495.x · Cited by 63
Endoplasmic Reticulum Dysfunction in Brain Pathology: Critical Role of Protein Synthesis
Paschen, W. (2004) · Current Neurovascular Research · doi:10.2174/1567202043480125 · Cited by 62
Michele Salanova, A., Priori, G., Barone, V., Intravaia, E., Flucher, B. E., Ciruela, F., McIlhinney, R. A. J., Parys, J. B., Mikoshiba, K., & Sorrentino, V. (2002) · Cell Calcium · doi:10.1016/s0143416002001549 · Cited by 62
Microglia maintain the normal structure and function of the hippocampal astrocyte network
Du, Y., Brennan, F. H., Popovich, P. G., & Zhou, M. (2022) · Glia · doi:10.1002/glia.24179 · Cited by 61
Homer1 Mediates Acute Stress-Induced Cognitive Deficits in the Dorsal Hippocampus
Wagner, K. V., Hartmann, J., Mangold, K., Wang, X., Labermaier, C., Liebl, C., Wolf, M., Gassen, N. C., Holsboer, F., Rein, T., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.4333-12.2013 · Cited by 61
Mutation screening of the Homer gene family and association analysis in schizophrenia
Norton, N., Williams, H. J., Williams, N. M., Spurlock, G., Zammit, S., Jones, G., Jones, S., Owen, R., O’Donovan, M. C., & Owen, M. J. (2003) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.20032 · Cited by 61
Requirement of the immediate early gene vesl-1S/homer-1a for fear memory formation
Inoue, N., Nakao, H., Suzuki-Migishima, R., Hino, T., Matsui, M., Hayashi, F., Nakao, K., Manabe, T., Aiba, A., & Inokuchi, K. (2009) · Molecular Brain · doi:10.1186/1756-6606-2-7 · Cited by 63
Li, S., Liu, X., & Ascoli, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13386 · Cited by 61
Petralia, R. S., Wang, Y., Sans, N., Worley, P. F., Hammer, J. A., & Wenthold, R. J. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01553.x · Cited by 60
Self-citationLocation-Dependent Signaling of the Group 1 Metabotropic Glutamate Receptor mGlu5
Jong, Y.-J. I., Sergin, I., Purgert, C. A., & O’Malley, K. L. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.094763 · Cited by 66
Structure of metabotropic glutamate receptor C-terminal domains in contact with interacting proteins
Enz, R. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00052 · Cited by 63
Structure and molecular organization of dendritic spines.
Tashiro, A., & Yuste, R. (2003) · PubMed · doi:10.14670/hh-18.617 · Cited by 60
Protein-protein interaction and functionTRPC channels
Kiselyov, K. I., Kim, J. Y., Zeng, W., & Muallem, S. (2005) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-005-1442-2 · Cited by 60
The origin and evolution of synaptic proteins – choanoflagellates lead the way
Burkhardt, P. (2015) · Journal of Experimental Biology · doi:10.1242/jeb.110247 · Cited by 59
IP3 Receptor Plasticity Underlying Diverse Functions
Hamada, K., & Mikoshiba, K. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021119-034433 · Cited by 59
The Homer-1 protein Ania-3 interacts with the plasma membrane calcium pump
Sgambato, V., Xiong, Y., Berke, J. D., Hyman, S. E., & Strehler, E. E. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.020 · Cited by 59
Spellmann, I., Rujescu, D., Musil, R., Mayr, A. J., Giegling, I., Genius, J., Zill, P., Dehning, S., Opgen-Rhein, M., Cerovecki, A., et al. (2010) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2010.06.004 · Cited by 59
Analysis of the QTL for sleep homeostasis in mice:Homer1ais a likely candidate
Mackiewicz, M., Paigen, B. J., Naidoo, N. N., & Pack, A. I. (2008) · Physiological Genomics · doi:10.1152/physiolgenomics.00189.2007 · Cited by 59
Homer‐1a/Vesl‐1S enhances hippocampal synaptic transmission
Hennou, S., Kato, A., Schneider, E. M., Lundstrom, K. H., Gähwiler, B. H., Inokuchi, K., Gerber, U. R., & Ehrengruber, M. U. (2003) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2003.02812.x · Cited by 59
Organisation of G-protein-coupled receptor signalling complexes by scaffolding proteins
Kreienkamp, H. (2002) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(02)00203-5 · Cited by 59
Molecular Determinants of Metabotropic Glutamate Receptor 1B Trafficking
Chan, W. Y., Soloviev, M., Ciruela, F., & McIlhinney, R. A. J. (2001) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2001.0965 · Cited by 59
Calcium signaling complexes in microdomains of polarized secretory cells
Kiselyov, K. I., Wang, X., Shin, D. M., Wj, Z., & Muallem, S. (2006) · Cell Calcium · doi:10.1016/j.ceca.2006.08.009 · Cited by 57
Impaired mTORC1-Dependent Expression of Homer-3 Influences SCA1 Pathophysiology
Ruegsegger, C., Stucki, D., Steiner, S., Angliker, N., Radecke, J., Keller, E., Zuber, B., Rüegg, M. A., & Saxena, S. (2016) · Neuron · doi:10.1016/j.neuron.2015.11.033 · Cited by 55
Phosphorylation of group I metabotropic glutamate receptors (mGluR1/5) in vitro and in vivo
Mao, L., Liu, X., Zhang, G.-C., Chu, X., Fibuch, E. E., Wang, L. S., Liu, Z., & Wang, J. Q. (2008) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.05.034 · Cited by 57
de Bartolomeis, A., & Tomasetti, C. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8293-6 · Cited by 58
Michele Salanova, A., Bortoloso, E., Schiffl, G., Gutsmann, M., Belavý, D. L., Felsenberg, D., Furlan, S., Pompeo Volpe, D., & Blottner, D. (2011) · The FASEB Journal · doi:10.1096/fj.11-186049 · Cited by 57
Mellentin, C., Jahnsen, H., & Abraham, W. C. (2006) · Neuropharmacology · doi:10.1016/j.neuropharm.2006.07.009 · Cited by 57
Inoue, A., & Okabe, S. (2003) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(03)00077-1 · Cited by 62
Genter, M. B., Veldhoven, P. P. V., Jegga, A. G., Sakthivel, B., Kong, S., Stanley, K., Witte, D. P., Ebert, C. L., & Aronow, B. J. (2003) · Physiological Genomics · doi:10.1152/physiolgenomics.00117.2003 · Cited by 57
Evolutionary insights into premetazoan functions of the neuronal protein homer
Burkhardt, P., Grønborg, M., McDonald, K., Sulur, T., Wang, Q., & King, N. (2014) · Molecular Biology and Evolution · doi:10.1093/molbev/msu178 · Cited by 56
Metabotropic glutamate receptor trafficking
Suh, Y. H., Chang, K., & Roche, K. W. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.03.014 · Cited by 56
Luo, P., Chen, T., Zhao, Y., Zhang, L., Yang, Y., Liu, W., Li, S., Rao, W., Dai, S., Yang, J., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.116 · Cited by 55
Chen, T., Zhu, J., Zhang, C., Huo, K., Fei, Z., & Jiang, X. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055601 · Cited by 55
Neuronal activity-regulated alternative mRNA splicing
Hermey, G., Blüthgen, N., & Kuhl, D. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.06.002 · Cited by 51
Sylantyev, S., Savtchenko, L. P., Ermolyuk, Y. S., Michaluk, P., & Rusakov, D. A. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.026 · Cited by 53
Lutzu, S., & Castillo, P. E. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.02.019 · Cited by 54
Bockaert, J., Perroy, J., & Ango, F. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.0026-21.2021 · Cited by 50
Developmental roles for Homer: more than just a pretty scaffold
Foa, L. C., & Gasperini, R. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05726.x · Cited by 54
The PDZ Scaffold NHERF-2 Interacts with mGluR5 and Regulates Receptor Activity
Paquet, M., Asay, M. J., Fam, S. R., Inuzuka, H., Castleberry, A. M., Oller, H., Smith, Y., Yun, C. C., Traynelis, S. F., & Hall, R. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602262200 · Cited by 52
Regulation of the Level of Vesl-1S/Homer-1a Proteins by Ubiquitin-Proteasome Proteolytic Systems
Ageta, H., Kato, A., Hatakeyama, S., Nakayama, K. I., Isojima, Y., & Sugiyama, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011097200 · Cited by 52
The Amino Terminus of the Glial Glutamate Transporter GLT-1 Interacts with the LIM Protein Ajuba
Marie, H., Billups, D., Bedford, F. K., Dumoulin, A., Goyal, R. K., Longmore, G. D., Moss, S. J., & Attwell, D. (2002) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2001.1066 · Cited by 52
Tanchuck, M. A., Yoneyama, N., Ford, M. M., Fretwell, A. M., & Finn, D. A. (2010) · Alcohol · doi:10.1016/j.alcohol.2010.07.009 · Cited by 51
Choi, K. Y., Chung, S., & Roche, K. W. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6253-10.2011 · Cited by 51
Guo, W., Molinaro, G., Collins, K. A., Hays, S. A., Paylor, R. E., Worley, P. F., Szumlinski, K. K., & Huber, K. M. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2921-15.2016 · Cited by 54
Self-citationAlthausen, S., & Paschen, W. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00208-4 · Cited by 51
The N-terminal domain of Homer/Vesl is a new class II EVH1 domain
Barzik, M., Carl, U. D., Schubert, W., Frank, R., Wehland, J., & Heinz, D. W. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4640 · Cited by 51
Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons
Maximov, A., Tang, T.-S., & Борисович, Б. И. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(02)00027-1 · Cited by 51
Scaffolding protein Homer1a protects against NMDA-induced neuronal injury
Wang, Y., Rao, W., Zhang, C., Zhang, C., Liu, M.-D., Han, F., Yao, L.-B., Han, H., Luo, P., Su, N., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.216 · Cited by 49
Sakagami, Y., Yamamoto, K., Sugiura, S., Inokuchi, K., Hayashi, T., & Kato, N. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04165.x · Cited by 50
Kurnellas, M., Fakira, A. K., Li, H., Deng, L., Ehrlich, D. J., & Elkabes, S. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.10.010 · Cited by 51
Acute administration of antipsychotics modulates Homer striatal gene expression differentially
de Bartolomeis, A., Aloj, L., Ambesi‐Impiombato, A., Bravi, D., Caracò, C., Muscettola, G., & Barone, P. (2002) · Molecular Brain Research · doi:10.1016/s0169-328x(01)00327-8 · Cited by 50
Nash, M. S., Saunders, R. M., Young, K. W., Challiss, R. A. J., & Nahorski, S. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007600200 · Cited by 50
CXCR4-mediated glutamate exocytosis from astrocytes
Calì, C., & Bezzi, P. (2010) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2010.05.004 · Cited by 49
Investigational NMDA receptor modulators for depression
Szewczyk, B., Pałucha-Poniewiera, A., Poleszak, E., Pilc, A., & Nowak, G. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2012.638916 · Cited by 50
Regulation of Homer and group I metabotropic glutamate receptors by nicotine
Kane, J. K., Hwang, Y., Konu, Ö., Loughlin, S. E., Leslie, F. M., & Li, M. D. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.03945.x · Cited by 49
Self-citationFerreri-Jacobia, M., Mak, D. D., & Foskett, J. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409462200 · Cited by 49
Isope, P., Hildebrand, M. E., & Snutch, T. P. (2010) · The Cerebellum · doi:10.1007/s12311-010-0195-4 · Cited by 58
Tomasetti, C., Dell’Aversano, C., Iasevoli, F., Marmo, F., & de Bartolomeis, A. (2011) · Progress in Neuro-psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2010.10.025 · Cited by 49
Homer1 Scaffold Proteins Govern Ca2+ Dynamics in Normal and Reactive Astrocytes
Buscemi, L., Ginet, V., Lopatář, J., Montana, V., Pucci, L., Spagnuolo, P., Zehnder, T., Grubišić, V., Truttman, A., Sala, C., et al. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw078 · Cited by 52
Mutations in Metabotropic Glutamate Receptor 1 Contribute to Natural Short Sleep Trait
Shi, G., Chen, Y., Fan, Z., Xing, L., Mostovoy, Y., Kwok, P., Ashbrook, L. H., Krystal, A. D., Ptáček, L. J., & Fu, Y. (2020) · Current Biology · doi:10.1016/j.cub.2020.09.071 · Cited by 49
Lipid Rafts Establish Calcium Waves in Hepatocytes
Nagata, J., Guerra, M. T., Shugrue, C., Gomes, D. A., Nagata, N., & Nathanson, M. H. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.03.115 · Cited by 48
Inositol 1,4,5‐trisphosphate receptor (type 1) phosphorylation and modulation by Cdc2
Malathi, K., Kohyama, S., Ho, M., Soghoian, D. Z., Li, X., Silane, M. F., Berenstein, A., & Jayaraman, T. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10720 · Cited by 48
Mechanisms of neuronal cell death: diverse roles of calcium in the various subcellular compartments
Paschen, W. (2003) · Cell Calcium · doi:10.1016/s0143-4160(03)00138-6 · Cited by 48
Diversity of polyproline recognition by EVH1 domains
Francis, C. P. (2009) · Frontiers in bioscience · doi:10.2741/3281 · Cited by 48
What we don't know about the structure of ryanodine receptor calcium release channels
Dulhunty, A. F., & Pouliquin, P. (2003) · Clinical and Experimental Pharmacology and Physiology · doi:10.1046/j.1440-1681.2003.03904.x · Cited by 46
Bodzęta, A., Scheefhals, N., & MacGillavry, H. D. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108799 · Cited by 49
Tomasetti, C., Dell’Aversano, C., Iasevoli, F., & de Bartolomeis, A. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.08.022 · Cited by 51
Doherty, A. J., Coutinho, V., Collingridge, G. L., & Henley, J. M. (1999) · Biochemical Journal · doi:10.1042/bj3410415 · Cited by 46
Matosin, N., Fernandez, F., Lum, J. S., & Newell, K. A. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.08.003 · Cited by 47
Kato, H., Kassai, H., Watabe, A. M., Aiba, A., & Manabe, T. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.232942 · Cited by 46
Usui, S., Konno, D., Hori, K., Maruoka, H., Okabe, S., Fujikado, T., Tano, Y., & Sobue, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210802200 · Cited by 46
Waldhoer, M., Wise, A., Milligan, G., Freissmuth, M., & Nanoff, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30571 · Cited by 46
Orlando, L. R., Ayala, R., Kett, L. R., Curley, A. A., Duffner, J. L., Bragg, D. C., Tsai, L., Dunah, A. W., & Young, A. B. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06139.x · Cited by 45
Tadavarty, R., Rajput, P. S., Wong, J. M., Kumar, U., & Sastry, B. R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024933 · Cited by 49
Spatial organization of intracellular Ca2+ signals
Konieczny, V., Keebler, M. V., & Taylor, C. W. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.09.006 · Cited by 46
Regulation of AMPA receptor trafficking and exit from the endoplasmic reticulum
Pick, J. E., & Ziff, E. B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.03.004 · Cited by 48
Calcium-Dependent Ion Channels and the Regulation of Arteriolar Myogenic Tone
Jackson, W. F. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.770450 · Cited by 45
Brandstätter, J. H., Dick, O., & Boeckers, T. M. (2004) · The Journal of Comparative Neurology · doi:10.1002/cne.20194 · Cited by 43
Paquet, M., Ribeiro, F. M., Guadagno, J., Esseltine, J. L., Ferguson, S. S. G., & Cregan, S. P. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-9 · Cited by 45
Evidence for the Presence of Two Homer 1 Transcripts in Skeletal and Cardiac Muscles
Sandonà, D., Tibaldo, E., & Pompeo Volpe, D. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3948 · Cited by 45
Vessey, J. P., & Karra, D. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04662.x · Cited by 44
Homer2 and Homer3 interact with amyloid precursor protein and inhibit Aβ production
Parisiadou, L., Bethani, I., Michaki, V., Krousti, K., Rapti, G., & Efthimiopoulos, S. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.02.004 · Cited by 43
Protective effect of Homer 1a against hydrogen peroxide-induced oxidative stress in PC12 cells
Luo, P., Chen, T., Zhao, Y., Xu, H., Huo, K., Zhao, M., Yang, Y., & Fei, Z. (2012) · Free Radical Research · doi:10.3109/10715762.2012.678340 · Cited by 44
de Bartolomeis, A., & Fiore, G. (2004) · International review of neurobiology · doi:10.1016/s0074-7742(04)59009-8 · Cited by 42
Keuren‐Jensen, K. R. V., & Cline, H. T. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.5083-05.2006 · Cited by 44
Steuber, V., & Willshaw, D. J. (2004) · Journal of Computational Neuroscience · doi:10.1023/b:jcns.0000037678.26155.b5 · Cited by 44
Homer Protein Increases Activation of Ca2+ Sparks in Permeabilized Skeletal Muscle
Ward, C. W., Feng, W., Tu, J., Pessah, I. N., Worley, P. F., & Schneider, M. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311422200 · Cited by 44
Self-citationColosetti, P., Tunwell, R. E. A., Cruttwell, C., Arsanto, J., Mauger, J., & Cassio, D. (2003) · Journal of Cell Science · doi:10.1242/jcs.00482 · Cited by 44
Metadata
- Authors
- Tu, J. C., Xiao, B., Yuan, J. P., Lanahan, A. A., Leoffert, K., Li, M., Linden, D. J., & Worley, P. F.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Worley, Paul F
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1998-10
- Volume
- 21
- Issue
- 4
- Pages
- 717-726
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2164762131
- Cited by
- 862
- References
- 68
- Citations by year
- 2026: 14 · 2025: 7 · 2024: 12 · 2023: 6 · 2022: 21 · 2021: 23 · 2020: 12 · 2019: 19 · 2018: 23 · 2017: 32 · 2016: 23 · 2015: 23 · 2014: 27 · 2013: 36 · 2012: 41
- FWCI
- 15.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Neuron (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Genentech
- National Institute of Mental Health (K02MH001152, KO2 MH01152)
- National Institute on Drug Abuse (DA 10309, DA 11742, R01DA011742)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Keywords
- Homer proteins, group I metabotropic glutamate receptors, IP3 receptor, proline-rich motif, receptor complex formation, intracellular calcium release, calcium signaling, immediate early genes, synaptic proteins
- MeSH terms
- Homer Scaffolding Proteins, Amino Acid Sequence, Animals, Calcium, Carrier Proteins, Intracellular Membranes, Ligands, Molecular Sequence Data, Neuropeptides, Proline, Time Factors, Calcium Channels, Gene Expression, Genes, Immediate-Early, Receptors, Metabotropic Glutamate, Receptors, Cytoplasmic and Nuclear, Glutamic Acid, GTP Phosphohydrolases, Dynamins, Rats, Inositol 1,4,5-Trisphosphate Receptors
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