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Reelin and brain development
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A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
D'Arcangelo, G., G. Miao, G., Chen, S.-C., Scares, H. D., Morgan, J. I., & Curran, T. (1995) · Nature · doi:10.1038/374719a0 · Cited by 1,748
Schizophrenia as a Disorder of Neurodevelopment
Lewis, D. A., & Levitt, P. (2002) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.25.112701.142754 · Cited by 1,163
Isolation of radial glial cells by fluorescent-activated cell sorting reveals a neuronal lineage
Malatesta, P., Hartfuss, E., & Götz, M. (2000) · Development · doi:10.1242/dev.127.24.5253 · Cited by 1,157
Hiesberger, T., Trommsdorff, M., Howell, B. W., Goffinet, A., Mumby, M. C., Cooper, J. A., & Herz, J. (1999) · Neuron · doi:10.1016/s0896-6273(00)80861-2 · Cited by 916
Self-citationOgawa, M., Miyata, T., Nakajimat, K., Yagyu, K., Seike, M., Ikenaka, K., Yamamoto, H., & Mikoshibat, K. (1995) · Neuron · doi:10.1016/0896-6273(95)90329-1 · Cited by 889 · cited 1×
“Reln can be studied using antibodies against N- and C-terminal epitope”
BackgroundReelin Is a Ligand for Lipoprotein Receptors
D'Arcangelo, G., Homayouni, R., Keshvara, L., Rice, D. S., Sheldon, M., & Curran, T. (1999) · Neuron · doi:10.1016/s0896-6273(00)80860-0 · Cited by 808 · cited 1×
“Reln can be endocytosed after binding to the surface of receptor transfected cell”
BackgroundScrambler and yotari disrupt the disabled gene and produce a reeler -like phenotype in mice
Sheldon, M., Rice, D. S., D'Arcangelo, G., Yoneshima, H., Nakajima, K., Mikoshiba, K., Howell, B. W., Cooper, J. A., Goldowitz, D., & Curran, T. (1997) · Nature · doi:10.1038/39601 · Cited by 638
Falconer, D. S. (1951) · Journal of Genetics · doi:10.1007/bf02996215 · Cited by 539
Structure of the LDL Receptor Extracellular Domain at Endosomal pH
Rudenko, G., Henry, L., Henderson, K., Ichtchenko, K., Brown, M. S., Goldstein, J. L., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1078124 · Cited by 482
A role for Cajal–Retzius cells and reelin in the development of hippocampal connections
Del Río, J. A., Heimrich, B., Borrell, V., Förster, E., Drakew, A., Alcántara, S., Nakajima, K., Miyata, T., Ogawa, M., Mikoshiba, K., et al. (1997) · Nature · doi:10.1038/385070a0 · Cited by 472
Research works printed but not linked: 88
- Rice, D. S. & Curran, T. Role of the reelin signaling pathway in central nervous system development. Annu. Rev. Neurosci. 24, 1005–1039 (2001). · DOI · Paper page
- Andersen, T. E., Finsen, B., Goffinet, A. M., Issinger, O. G. & Boldyreff, B. A reeler mutant mouse with a new, spontaneous mutation in the reelin gene. Brain Res. Mol. Brain Res. 105, 153–156 (2002). This work is important as it demonstrates biochemically the direct binding of Reln to lipoprotein receptors, thereby confirming the genetic data of Trommsdorf et al . described in reference 11. · DOI
- Hong, S. E. et al. Autosomal recessive lissencephaly with cerebellar hypoplasia is associated with human RELN mutations. Nature Genet. 26, 93–96 (2000). · DOI · Paper page
- Ware, M. L. et al. Aberrant splicing of a mouse disabled homolog, mdab1, in the scrambler mouse. Neuron 19, 239–249 (1997). This paper reported the positional cloning of the scrambler mutation, with identification of mutations in the Dab1 gene. · DOI · Paper page
- Howell, B. W., Hawkes, R., Soriano, P. & Cooper, J. A. Neuronal position in the developing brain is regulated by mouse disabled-1. Nature 389, 733–737 (1997). This paper reported the knockout of the Dab1 gene and showed that it mimics the reeler phenotype, thereby establishing the key role of the Dab1 adaptor. Together with references 7 and 8, it established the position of Dab1 in the Reln pathway. · DOI · Paper page
- Trommsdorff, M. et al. Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2. Cell 97, 689–701 (1999). This paper showed that mice with mutations in the VLDLR and ApoER2 genes have a reeler -like phenotype, whereas single mutants have only subtle anomalies of brain development. This demonstrated the importance of lipoprotein receptors in the pathway. · DOI · Paper page
- Rice, D. S. et al. The reelin pathway modulates the structure and function of retinal synaptic circuitry. Neuron 31, 929–941 (2001). · DOI
- Yip, J. W., Yip, Y. P., Nakajima, K. & Capriotti, C. Reelin controls position of autonomic neurons in the spinal cord. Proc. Natl Acad. Sci. USA 97, 8612–8616 (2000). · DOI
- Meyer, G., Lambert de Rouvroit, C., Goffinet, A. M. & Wahle, P. Disabled-1 mRNA and protein expression in developing human cortex. Eur. J. Neurosci. 17, 517–525 (2003). · DOI
- Kobold, D. et al. Expression of reelin in hepatic stellate cells and during hepatic tissue repair: a novel marker for the differentiation of HSC from other liver myofibroblasts. J. Hepatol. 36, 607–613 (2002). · DOI
- Buchaille, R., Couble, M. L., Magloire, H. & Bleicher, F. A substractive PCR-based cDNA library from human odontoblast cells: identification of novel genes expressed in tooth forming cells. Matrix Biol. 19, 421–430 (2000). · DOI
- Smalheiser, N. R. et al. Expression of reelin in adult mammalian blood, liver, pituitary pars intermedia, and adrenal chromaffin cells. Proc. Natl Acad. Sci. USA 97, 1281–1286 (2000). · DOI · Paper page
- Ikeda, Y. & Terashima, T. Expression of reelin, the gene responsible for the reeler mutation, in embryonic development and adulthood in the mouse. Dev. Dyn. 210, 157–172 (1997). · DOI
- Bar, I. et al. A YAC contig containing the reeler locus with preliminary characterization of candidate gene fragments. Genomics 26, 543–549 (1995). · DOI
- DeSilva, U. et al. The human reelin gene: isolation, sequencing, and mapping on chromosome 7. Genome Res. 7, 157–164 (1997). · DOI
- Royaux, I., Lambert de Rouvroit, C., D'Arcangelo, G., Demirov, D. & Goffinet, A. M. Genomic organization of the mouse reelin gene. Genomics 46, 240–250 (1997). · DOI
- Tremolizzo, L. et al. An epigenetic mouse model for molecular and behavioral neuropathologies related to schizophrenia vulnerability. Proc. Natl Acad. Sci. USA 99, 17095–17100 (2002). · DOI
- Chen, Y., Sharma, R. P., Costa, R. H., Costa, E. & Grayson, D. R. On the epigenetic regulation of the human reelin promoter. Nucleic Acids Res. 30, 2930–2939 (2002). · DOI · Paper page
- Chen, M. L., Chen, S. Y., Huang, C. H. & Chen, C. H. Identification of a single nucleotide polymorphism at the 5' promoter region of human reelin gene and association study with schizophrenia. Mol. Psychiatry 7, 447–448 (2002). · DOI
- Bar, I., Lambert de Rouvroit, C. & Goffinet, A. M. The evolution of cortical development. An hypothesis based on the role of the Reelin signaling pathway. Trends Neurosci. 23, 633–638 (2000). · DOI
- Lambert de Rouvroit, C., Bernier, B., Royaux, I., de Bergeyck, V. & Goffinet, A. M. Evolutionarily conserved, alternative splicing of reelin during brain development. Exp. Neurol. 156, 229–238 (1999). · DOI
- D'Arcangelo, G. et al. Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal antibody. J. Neurosci. 17, 23–31 (1997). · DOI · Paper page
- de Bergeyck, V., Naerhuyzen, B., Goffinet, A. M. & Lambert de Rouvroit, C. A panel of monoclonal antibodies against reelin, the extracellular matrix protein defective in reeler mutant mice. J. Neurosci. Methods 82, 17–24 (1998). · DOI
- Lambert de Rouvroit, C. et al. Reelin, the extracellular matrix protein deficient in reeler mutant mice, is processed by a metalloproteinase. Exp. Neurol. 156, 214–217 (1999). · DOI
- Nimpf, J. & Schneider, W. J. From cholesterol transport to signal transduction: low density lipoprotein receptor, very low density lipoprotein receptor, and apolipoprotein E receptor-2. Biochim. Biophys. Acta 1529, 287–298 (2000). · DOI
- Howell, B. W., Lanier, L. M., Frank, R., Gertler, F. B. & Cooper, J. A. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol. Cell. Biol. 19, 5179–5188 (1999). · DOI · Paper page
- Benhayon, D., Magdaleno, S. & Curran, T. Binding of purified Reelin to ApoER2 and VLDLR mediates tyrosine phosphorylation of Disabled-1. Brain Res. Mol. Brain Res. 112, 33–45 (2003). · DOI
- Boucher, P. et al. Platelet-derived growth factor mediates tyrosine phosphorylation of the cytoplasmic domain of the low Density lipoprotein receptor-related protein in caveolae. J. Biol. Chem. 277, 15507–15513 (2002). · DOI · Paper page
- Riddell, D. R., Sun, X. M., Stannard, A. K., Soutar, A. K. & Owen, J. S. Localization of apolipoprotein E receptor 2 to caveolae in the plasma membrane. J. Lipid Res. 42, 998–1002 (2001). · DOI
- Kojima, T., Nakajima, K. & Mikoshiba, K. The disabled 1 gene is disrupted by a replacement with L1 fragment in yotari mice. Brain Res. Mol. Brain Res. 75, 121–127 (2000). · DOI
- Howell, B. W., Herrick, T. M. & Cooper, J. A. Reelin-induced tryosine phosphorylation of disabled 1 during neuronal positioning. Genes Dev. 13, 643–648 (1999). · DOI · Paper page
- Keshvara, L., Benhayon, D., Magdaleno, S. & Curran, T. Identification of reelin-induced sites of tyrosyl phosphorylation on disabled 1. J. Biol. Chem. 276, 16008–16014 (2001). · DOI
- Lambert de Rouvroit, C. & Goffinet, A. M. Cloning of human DAB1 and mapping to chromosome 1p31-p32. Genomics 53, 246–247 (1998). · DOI
- Bar, I., Tissir, F., Lambert De Rouvroit, C., De Backer, O. & Goffinet, A. M. The gene encoding disabled-1 (DAB1), the intracellular adaptor of the reelin pathway, reveals unusual complexity in human and mouse. J. Biol. Chem., 278, 5802-5812, (2003). · DOI
- Howell, B. W., Herrick, T. M., Hildebrand, J. D., Zhang, Y. & Cooper, J. A. Dab1 tyrosine phosphorylation sites relay positional signals during mouse brain development. Curr. Biol. 10, 877–885 (2000). · DOI · Paper page
- Herrick, T. M. & Cooper, J. A. A hypomorphic allele of dab1 reveals regional differences in reelin-Dab1 signaling during brain development. Development 129, 787–796 (2002). This paper shows that a Dab1 null mutation can be rescued fully by a knock-in of the normal Dab1 cDNA, and partially by a partial cDNA that contains the PI/PTB domain and the adjacent region that encodes key Tyr residues, but not by a cDNA in which five Tyr residues are replaced by Phe. · DOI
- Keshvara, L., Magdaleno, S., Benhayon, D. & Curran, T. Cyclin-dependent kinase 5 phosphorylates disabled 1 independently of Reelin signaling. J. Neurosci. 22, 4869–4877 (2002). · DOI
- Kubo, K., Mikoshiba, K. & Nakajima, K. Secreted Reelin molecules form homodimers. Neurosci. Res. 43, 381–388 (2002). · DOI
- Jossin, Y. et al. The Reelin signaling pathway: some recent developments. Cereb. Cortex, 13, 627-633 (2003). · DOI
- Miyata, T., Nakajima, K., Mikoshiba, K. & Ogawa, M. Regulation of Purkinje cell alignment by reelin as revealed with CR-50 antibody. J. Neurosci. 17, 3599–3609 (1997). · DOI · Paper page
- Nakajima, K., Mikoshiba, K., Miyata, T., Kudo, C. & Ogawa, M. Disruption of hippocampal development in vivo by CR-50 mAb against reelin. Proc. Natl Acad. Sci. USA. 94, 8196–8201 (1997). · DOI · Paper page
- Bock, H. H. & Herz, J. Reelin activates SRC family tyrosine kinases in neurons. Curr. Biol. 13, 18–26 (2003). · DOI · Paper page
- Arnaud, L., Ballif, B. A., Forster, E. & Cooper, J. A. Fyn tyrosine kinase is a critical regulator of disabled-1 during brain development. Curr. Biol. 13, 9–17 (2003). References 54 and 55 show that tyrosine kinases of the Src family, particularly Fyn and Yes, are key elements in the transduction of the Reln signal, and that they mediate Dab1 tyrosine phosphorylation. These two studies also indicate that there is redundancy among this kinase family. · DOI · Paper page
- Weiss, A. & Littman, D. R. Signal transduction by lymphocyte antigen receptors. Cell 76, 263–274 (1994). · DOI · Paper page
- Zhang, Z., Coomans, C. & David, G. Membrane heparan sulfate proteoglycan-supported FGF2-FGFR1 signaling: evidence in support of the 'cooperative end structures' model. J. Biol. Chem. 276, 41921–41929 (2001). · DOI
- Loukinova, E. et al. Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptor function between LRP and the PDGF. J. Biol. Chem. 277, 15499–15506 (2002). · DOI · Paper page
- Pinson, K. I., Brennan, J., Monkley, S., Avery, B. J. & Skarnes, W. C. An LDL-receptor-related protein mediates Wnt signalling in mice. Nature 407, 535–538 (2000). · DOI
- Meyer, G., De Rouvroit, C. L., Goffinet, A. M. & Wahle, P. Disabled-1 mRNA and protein expression in developing human cortex. Eur. J. Neurosci. 17, 517–525 (2003). · DOI
- Hack, I., Bancila, M., Loulier, K., Carroll, P. & Cremer, H. Reelin is a detachment signal in tangential chain-migration during postnatal neurogenesis. Nature Neurosci. 5, 939–945 (2002). · DOI
- Kim, H. M. et al. Reelin function in neural stem cell biology. Proc. Natl Acad. Sci. USA 99, 4020–4025 (2002). · DOI
- Tissir, F., Lambert de Rouvroit, C., Sire, J. Y., Meyer, G. & Goffinet, A. M. Reelin expression during embryonic brain development in Crocodylus niloticus. J. Comp. Neurol. 457, 250–262 (2003). · DOI
- Haas, C. A. et al. Role for reelin in the development of granule cell dispersion in temporal lobe epilepsy. J. Neurosci. 22, 5797–5802 (2002). · DOI
- Perez-Costas, E. et al. Reelin immunoreactivity in the larval sea lamprey brain. J. Chem. Neuroanat. 23, 211–221 (2002). · DOI
- Costagli, A., Kapsimali, M., Wilson, S. W. & Mione, M. Conserved and divergent patterns of Reelin expression in the zebrafish central nervous system. J. Comp. Neurol. 450, 73–93 (2002). · DOI
- Rice, D. S. & Curran, T. Disabled-1 is expressed in type AII amacrine cells in the mouse retina. J. Comp. Neurol. 424, 327–338 (2000). · DOI
- Pearlman, A. L., Faust, P. L., Hatten, M. E. & Brunstrom, J. E. New directions for neuronal migration. Curr. Opin. Neurobiol. 8, 45–54 (1998). · DOI
- Frotscher, M. Cajal-Retzius cells, Reelin, and the formation of layers. Curr. Opin. Neurobiol. 8, 570–575 (1998). · DOI · Paper page
- Lambert de Rouvroit, C. & Goffinet, A. M. Neuronal migration. Mech. Dev. 105, 47–56 (2001). · DOI
- Noctor, S. C., Flint, A. C., Weissman, T. A., Dammerman, R. S. & Kriegstein, A. R. Neurons derived from radial glial cells establish radial units in neocortex. Nature 409, 714–720 (2001). · DOI · Paper page
- Miyata, T., Kawaguchi, A., Okano, H. & Ogawa, M. Asymmetric inheritance of radial glial fibers by cortical neurons. Neuron 31, 727–741 (2001). · DOI · Paper page
- Nadarajah, B., Brunstrom, J. E., Grutzendler, J., Wong, R. O. & Pearlman, A. L. Two modes of radial migration in early development of the cerebral cortex. Nature Neurosci. 4, 143–150 (2001). · DOI · Paper page
- Nadarajah, B. & Parnavelas, J. G. Modes of neuronal migration in the developing cerebral cortex. Nature Rev. Neurosci. 3, 423–432 (2002). · DOI · Paper page
- Deller, T. et al. The hippocampus of the reeler mutant mouse: fiber segregation in area CA1 depends on the position of the postsynaptic target cells. Exp. Neurol. 156, 254–267 (1999). · DOI
- Jossin, Y. & Goffinet, A. M. Reelin does not directly influence axonal growth. J. Neurosci. 21, RC183 (2001). · DOI
- Teillon, S. M., Yiu, G. & Walsh, C. A. Reelin is expressed in the accessory olfactory system, but is not a guidance cue for vomeronasal axons. Brain Res. Dev. Brain Res. 140, 303–307 (2003). · DOI
- Walsh, C. A. & Goffinet, A. M. Potential mechanisms of mutations that affect neuronal migration in man and mouse. Curr. Opin. Genet. Dev. 10, 270–274 (2000). · DOI
- Phelps, P. E., Rich, R., Dupuy-Davies, S., Rios, Y. & Wong, T. Evidence for a cell-specific action of Reelin in the spinal cord. Dev. Biol. 244, 180–198 (2002). · DOI
- Magdaleno, S., Keshvara, L. & Curran, T. Rescue of ataxia and preplate splitting by ectopic expression of Reelin in reeler mice. Neuron 33, 573–586 (2002). This is the first attempt to rescue the reeler phenotype by transgenesis with a Reln cDNA under the control of the nestin promoter. A partial rescue was obtained, even though Reln was expressed ectopically in the ventricular zone instead of Cajal–Retzius cells. This provides an argument for an indirect action of Reln that would make neurons responsive to another signal in the marginal zone. · DOI
- Hammond, V., Howell, B., Godinho, L. & Tan, S. S. Disabled-1 functions cell autonomously during radial migration and cortical layering of pyramidal neurons. J. Neurosci. 21, 8798–8808 (2001). · DOI
- Yang, H., Jensen, P. & Goldowitz, D. The community effect and Purkinje cell migration in the cerebellar cortex: analysis of scrambler chimeric mice. J. Neurosci. 22, 464–470 (2002). By studying chimaeras produced by aggregation of normal and Dab1 mutant morulae, these authors show that some actions of Dab1 are not fully explained by a cell-autonomous effect of this intracellular adaptor, implying a 'community effect' that hints at the importance of cell–cell interaction events. · DOI
- Goffinet, A. M. An early development defect in the cerebral cortex of the reeler mouse. A morphological study leading to a hypothesis concerning the action of the mutant gene. Anat. Embryol. (Berl.) 157, 205–216 (1979). · DOI
- Dulabon, L. et al. Reelin binds α3β1 integrin and inhibits neuronal migration. Neuron 27, 33–44 (2000). · DOI · Paper page
- Costa, E., Davis, J., Pesold, C., Tueting, P. & Guidotti, A. The heterozygote reeler mouse as a model for the development of a new generation of antipsychotics. Curr. Opin. Pharmacol. 2, 56–62 (2002). · DOI
- Fatemi, S. H., Kroll, J. L. & Stary, J. M. Altered levels of Reelin and its isoforms in schizophrenia and mood disorders. Neuroreport 12, 3209–3215 (2001). · DOI
- Guidotti, A., Pesold, C. & Costa, E. New neurochemical markers for psychosis: a working hypothesis of their operation. Neurochem. Res. 25, 1207–1218 (2000). · DOI
- Impagnatiello, F. et al. A decrease of reelin expression as a putative vulnerability factor in schizophrenia. Proc. Natl Acad. Sci. USA 95, 15718–15723 (1998). · DOI · Paper page
- Fatemi, S. H. The role of Reelin in pathology of autism. Mol. Psychiatry 7, 919–920 (2002). · DOI
- Andres, C. Molecular genetics and animal models in autistic disorder. Brain Res. Bull. 57, 109–119 (2002). · DOI
- Zhang, H. et al. Reelin gene alleles and susceptibility to autism spectrum disorders. Mol. Psychiatry 7, 1012–1017 (2002). · DOI
- Stokstad, E. Development. New hints into the biological basis of autism. Science 294, 34–37 (2001). · DOI
- Krebs, M. O. et al. Absence of association between a polymorphic GGC repeat in the 5' untranslated region of the reelin gene and autism. Mol. Psychiatry 7, 801–804 (2002). · DOI
- Tueting, P. et al. The phenotypic characteristics of heterozygous reeler mouse. Neuroreport 10, 1329–1334 (1999). · DOI
- Ohkubo, N. et al. Apolipoprotein E and Reelin ligands modulate tau phosphorylation through an apolipoprotein E receptor/disabled-1/glycogen synthase kinase-3β cascade. FASEB J. 17, 295–297 (2003). · DOI
- Homayouni, R., Rice, D. S., Sheldon, M. & Curran, T. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J. Neurosci. 19, 7507–7515 (1999). · DOI
- Ohshima, T. & Mikoshiba, K. Reelin signaling and Cdk5 in the control of neuronal positioning. Mol. Neurobiol. 26, 153–166 (2002). · DOI
- Ko, J. et al. p35 and p39 are essential for cyclin-dependent kinase 5 function during neurodevelopment. J. Neurosci. 21, 6758–6771 (2001). · DOI · Paper page
- Beffert, U. et al. Reelin-mediated signaling locally regulates protein kinase B/Akt and glycogen synthase kinase 3β. J. Biol. Chem. 277, 49958–49964 (2002). · DOI · Paper page
- Brich, J. et al. Genetic modulation of tau phosphorylation in the mouse. J. Neurosci. 23, 187–192 (2003). · DOI
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Groc, L., Choquet, D., Stephenson, F. A., Verrier, D., Manzoni, O. J., & Chavis, P. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.1772-07.2007 · Cited by 225
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Self-citationAdlakha, Y. K., & Saini, N. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-33 · Cited by 213
Chai, X., Förster, E., Zhao, S., Bock, H. H., & Frotscher, M. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2934-08.2009 · Cited by 202
Chow, M. L., Pramparo, T., Winn, M. E., Barnes, C. C., Li, H.-R., Weiss, L., Fan, J.-B., Murray, S., April, C., Belinson, H., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002592 · Cited by 202
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QIU, S., KORWEK, K., PRATTDAVIS, A., PETERS, M., BERGMAN, M., & WEEBER, E. (2006) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2005.11.001 · Cited by 202
Chin, J., Massaro, C. M., Palop, J. J., Thwin, M. T., Yu, G.-Q., Bien-Ly, N., Bender, A., & Mucke, L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3758-06.2007 · Cited by 188
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Extracellular matrix abnormalities in schizophrenia
Berretta, S. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.08.010 · Cited by 179
Erbel-Sieler, C., Dudley, C., Zhou, Y., Wu, X., Estill, S. J., Han, T., Diaz-Arrastia, R., Brunskill, E. W., Potter, S. S., & McKnight, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405310101 · Cited by 178
Shaping Synapses by the Neural Extracellular Matrix
Ferrer-Ferrer, M., & Dityatev, A. (2018) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2018.00040 · Cited by 169
Role for Reelin in stabilizing cortical architecture
Frotscher, M. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.06.001 · Cited by 157
Evangelisti, C., Florian, M. C., Massimi, I., Dominici, C., Giannini, G., Galardi, S., Buè, M. C., Massalini, S., McDowell, H. P., Messi, E., et al. (2009) · The FASEB Journal · doi:10.1096/fj.09-134965 · Cited by 140
Converting juvenile into adult plasticity: a role for the brain's extracellular matrix
Gundelfinger, E. D., Frischknecht, R., Choquet, D., & Heine, M. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07253.x · Cited by 136
Bal, M., Leitz, J., Reese, A. L., Ramirez, D. M. O., Durakoglugil, M., Herz, J., Monteggia, L. M., & Kavalali, E. T. (2013) · Neuron · doi:10.1016/j.neuron.2013.08.024 · Cited by 131
Emerging topics in Reelin function
Förster, E., Bock, H. H., Herz, J., Chai, X., Frotscher, M., & Zhao, S. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07222.x · Cited by 130
Pujadas, L., Rossi, D., Andrés, R., Teixeira, C. M., Serra-Vidal, B., Parcerisas, A., Maldonado, R., Giralt, E., Carulla, N., & Soriano, E. (2014) · Nature Communications · doi:10.1038/ncomms4443 · Cited by 129
The extracellular matrix and synapses
Dityatev, A., & Schachner, M. (2006) · Cell and Tissue Research · doi:10.1007/s00441-006-0217-1 · Cited by 128
Sekine, K., Kubo, K.-I., & Nakajima, K. (2014) · Neuroscience Research · doi:10.1016/j.neures.2014.06.004 · Cited by 124
Blaze, J., Scheuing, L., & Roth, T. L. (2013) · Developmental Neuroscience · doi:10.1159/000350716 · Cited by 123
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Inhibition of the canonical Wnt signaling pathway by apolipoprotein E4 in PC12 cells
Caruso, A., Motolese, M., Iacovelli, L., Caraci, F., Copani, A., Nicoletti, F., Terstappen, G. C., Gaviraghi, G., & Caricasole, A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03867.x · Cited by 101
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Campo, C. G., Sinagra, M., Verrier, D., Manzoni, O. J., & Chavis, P. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005505 · Cited by 100
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Haas, C. A., & Frotscher, M. (2010) · Experimental Brain Research · doi:10.1007/s00221-009-1948-5 · Cited by 96
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Teixeira, C. M., Kron, M. M., Masachs, N., Zhang, H., Lagace, D. C., Martinez, A., Reillo, I., Duan, X., Bosch, C., Pujadas, L., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1857-12.2012 · Cited by 97
Similarities and differences in structure, expression, and functions of VLDLR and ApoER2
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Herring, A., Donath, A., Steiner, K. M., Widera, M. P., Hamzehian, S., Kanakis, D., Kölble, K., ElAli, A., Hermann, D. M., Paulus, W., et al. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-112069 · Cited by 92
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Reelin-mediated signaling in neuropsychiatric and neurodegenerative diseases
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Nakano, Y., Kohno, T., Hibi, T., Kohno, S., Baba, A., Mikoshiba, K., Nakajima, K., & Hattori, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702300200 · Cited by 86
Leemhuis, J., Bouché, E., Frotscher, M., Henle, F., Hein, L., Herz, J., Meyer, D. K., Pichler, M., Roth, G., Schwan, C., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4036-10.2010 · Cited by 80
Identification of Tbr-1/CASK complex target genes in neurons
Wang, T., Ding, C., Wang, G., Luo, S., Lin, Y., Ruan, Y., Hevner, R., Rubenstein, J. L. R., & Hsueh, Y. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02845.x · Cited by 83
Kofink, D., Boks, M. P. M., Timmers, H. T. M., & Kas, M. J. (2013) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2013.03.020 · Cited by 83
Reelin-deficient mice show impaired neurogenesis and increased stroke size
Won, S. J., Kim, S. H., Xie, L., Wang, Y., Mao, X. O., Jin, K., & Greenberg, D. A. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2005.12.008 · Cited by 84
Inoue, T., Ogawa, M., Mikoshiba, K., & Aruga, J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.5735-07.2008 · Cited by 76
Cellular and Molecular Mechanisms Linking Human Cortical Development and Evolution
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Simó, S., Jossin, Y., & Cooper, J. A. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.0035-10.2010 · Cited by 72
Duit, S., Mayer, H., Blake, S. M., Schneider, W. J., & Nimpf, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.025973 · Cited by 71
The multifaceted roles of primary cilia in the development of the cerebral cortex
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Polymorphic GGC repeat differentially regulates human reelin gene expression levels
Persico, A. M., Levitt, P., & Pimenta, A. F. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0441-6 · Cited by 52
Blaze, J., Asok, A., & Roth, T. L. (2015) · Stress · doi:10.3109/10253890.2015.1071790 · Cited by 52
Meta-analyses of RELN variants in neuropsychiatric disorders
Chen, N., Bao, Y., Xue, Y., Sun, Y., Hu, D., Meng, S., Lu, L., & Shi, J. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.05.028 · Cited by 44
TIMP-1 inhibits the proteolytic processing of Reelin in experimental epilepsy
Tinnes, S., Ringwald, J., & Haas, C. A. (2013) · The FASEB Journal · doi:10.1096/fj.12-224899 · Cited by 39
Brosda, J., Dietz, F., & Koch, M. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.07.008 · Cited by 37
Reelin proteolysis affects signaling related to normal synapse function and neurodegeneration
Lussier, A. L., Weeber, E. J., & Rebeck, G. W. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00075 · Cited by 31
Gärtner, A., Fornasiero, E. F., Valtorta, F., & Dotti, C. G. (2014) · Journal of Cell Science · doi:10.1242/jcs.149815 · Cited by 27
Orcinha, C., Münzner, G., Gerlach, J., Kilias, A., Follo, M., Egert, U., & Haas, C. A. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00183 · Cited by 26
Wang, S., Brunne, B., Zhao, S., Chai, X., Li, J., Lau, J., Failla, A. V., Zobiak, B., Sibbe, M., Westbrook, G. L., et al. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.0988-17.2017 · Cited by 26
Do, H. T., Bruelle, C., Tselykh, T., Jalonen, P., Korhonen, L., & Lindholm, D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.500967 · Cited by 20
Chen, Q., Takahashi, Y., Oka, K., & Ma, J.-X. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00235-16 · Cited by 17
Possamai-Della, T., Cararo, J. H., Aguiar-Geraldo, J. M., Peper-Nascimento, J., Zugno, A. I., Fries, G. R., Quevedo, J., & Valvassori, S. S. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03348-1 · Cited by 16
Glutamatergic cerebellar granule neurons synthesize and secrete reelin in vitro
Sinagra, M., Gonzalez Campo, C., Verrier, D., Moustié, O., Manzoni, O. J., & Chavis, P. (2008) · Neuron Glia Biology · doi:10.1017/s1740925x09990214 · Cited by 15
Area Patterning of the Mammalian Cortex
O'Leary, D. D. M., Stocker, A. M., & Zembrzycki, A. (2013) · Patterning and Cell Type Specification in the Developing CNS and PNS · doi:10.1016/b978-0-12-397265-1.00021-6 · Cited by 14
The potential role of cyclin-dependent kinase 5 in focal cortical dysplasia.
Sen, A., Thom, M., Nikolić, M., & Sisodiya, S. M. (2008) · Developmental Neuroscience · doi:10.1159/000109855 · Cited by 10
Cavusoglu, D., Ozturk, G., Turkdogan, D., Kurul, S. H., Yis, U., Komur, M., Incecik, F., Kara, B., Sahin, T., Unver, O., et al. (2024) · The Cerebellum · doi:10.1007/s12311-024-01690-1 · Cited by 8
Metadata
- Authors
- Tissir, F., & Goffinet, A. M.
- Venue
- Nature Reviews Neuroscience
- Published
- 2003-06-01
- Volume
- 4
- Issue
- 6
- Pages
- 496-505
- ISSN
- 1471-003X (ISSN-L)
- 1471-0048
- OpenAlex
- W2062087581
- Cited by
- 751
- References
- 19
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- www.springer.com/tdm (vor)
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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.
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.