1. Südhof T.C. Neuroligins and neurexins link synaptic function to cognitive disease. Nature. 2008;455(7215):903–911. [PMC free article] [PubMed] [Google Scholar]
2. Poo M.M., Pignatelli M., Ryan T.J., et al. What is memory? The present state of the engram. BMC Biol. 2016;14:40. [PMC free article] [PubMed] [Google Scholar]
3. Peineau S., Rabiant K., Pierrefiche O., Potier B. Synaptic plasticity modulation by circulating peptides and metaplasticity: involvement in Alzheimer's disease. Pharmacol Res. 2018;130:385–401. [PubMed] [Google Scholar]
4. Chih B., Engelman H., Scheiffele P. Control of excitatory and inhibitory synapse formation by neuroligins. Science. 2005;307(5713):1324–1328. [PubMed] [Google Scholar]
5. Missaire M., Hindges R. The role of cell adhesion molecules in visual circuit formation: from neurite outgrowth to maps and synaptic specificity. Dev Neurobiol. 2015;75(6):569–583. [PMC free article] [PubMed] [Google Scholar]
6. Dong Z., Han H., Li H., et al. Long-term potentiation decay and memory loss are mediated by AMPAR endocytosis. J Clin Invest. 2015;125(1):234–247. [PMC free article] [PubMed] [Google Scholar]
7. Tabuchi K., Südhof T.C. Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing. Genomics. 2002;79(6):849–859. [PubMed] [Google Scholar]
8. Harkin L.F., Lindsay S.J., Xu Y., et al. Neurexins 1-3 each have a distinct pattern of expression in the early developing human cerebral cortex. Cerebr Cortex. 2017;27(1):216–232. [PMC free article] [PubMed] [Google Scholar]
9. Ushkaryov Y.A., Petrenko A.G., Geppert M., Südhof T.C. Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin. Science. 1992;257(5066):50–56. [PubMed] [Google Scholar]
10. Occhi G., Rampazzo A., Beffa*gna G., Antonio Danieli G. Identification and characterization of heart-specific splicing of human neurexin 3 mRNA (NRXN3) Biochem Biophys Res Commun. 2002;298(1):151–155. [PubMed] [Google Scholar]
11. Ullrich B., Ushkaryov Y.A., Südhof T.C. Cartography of neurexins: more than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons. Neuron. 1995;14(3):497–507. [PubMed] [Google Scholar]
12. Bang M.L., Owczarek S. A matter of balance: role of neurexin and neuroligin at the synapse. Neurochem Res. 2013;38(6):1174–1189. [PubMed] [Google Scholar]
13. Sindi I.A., Tannenberg R.K., Dodd P.R. Role for the neurexin-neuroligin complex in Alzheimer's disease. Neurobiol Aging. 2014;35(4):746–756. [PubMed] [Google Scholar]
14. Ushkaryov Y.A., Südhof T.C. Neurexin III alpha: extensive alternative splicing generates membrane-bound and soluble forms. Proc Natl Acad Sci U S A. 1993;90(14):6410–6414. [PMC free article] [PubMed] [Google Scholar]
15. Sons M.S., Busche N., Strenzke N., et al. alpha-Neurexins are required for efficient transmitter release and synaptic homeostasis at the mouse neuromuscular junction. Neuroscience. 2006;138(2):433–446. [PubMed] [Google Scholar]
16. Bartels M.F., Winterhalter P.R., Yu J., et al. Protein O-mannosylation in the murine brain: occurrence of mono-O-mannosyl glycans and identification of new substrates. PLoS One. 2016;11(11):e0166119. [PMC free article] [PubMed] [Google Scholar]
17. Pandey H., Bourahmoune K., Honda T., et al. Genetic interaction of DISC1 and Neurexin in the development of fruit fly glutamatergic synapses. NPJ Schizophr. 2017;3(1):39. [PMC free article] [PubMed] [Google Scholar]
18. Banerjee S., Riordan M. Coordinated regulation of axonal microtubule organization and transport by Drosophila neurexin and BMP pathway. Sci Rep. 2018;8(1):17337. [PMC free article] [PubMed] [Google Scholar]
19. Craig A.M., Kang Y. Neurexin-neuroligin signaling in synapse development. Curr Opin Neurobiol. 2007;17(1):43–52. [PMC free article] [PubMed] [Google Scholar]
20. Roppongi R.T., Karimi B., Siddiqui T.J. Role of LRRTMs in synapse development and plasticity. Neurosci Res. 2017;116:18–28. [PubMed] [Google Scholar]
21. Gomez A.M., Traunmuller L., Scheiffele P. Neurexins: molecular codes for shaping neuronal synapses. Nat Rev Neurosci. 2021;22(3):137–151. [PMC free article] [PubMed] [Google Scholar]
22. Graf E.R., Zhang X., Jin S.X., Linhoff M.W., Craig A.M. Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Cell. 2004;119(7):1013–1026. [PMC free article] [PubMed] [Google Scholar]
23. Karki S., Maksimainen M.M., Lehtiö L., Kajander T. Inhibitor screening assay for neurexin-LRRTM adhesion protein interaction involved in synaptic maintenance and neurological disorders. Anal Biochem. 2019;587:113463. [PubMed] [Google Scholar]
24. Liouta K., Chabbert J., Benquet S., et al. Role of regulatory C-terminal motifs in synaptic confinement of LRRTM2. Biol Cell. 2021;113(12):492–506. [PubMed] [Google Scholar]
25. Ko J., Fuccillo M.V., Malenka R.C., Südhof T.C. LRRTM2 functions as a neurexin ligand in promoting excitatory synapse formation. Neuron. 2009;64(6):791–798. [PMC free article] [PubMed] [Google Scholar]
26. Minatohara K., Murata Y., Fujiyoshi Y., Doi T. An intracellular domain with a novel sequence regulates cell surface expression and synaptic clustering of leucine-rich repeat transmembrane proteins in hippocampal neurons. J Neurochem. 2015;134(4):618–628. [PubMed] [Google Scholar]
27. Linhoff M.W., Laurén J., Cassidy R.M., et al. An unbiased expression screen for synaptogenic proteins identifies the LRRTM protein family as synaptic organizers. Neuron. 2009;61(5):734–749. [PMC free article] [PubMed] [Google Scholar]
28. Siddiqui T.J., Pancaroglu R., Kang Y., Rooyakkers A., Craig A.M. LRRTMs and neuroligins bind neurexins with a differential code to cooperate in glutamate synapse development. J Neurosci. 2010;30(22):7495–7506. [PMC free article] [PubMed] [Google Scholar]
29. Siddiqui T.J., Tari P.K., Connor S.A., et al. An LRRTM4-HSPG complex mediates excitatory synapse development on dentate gyrus granule cells. Neuron. 2013;79(4):680–695. [PubMed] [Google Scholar]
30. Soler-Llavina G.J., Arstikaitis P., Morish*ta W., Ahmad M., Südhof T.C., Malenka R.C. Leucine-rich repeat transmembrane proteins are essential for maintenance of long-term potentiation. Neuron. 2013;79(3):439–446. [PMC free article] [PubMed] [Google Scholar]
31. Um J.W., Choi T.Y., Kang H., et al. LRRTM3 regulates excitatory synapse development through alternative splicing and neurexin binding. Cell Rep. 2016;14(4):808–822. [PubMed] [Google Scholar]
32. Ludwig K.U., Mattheisen M., Mühleisen T.W., et al. Supporting evidence for LRRTM1 imprinting effects in schizophrenia. Mol Psychiatr. 2009;14(8):743–745. [PubMed] [Google Scholar]
33. Malhotra D., McCarthy S., Michaelson J.J., et al. High frequencies of de novo CNVs in bipolar disorder and schizophrenia. Neuron. 2011;72(6):951–963. [PMC free article] [PubMed] [Google Scholar]
34. Cuttler K., Hassan M., Carr J., Cloete R., Bardien S. Emerging evidence implicating a role for neurexins in neurodegenerative and neuropsychiatric disorders. Open Biol. 2021;11(10):210091. [PMC free article] [PubMed] [Google Scholar]
35. Soler-Llavina G.J., Fuccillo M.V., Ko J., Südhof T.C., Malenka R.C. The neurexin ligands, neuroligins and leucine-rich repeat transmembrane proteins, perform convergent and divergent synaptic functions invivo. Proc Natl Acad Sci U S A. 2011;108(40):16502–16509. [PMC free article] [PubMed] [Google Scholar]
36. Ko J., Soler-Llavina G.J., Fuccillo M.V., Malenka R.C., Südhof T.C. Neuroligins/LRRTMs prevent activity- and Ca2+/calmodulin-dependent synapse elimination in cultured neurons. J Cell Biol. 2011;194(2):323–334. [PMC free article] [PubMed] [Google Scholar]
37. Dagar S., Gottmann K. Differential properties of the synaptogenic activities of the neurexin ligands Neuroligin1 and LRRTM2. Front Mol Neurosci. 2019;12:269. [PMC free article] [PubMed] [Google Scholar]
38. Südhof T.C. Synaptic neurexin complexes: a molecular code for the logic of neural circuits. Cell. 2017;171(4):745–769. [PMC free article] [PubMed] [Google Scholar]
39. Nguyen T., Südhof T.C. Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules. J Biol Chem. 1997;272(41):26032–26039. [PubMed] [Google Scholar]
40. Ichtchenko K., Nguyen T., Südhof T.C. Structures, alternative splicing, and neurexin binding of multiple neuroligins. J Biol Chem. 1996;271(5):2676–2682. [PubMed] [Google Scholar]
41. Ylisaukko-oja T., Rehnström K., Auranen M., et al. Analysis of four neuroligin genes as candidates for autism. Eur J Hum Genet. 2005;13(12):1285–1292. [PubMed] [Google Scholar]
42. Song J.Y., Ichtchenko K., Südhof T.C., Brose N. Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses. Proc Natl Acad Sci U S A. 1999;96(3):1100–1105. [PMC free article] [PubMed] [Google Scholar]
43. Poulopoulos A., Aramuni G., Meyer G., et al. Neuroligin 2 drives postsynaptic assembly at perisomatic inhibitory synapses through gephyrin and collybistin. Neuron. 2009;63(5):628–642. [PubMed] [Google Scholar]
44. Takács V.T., Freund T.F., Nyiri G. Neuroligin 2 is expressed in synapses established by cholinergic cells in the mouse brain. PLoS One. 2013;8(9):e72450. [PMC free article] [PubMed] [Google Scholar]
45. Uchigashima M., Ohtsuka T., Kobayashi K., Watanabe M. Dopamine synapse is a neuroligin-2-mediated contact between dopaminergic presynaptic and GABAergic postsynaptic structures. Proc Natl Acad Sci U S A. 2016;113(15):4206–4211. [PMC free article] [PubMed] [Google Scholar]
46. Uchigashima M., Cheung A., Futai K. Neuroligin-3: a circuit-specific synapse organizer that shapes normal function and autism spectrum disorder-associated dysfunction. Front Mol Neurosci. 2021;14:749164. [PMC free article] [PubMed] [Google Scholar]
47. Hoon M., Soykan T., Falkenburger B., et al. Neuroligin-4 is localized to glycinergic postsynapses and regulates inhibition in the retina. Proc Natl Acad Sci U S A. 2011;108(7):3053–3058. [PMC free article] [PubMed] [Google Scholar]
48. Bolliger M.F., Frei K., Winterhalter K.H., Gloor S.M. Identification of a novel neuroligin in humans which binds to PSD-95 and has a widespread expression. Biochem J. 2001;356(Pt 2):581–588. [PMC free article] [PubMed] [Google Scholar]
49. Varoqueaux F., Jamain S., Brose N. Neuroligin 2 is exclusively localized to inhibitory synapses. Eur J Cell Biol. 2004;83(9):449–456. [PubMed] [Google Scholar]
50. Chubykin A.A., Atasoy D., Etherton M.R., et al. Activity-dependent validation of excitatory versus inhibitory synapses by neuroligin-1 versus neuroligin-2. Neuron. 2007;54(6):919–931. [PMC free article] [PubMed] [Google Scholar]
51. Chanda S., Hale W.D., Zhang B., Wernig M., Südhof T.C. Unique versus redundant functions of neuroligin genes in shaping excitatory and inhibitory synapse properties. J Neurosci. 2017;37(29):6816–6836. [PMC free article] [PubMed] [Google Scholar]
52. Jiang M., Polepalli J., Chen L.Y., Zhang B., Südhof T.C., Malenka R.C. Conditional ablation of neuroligin-1 in CA1 pyramidal neurons blocks LTP by a cell-autonomous NMDA receptor-independent mechanism. Mol Psychiatr. 2017;22(3):375–383. [PMC free article] [PubMed] [Google Scholar]
53. Hines R.M., Wu L., Hines D.J., et al. Synaptic imbalance, stereotypies, and impaired social interactions in mice with altered neuroligin 2 expression. J Neurosci. 2008;28(24):6055–6067. [PMC free article] [PubMed] [Google Scholar]
54. Zhang B., Chen L.Y., Liu X., et al. Neuroligins sculpt cerebellar Purkinje-cell circuits by differential control of distinct classes of synapses. Neuron. 2015;87(4):781–796. [PMC free article] [PubMed] [Google Scholar]
55. Aoto J., Martinelli D.C., Malenka R.C., Tabuchi K., Südhof T.C. Presynaptic neurexin-3 alternative splicing trans-synaptically controls postsynaptic AMPA receptor trafficking. Cell. 2013;154(1):75–88. [PMC free article] [PubMed] [Google Scholar]
56. Aoto J., Földy C., Ilcus S.M., Tabuchi K., Südhof T.C. Distinct circuit-dependent functions of presynaptic neurexin-3 at GABAergic and glutamatergic synapses. Nat Neurosci. 2015;18(7):997–1007. [PMC free article] [PubMed] [Google Scholar]
57. Nam C.I., Chen L. Postsynaptic assembly induced by neurexin-neuroligin interaction and neurotransmitter. Proc Natl Acad Sci U S A. 2005;102(17):6137–6142. [PMC free article] [PubMed] [Google Scholar]
58. Hollmann M., Maron C., Heinemann S. N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron. 1994;13(6):1331–1343. [PubMed] [Google Scholar]
59. Shepherd J.D., Huganir R.L. The cell biology of synaptic plasticity: AMPA receptor trafficking. Annu Rev Cell Dev Biol. 2007;23:613–643. [PubMed] [Google Scholar]
60. Bassani S., Folci A., Zapata J., Passafaro M. AMPAR trafficking in synapse maturation and plasticity. Cell Mol Life Sci. 2013;70(23):4411–4430. [PMC free article] [PubMed] [Google Scholar]
61. Ashby M.C., De La Rue S.A., Ralph G.S., Uney J., Collingridge G.L., Henley J.M. Removal of AMPA receptors (AMPARs) from synapses is preceded by transient endocytosis of extrasynaptic AMPARs. J Neurosci. 2004;24(22):5172–5176. [PMC free article] [PubMed] [Google Scholar]
62. Kakegawa W., Katoh A., Narumi S., et al. Optogenetic control of synaptic AMPA receptor endocytosis reveals roles of LTD in motor learning. Neuron. 2018;99(5):985–998. [PubMed] [Google Scholar]
63. Awasthi A., Ramachandran B., Ahmed S., et al. Synaptotagmin-3 drives AMPA receptor endocytosis, depression of synapse strength, and forgetting. Science. 2019;363(6422):eaav1483. [PubMed] [Google Scholar]
64. Teravskis P.J., Covelo A., Miller E.C., et al. A53T mutant alpha-synuclein induces tau-dependent postsynaptic impairment independently of neurodegenerative changes. J Neurosci. 2018;38(45):9754–9767. [PMC free article] [PubMed] [Google Scholar]
65. Boucard A.A., Chubykin A.A., Comoletti D., Taylor P., Südhof T.C. A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha- and beta-neurexins. Neuron. 2005;48(2):229–236. [PubMed] [Google Scholar]
66. Irie M., Hata Y., Takeuchi M., et al. Binding of neuroligins to PSD-95. Science. 1997;277(5331):1511–1515. [PubMed] [Google Scholar]
67. Coley A.A., Gao W.J. PSD95: a synaptic protein implicated in schizophrenia or autism? Prog Neuro-Psychopharmacol Biol Psychiatry. 2018;82:187–194. [PMC free article] [PubMed] [Google Scholar]
68. Ichtchenko K., Hata Y., Nguyen T., et al. Neuroligin 1: a splice site-specific ligand for beta-neurexins. Cell. 1995;81(3):435–443. [PubMed] [Google Scholar]
69. Dai J., Aoto J., Südhof T.C. Alternative splicing of presynaptic neurexins differentially controls postsynaptic NMDA and AMPA receptor responses. Neuron. 2019;102(5):993–1008. [PMC free article] [PubMed] [Google Scholar]
70. Bormann J. ‘The ABC’ of GABA receptors. Trends Pharmacol Sci. 2000;21(1):16–19. [PubMed] [Google Scholar]
71. Wu X., Wu Z., Ning G., et al. γ-Aminobutyric acid type A (GABAA) receptor α subunits play a direct role in synaptic versus extrasynaptic targeting. J Biol Chem. 2012;287(33):27417–27430. [PMC free article] [PubMed] [Google Scholar]
72. Luscher B., Fuchs T., Kilpatrick C.L. GABAA receptor trafficking-mediated plasticity of inhibitory synapses. Neuron. 2011;70(3):385–409. [PMC free article] [PubMed] [Google Scholar]
73. Schmidt M.J., Mirnics K. Neurodevelopment, GABA system dysfunction, and schizophrenia. Neuropsychopharmacology. 2015;40(1):190–206. [PMC free article] [PubMed] [Google Scholar]
74. Kadoyama K., Matsuura K., Takano M., et al. Proteomic analysis involved with synaptic plasticity improvement by GABAA receptor blockade in hippocampus of a mouse model of Alzheimer's disease. Neurosci Res. 2021;165:61–68. [PubMed] [Google Scholar]
75. Ali H., Marth L., Krueger-Burg D. Neuroligin-2 as a central organizer of inhibitory synapses in health and disease. Sci Signal. 2020;13(663):eabd8379. [PubMed] [Google Scholar]
76. Kins S., Betz H., Kirsch J. Collybistin, a newly identified brain-specific GEF, induces submembrane clustering of gephyrin. Nat Neurosci. 2000;3(1):22–29. [PubMed] [Google Scholar]
77. Harvey K., Duguid I.C., Alldred M.J., et al. The GDP-GTP exchange factor collybistin: an essential determinant of neuronal gephyrin clustering. J Neurosci. 2004;24(25):5816–5826. [PMC free article] [PubMed] [Google Scholar]
78. Kalscheuer V.M., Musante L., Fang C., et al. A balanced chromosomal translocation disrupting ARHGEF9 is associated with epilepsy, anxiety, aggression, and mental retardation. Hum Mutat. 2009;30(1):61–68. [PMC free article] [PubMed] [Google Scholar]
79. Prior P., Schmitt B., Grenningloh G., et al. Primary structure and alternative splice variants of gephyrin, a putative glycine receptor-tubulin linker protein. Neuron. 1992;8(6):1161–1170. [PubMed] [Google Scholar]
80. Essrich C., Lorez M., Benson J.A., Fritschy J.M., Lüscher B. Postsynaptic clustering of major GABAA receptor subtypes requires the gamma 2 subunit and gephyrin. Nat Neurosci. 1998;1(7):563–571. [PubMed] [Google Scholar]
81. Feng G., Tintrup H., Kirsch J., et al. Dual requirement for gephyrin in glycine receptor clustering and molybdoenzyme activity. Science. 1998;282(5392):1321–1324. [PubMed] [Google Scholar]
82. Moss S.J., Smart T.G. Constructing inhibitory synapses. Nat Rev Neurosci. 2001;2(4):240–250. [PubMed] [Google Scholar]
83. Zhang C., Atasoy D., Araç D., et al. Neurexins physically and functionally interact with GABA(A) receptors. Neuron. 2010;66(3):403–416. [PMC free article] [PubMed] [Google Scholar]
84. Miyazaki T., Morimoto-Tomita M., Berthoux C., et al. Excitatory and inhibitory receptors utilize distinct post- and trans-synaptic mechanisms invivo. Elife. 2021;10:e59613. [PMC free article] [PubMed] [Google Scholar]
85. Hsueh Y.P. The role of the MAGUK protein CASK in neural development and synaptic function. Curr Med Chem. 2006;13(16):1915–1927. [PubMed] [Google Scholar]
86. Hata Y., Butz S., Südhof T.C. CASK: a novel dlg/PSD95 hom*olog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J Neurosci. 1996;16(8):2488–2494. [PMC free article] [PubMed] [Google Scholar]
87. Butz S., Okamoto M., Südhof T.C. A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Cell. 1998;94(6):773–782. [PubMed] [Google Scholar]
88. Biederer T., Südhof T.C. Mints as adaptors. Direct binding to neurexins and recruitment of munc18. J Biol Chem. 2000;275(51):39803–39806. [PubMed] [Google Scholar]
89. Seigneur E., Wang J., Dai J., Polepalli J., Südhof T.C. Cerebellin-2 regulates a serotonergic dorsal raphe circuit that controls compulsive behaviors. Mol Psychiatr. 2021;26(12):7509–7521. [PMC free article] [PubMed] [Google Scholar]
90. Dai J., Patzke C., Liakath-Ali K., Seigneur E., Südhof T.C. GluD1 is a signal transduction device disguised as an ionotropic receptor. Nature. 2021;595(7866):261–265. [PMC free article] [PubMed] [Google Scholar]
91. Monteiro P., Feng G. SHANK proteins: roles at the synapse and in autism spectrum disorder. Nat Rev Neurosci. 2017;18(3):147–157. [PubMed] [Google Scholar]
92. Roberts S., Delury C., Marsh E. The PDZ protein discs-large (DLG): the ‘Jekyll and Hyde' of the epithelial polarity proteins. FEBS J. 2012;279(19):3549–3558. [PubMed] [Google Scholar]
93. Anderson G.R., Aoto J., Tabuchi K., et al. β-Neurexins control neural circuits by regulating synaptic endocannabinoid signaling. Cell. 2015;162(3):593–606. [PMC free article] [PubMed] [Google Scholar]
94. Missler M., Zhang W., Rohlmann A., et al. Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis. Nature. 2003;423(6943):939–948. [PubMed] [Google Scholar]
95. Matsuda K., Budisantoso T., Mitakidis N., et al. Transsynaptic modulation of kainate receptor functions by C1q-like proteins. Neuron. 2016;90(4):752–767. [PubMed] [Google Scholar]
96. Luo F., Sclip A., Merrill S., Südhof T.C. Neurexins regulate presynaptic GABAB-receptors at central synapses. Nat Commun. 2021;12(1):2380. [PMC free article] [PubMed] [Google Scholar]
97. Celone K.A., Calhoun V.D., Dickerson B.C., et al. Alterations in memory networks in mild cognitive impairment and Alzheimer's disease: an independent component analysis. J Neurosci. 2006;26(40):10222–10231. [PMC free article] [PubMed] [Google Scholar]
98. Xu Y., Zhao M., Han Y., Zhang H. GABAergic inhibitory interneuron deficits in Alzheimer's disease: implications for treatment. Front Neurosci. 2020;14:660. [PMC free article] [PubMed] [Google Scholar]
99. Yu J., Cho E., Kwon H., et al. Akt and calcium-permeable AMPA receptor are involved in the effect of pinoresinol on amyloid beta-induced synaptic plasticity and memory deficits. Biochem Pharmacol. 2021;184:114366. [PubMed] [Google Scholar]
100. Perdahl E., Adolfsson R., Alafuzoff I., et al. Synapsin I (protein I) in different brain regions in senile dementia of Alzheimer type and in multi-infarct dementia. J Neural Transm. 1984;60(2):133–141. [PubMed] [Google Scholar]
101. Honer W.G., Dickson D.W., Gleeson J., Davies P. Regional synaptic pathology in Alzheimer's disease. Neurobiol Aging. 1992;13(3):375–382. [PubMed] [Google Scholar]
102. Bancher C., Braak H., Fischer P., Jellinger K.A. Neuropathological staging of Alzheimer lesions and intellectual status in Alzheimer's and Parkinson's disease patients. Neurosci Lett. 1993;162(1–2):179–182. [PubMed] [Google Scholar]
103. Sze C.I., Troncoso J.C., Kawas C., Mouton P., Price D.L., Martin L.J. Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease. J Neuropathol Exp Neurol. 1997;56(8):933–944. [PubMed] [Google Scholar]
104. Lassmann H., Weiler R., Fischer P., et al. Synaptic pathology in Alzheimer's disease: immunological data for markers of synaptic and large dense-core vesicles. Neuroscience. 1992;46(1):1–8. [PubMed] [Google Scholar]
105. Tannenberg R.K., Scott H.L., Tannenberg A.E., Dodd P.R. Selective loss of synaptic proteins in Alzheimer's disease: evidence for an increased severity with APOE varepsilon4. Neurochem Int. 2006;49(7):631–639. [PubMed] [Google Scholar]
106. Brinkmalm G., Sjödin S., Simonsen A.H., et al. A parallel reaction monitoring mass spectrometric method for analysis of potential CSF biomarkers for Alzheimer's disease. Proteonomics Clin Appl. 2018;12(1):e1700131. [PubMed] [Google Scholar]
107. Duits F.H., Brinkmalm G., Teunissen C.E., et al. Synaptic proteins in CSF as potential novel biomarkers for prognosis in prodromal Alzheimer's disease. Alzheimer's Res Ther. 2018;10(1):5. [PMC free article] [PubMed] [Google Scholar]
108. Lleó A., Núñez-Llaves R., Alcolea D., et al. Changes in synaptic proteins precede neurodegeneration markers in preclinical Alzheimer's disease cerebrospinal fluid. Mol Cell Proteomics. 2019;18(3):546–560. [PMC free article] [PubMed] [Google Scholar]
109. Dufort-Gervais J., Provost C., Charbonneau L., et al. Neuroligin-1 is altered in the hippocampus of Alzheimer's disease patients and mouse models, and modulates the toxicity of amyloid-beta oligomers. Sci Rep. 2020;10(1):6956. [PMC free article] [PubMed] [Google Scholar]
110. Bie B., Wu J., Yang H., Xu J.J., Brown D.L., Naguib M. Epigenetic suppression of neuroligin 1 underlies amyloid-induced memory deficiency. Nat Neurosci. 2014;17(2):223–231. [PubMed] [Google Scholar]
111. Martinez-Mir A., González-Pérez A., Gayán J., et al. Genetic study of neurexin and neuroligin genes in Alzheimer's disease. J Alzheim Dis. 2013;35(2):403–412. [PubMed] [Google Scholar]
112. Bot N., Schweizer C., Ben Halima S., Fraering P.C. Processing of the synaptic cell adhesion molecule neurexin-3beta by Alzheimer disease alpha- and gamma-secretases. J Biol Chem. 2011;286(4):2762–2773. [PMC free article] [PubMed] [Google Scholar]
113. Saura C.A., Servián-Morilla E., Scholl F.G. Presenilin/γ-secretase regulates neurexin processing at synapses. PLoS One. 2011;6(4):e19430. [PMC free article] [PubMed] [Google Scholar]
114. Nestler E.J. Is there a common molecular pathway for addiction? Nat Neurosci. 2005;8(11):1445–1449. [PubMed] [Google Scholar]
115. Liu Q.R., Drgon T., Johnson C., Walther D., Hess J., Uhl G.R. Addiction molecular genetics: 639,401 SNP whole genome association identifies many "cell adhesion" genes. Am J Med Genet B Neuropsychiatr Genet. 2006;141B(8):918–925. [PubMed] [Google Scholar]
116. Liu Q.R., Drgon T., Walther D., et al. Pooled association genome scanning: validation and use to identify addiction vulnerability loci in two samples. Proc Natl Acad Sci U S A. 2005;102(33):11864–11869. [PMC free article] [PubMed] [Google Scholar]
117. Novak G., Boukhadra J., Shaikh S.A., Kennedy J.L., Le Foll B. Association of a polymorphism in the NRXN3 gene with the degree of smoking in schizophrenia: a preliminary study. World J Biol Psychiatr. 2009;10(4 Pt 3):929–935. [PubMed] [Google Scholar]
118. Sasabe T., Ishiura S. Alcoholism and alternative splicing of candidate genes. Int J Environ Res Publ Health. 2010;7(4):1448–1466. [PMC free article] [PubMed] [Google Scholar]
119. Lein E.S., Hawrylycz M.J., Ao N., et al. Genome-wide atlas of gene expression in the adult mouse brain. Nature. 2007;445(7124):168–176. [PubMed] [Google Scholar]
120. Lachman H.M., Fann C.S., Bartzis M., et al. Genomewide suggestive linkage of opioid dependence to chromosome 14q. Hum Mol Genet. 2007;16(11):1327–1334. [PubMed] [Google Scholar]
121. Kelai S., Maussion G., Noble F., et al. Nrxn3 upregulation in the globus pallidus of mice developing cocaine addiction. Neuroreport. 2008;19(7):751–755. [PMC free article] [PubMed] [Google Scholar]
122. Wolock S.L., Yates A., Petrill S.A., et al. Gene x smoking interactions on human brain gene expression: finding common mechanisms in adolescents and adults. J Child Psychol Psychiatry. 2013;54(10):1109–1119. [PMC free article] [PubMed] [Google Scholar]
123. Güleç G., Coşan D.T., Şahin F.M., et al. Association of nicotine use disorder with Neurexin 3 gene polymorphisms. Türk Psikiyatri Derg. 2021;32(3):160–166. [PubMed] [Google Scholar]
124. Docampo E., Ribasés M., Gratacòs M., et al. Association of neurexin 3 polymorphisms with smoking behavior. Gene Brain Behav. 2012;11(6):704–711. [PubMed] [Google Scholar]
125. Charness M.E., Safran R.M., Perides G. Ethanol inhibits neural cell-cell adhesion. J Biol Chem. 1994;269(12):9304–9309. [PubMed] [Google Scholar]
126. Hishimoto A., Liu Q.R., Drgon T., et al. Neurexin 3 polymorphisms are associated with alcohol dependence and altered expression of specific isoforms. Hum Mol Genet. 2007;16(23):2880–2891. [PubMed] [Google Scholar]
127. Stoltenberg S.F., Lehmann M.K., Christ C.C., Hersrud S.L., Davies G.E. Associations among types of impulsivity, substance use problems and neurexin-3 polymorphisms. Drug Alcohol Depend. 2011;119(3):e31–e38. [PMC free article] [PubMed] [Google Scholar]
128. Autism Genome Project Consortium. Szatmari P., Paterson A.D., et al. Mapping autism risk loci using genetic linkage and chromosomal rearrangements. Nat Genet. 2007;39(3):319–328. [PMC free article] [PubMed] [Google Scholar]
129. Chakrabarti S., Fombonne E. Pervasive developmental disorders in preschool children: confirmation of high prevalence. Am J Psychiatr. 2005;162(6):1133–1141. [PubMed] [Google Scholar]
130. Vaags A.K., Lionel A.C., Sato D., et al. Rare deletions at the neurexin 3 locus in autism spectrum disorder. Am J Hum Genet. 2012;90(1):133–141. [PMC free article] [PubMed] [Google Scholar]
131. Yuan H., Wang Q., Liu Y., et al. A rare exonic NRXN3 deletion segregating with neurodevelopmental and neuropsychiatric conditions in a three-generation Chinese family. Am J Med Genet B Neuropsychiatr Genet. 2018;177(6):589–595. [PMC free article] [PubMed] [Google Scholar]
132. Hu X., Zhang J., Jin C., et al. Association study of NRXN3 polymorphisms with schizophrenia and risperidone-induced bodyweight gain in Chinese Han population. Prog Neuro-Psychopharmacol Biol Psychiatry. 2013;43:197–202. [PubMed] [Google Scholar]
133. Guedes B.F., Ribeiro A.F., Pinto L.F., et al. Potential autoimmune encephalitis following yellow fever vaccination: a report of three cases. J Neuroimmunol. 2021;355:577548. [PubMed] [Google Scholar]
134. Al Shweiki M.R., Oeckl P., Steinacker P., et al. Proteomic analysis reveals a biosignature of decreased synaptic protein in cerebrospinal fluid of major depressive disorder. Transl Psychiatry. 2020;10(1):144. [PMC free article] [PubMed] [Google Scholar]
135. Li W., Zhang Y., Gu R., et al. DNA pooling base genome-wide association study identifies variants at NRXN3 associated with delayed encephalopathy after acute carbon monoxide poisoning. PLoS One. 2013;8(11):e79159. [PMC free article] [PubMed] [Google Scholar]
136. Panagopoulos V.N., Trull T.J., Glowinski A.L., et al. Examining the association of NRXN3 SNPs with borderline personality disorder phenotypes in heroin dependent cases and socio-economically disadvantaged controls. Drug Alcohol Depend. 2013;128(3):187–193. [PMC free article] [PubMed] [Google Scholar]
137. Zarrilli F., Tomaiuolo R., Ceglia C., et al. Molecular analysis of cluster headache. Clin J Pain. 2015;31(1):52–57. [PubMed] [Google Scholar]
138. Marchese E., Valentini M., Di Sante G., et al. Alternative splicing of neurexins 1-3 is modulated by neuroinflammation in the prefrontal cortex of a murine model of multiple sclerosis. Exp Neurol. 2021;335:113497. [PubMed] [Google Scholar]
139. Liu L., Zhang P., Dong X., et al. Circ_0001367 inhibits glioma proliferation, migration and invasion by sponging miR-431 and thus regulating NRXN3. Cell Death Dis. 2021;12(6):536. [PMC free article] [PubMed] [Google Scholar]
140. Keum S., Kim A., Shin J.J., Kim J.H., Park J., Shin H.S. A missense variant at the Nrxn3 locus enhances empathy fear in the mouse. Neuron. 2018;98(3):588–601. [PubMed] [Google Scholar]
141. Sun H.B., Yokota H., Chi X.X., Xu Z.C. Differential expression of neurexin mRNA in CA1 and CA3 hippocampal neurons in response to ischemic insult. Brain Res Mol Brain Res. 2000;84(1–2):146–149. [PubMed] [Google Scholar]