Статті в журналах з теми "Synaptic adhesion proteins"
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Leshchyns’ka, Iryna, and Vladimir Sytnyk. "Synaptic Cell Adhesion Molecules in Alzheimer’s Disease." Neural Plasticity 2016 (2016): 1–9. http://dx.doi.org/10.1155/2016/6427537.
Zobel, K., S. E. Choi, R. Minakova, M. Gocyla, and A. Offenhäusser. "N-Cadherin modified lipid bilayers promote neural network formation and circuitry." Soft Matter 13, no. 44 (2017): 8096–107. http://dx.doi.org/10.1039/c7sm01214d.
Hayano, Yasufumi, Yugo Ishino, Jung Ho Hyun, Carlos G. Orozco, André Steinecke, Elizabeth Potts, Yasuhiro Oisi, et al. "IgSF11 homophilic adhesion proteins promote layer-specific synaptic assembly of the cortical interneuron subtype." Science Advances 7, no. 29 (July 2021): eabf1600. http://dx.doi.org/10.1126/sciadv.abf1600.
Brose, N. "Neuroligin-family synaptic adhesion proteins in autism spectrum disorders." European Neuropsychopharmacology 26 (October 2016): S131. http://dx.doi.org/10.1016/s0924-977x(16)30913-0.
Stewart, Luke T. "Cell adhesion proteins and the pathogenesis of autism spectrum disorders." Journal of Neurophysiology 113, no. 5 (March 1, 2015): 1283–86. http://dx.doi.org/10.1152/jn.00780.2013.
Lee, Tet Woo, Vicky W. K. Tsang, and Nigel P. Birch. "Synaptic plasticity-associated proteases and protease inhibitors in the brain linked to the processing of extracellular matrix and cell adhesion molecules." Neuron Glia Biology 4, no. 3 (August 2008): 223–34. http://dx.doi.org/10.1017/s1740925x09990172.
Uchida, N., Y. Honjo, K. R. Johnson, M. J. Wheelock, and M. Takeichi. "The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones." Journal of Cell Biology 135, no. 3 (November 1, 1996): 767–79. http://dx.doi.org/10.1083/jcb.135.3.767.
Olsen, Olav, Kimberly A. Moore, Masaki Fukata, Toshinari Kazuta, Jonathan C. Trinidad, Fred W. Kauer, Michel Streuli та ін. "Neurotransmitter release regulated by a MALS–liprin-α presynaptic complex". Journal of Cell Biology 170, № 7 (26 вересня 2005): 1127–34. http://dx.doi.org/10.1083/jcb.200503011.
Costain, Willard J., Ingrid Rasquinha, Jagdeep K. Sandhu, Peter Rippstein, Bogdan Zurakowski, Jacqueline Slinn, John P. MacManus, and Danica B. Stanimirovic. "Cerebral Ischemia Causes Dysregulation of Synaptic Adhesion in Mouse Synaptosomes." Journal of Cerebral Blood Flow & Metabolism 28, no. 1 (May 16, 2007): 99–110. http://dx.doi.org/10.1038/sj.jcbfm.9600510.
Ribic, Adema, and Thomas Biederer. "Emerging Roles of Synapse Organizers in the Regulation of Critical Periods." Neural Plasticity 2019 (September 3, 2019): 1–9. http://dx.doi.org/10.1155/2019/1538137.
Kohsaka, Hiroshi, Etsuko Takasu, and Akinao Nose. "In vivo induction of postsynaptic molecular assembly by the cell adhesion molecule Fasciclin2." Journal of Cell Biology 179, no. 6 (December 10, 2007): 1289–300. http://dx.doi.org/10.1083/jcb.200705154.
Smith, Ireland R., Emily L. Hendricks, Nina K. Latcheva, Daniel R. Marenda, and Faith L. W. Liebl. "The CHD Protein Kismet Restricts the Synaptic Localization of Cell Adhesion Molecules at the Drosophila Neuromuscular Junction." International Journal of Molecular Sciences 25, no. 5 (March 6, 2024): 3074. http://dx.doi.org/10.3390/ijms25053074.
Mah, W., J. Ko, J. Nam, K. Han, W. S. Chung, and E. Kim. "Selected SALM (Synaptic Adhesion-Like Molecule) Family Proteins Regulate Synapse Formation." Journal of Neuroscience 30, no. 16 (April 21, 2010): 5559–68. http://dx.doi.org/10.1523/jneurosci.4839-09.2010.
Schöpf, Clemens L., Cornelia Ablinger, Stefanie M. Geisler, Ruslan I. Stanika, Marta Campiglio, Walter A. Kaufmann, Benedikt Nimmervoll та ін. "Presynaptic α2δ subunits are key organizers of glutamatergic synapses". Proceedings of the National Academy of Sciences 118, № 14 (29 березня 2021): e1920827118. http://dx.doi.org/10.1073/pnas.1920827118.
Lin, Bin, Amy C. Arai, Gary Lynch, and Christine M. Gall. "Integrins Regulate NMDA Receptor-Mediated Synaptic Currents." Journal of Neurophysiology 89, no. 5 (May 1, 2003): 2874–78. http://dx.doi.org/10.1152/jn.00783.2002.
Boll, Inga, Pia Jensen, Veit Schwämmle, and Martin R. Larsen. "Depolarization-dependent Induction of Site-specific Changes in Sialylation on N-linked Glycoproteins in Rat Nerve Terminals." Molecular & Cellular Proteomics 19, no. 9 (June 9, 2020): 1418–35. http://dx.doi.org/10.1074/mcp.ra119.001896.
Chamma, Ingrid, Florian Levet, Jean-Baptiste Sibarita, Matthieu Sainlos, and Olivier Thoumine. "Nanoscale organization of synaptic adhesion proteins revealed by single-molecule localization microscopy." Neurophotonics 3, no. 4 (November 3, 2016): 041810. http://dx.doi.org/10.1117/1.nph.3.4.041810.
Honer, W. G., P. Falkai, C. Young, T. Wang, J. Xie, J. Bonner, L. Hu, G. L. Boulianne, Z. Luo, and W. S. Trimble. "Cingulate cortex synaptic terminal proteins and neural cell adhesion molecule in schizophrenia." Neuroscience 78, no. 1 (February 1997): 99–110. http://dx.doi.org/10.1016/s0306-4522(96)00489-7.
Brose, N. "Synaptic Cell Adhesion Proteins and Synaptogenesis in the Mammalian Central Nervous System." Naturwissenschaften 86, no. 11 (November 3, 1999): 516–24. http://dx.doi.org/10.1007/s001140050666.
Torres, Viviana I., Daniela Vallejo, and Nibaldo C. Inestrosa. "Emerging Synaptic Molecules as Candidates in the Etiology of Neurological Disorders." Neural Plasticity 2017 (2017): 1–25. http://dx.doi.org/10.1155/2017/8081758.
Stachowicz, Katarzyna. "Physicochemical Principles of Adhesion Mechanisms in the Brain." International Journal of Molecular Sciences 24, no. 6 (March 7, 2023): 5070. http://dx.doi.org/10.3390/ijms24065070.
Bhouri, Mehdi, Wade Morishita, Paul Temkin, Debanjan Goswami, Hiroshi Kawabe, Nils Brose, Thomas C. Südhof, Ann Marie Craig, Tabrez J. Siddiqui, and Robert Malenka. "Deletion of LRRTM1 and LRRTM2 in adult mice impairs basal AMPA receptor transmission and LTP in hippocampal CA1 pyramidal neurons." Proceedings of the National Academy of Sciences 115, no. 23 (May 21, 2018): E5382—E5389. http://dx.doi.org/10.1073/pnas.1803280115.
Mitoma, Hiroshi, Jerome Honnorat, Kazuhiko Yamaguchi, and Mario Manto. "Fundamental Mechanisms of Autoantibody-Induced Impairments on Ion Channels and Synapses in Immune-Mediated Cerebellar Ataxias." International Journal of Molecular Sciences 21, no. 14 (July 13, 2020): 4936. http://dx.doi.org/10.3390/ijms21144936.
Pehkonen, Henna, Ivan de Curtis, and Outi Monni. "Liprins in oncogenic signaling and cancer cell adhesion." Oncogene 40, no. 46 (October 15, 2021): 6406–16. http://dx.doi.org/10.1038/s41388-021-02048-1.
Sandau, Ursula S., Alison E. Mungenast, Jack McCarthy, Thomas Biederer, Gabriel Corfas, and Sergio R. Ojeda. "The Synaptic Cell Adhesion Molecule, SynCAM1, Mediates Astrocyte-to-Astrocyte and Astrocyte-to-GnRH Neuron Adhesiveness in the Mouse Hypothalamus." Endocrinology 152, no. 6 (April 12, 2011): 2353–63. http://dx.doi.org/10.1210/en.2010-1434.
Cijsouw, Tony, Austin Ramsey, TuKiet Lam, Beatrice Carbone, Thomas Blanpied, and Thomas Biederer. "Mapping the Proteome of the Synaptic Cleft through Proximity Labeling Reveals New Cleft Proteins." Proteomes 6, no. 4 (November 28, 2018): 48. http://dx.doi.org/10.3390/proteomes6040048.
Hu, Xiaoge, Jian-hong Luo, and Junyu Xu. "The Interplay between Synaptic Activity and Neuroligin Function in the CNS." BioMed Research International 2015 (2015): 1–13. http://dx.doi.org/10.1155/2015/498957.
Ramsey, Austin M., Ai-Hui Tang, Tara A. LeGates, Xu-Zhuo Gou, Beatrice E. Carbone, Scott M. Thompson, Thomas Biederer, and Thomas A. Blanpied. "Subsynaptic positioning of AMPARs by LRRTM2 controls synaptic strength." Science Advances 7, no. 34 (August 2021): eabf3126. http://dx.doi.org/10.1126/sciadv.abf3126.
Lu, Cecilia S., Bo Zhai, Alex Mauss, Matthias Landgraf, Stephen Gygi, and David Van Vactor. "MicroRNA-8 promotes robust motor axon targeting by coordinate regulation of cell adhesion molecules during synapse development." Philosophical Transactions of the Royal Society B: Biological Sciences 369, no. 1652 (September 26, 2014): 20130517. http://dx.doi.org/10.1098/rstb.2013.0517.
Zambonino, Marjorie, та Pamela Pereira. "The structure of Neurexin 1α (n1α) and its role as synaptic organizer". Bionatura 4, № 2 (15 травня 2019): 883–86. http://dx.doi.org/10.21931/rb/2019.04.02.12.
Kreienkamp, H. J., M. Soltau, D. Richter, and T. Böckers. "Interaction of G-protein-coupled receptors with synaptic scaffolding proteins." Biochemical Society Transactions 30, no. 4 (August 1, 2002): 464–68. http://dx.doi.org/10.1042/bst0300464.
Goethe, Eric A., Benjamin Deneen, Jeffrey Noebels, and Ganesh Rao. "The Role of Hyperexcitability in Gliomagenesis." International Journal of Molecular Sciences 24, no. 1 (January 1, 2023): 749. http://dx.doi.org/10.3390/ijms24010749.
Kuhl, D., T. E. Kennedy, A. Barzilai, and E. R. Kandel. "Long-term sensitization training in Aplysia leads to an increase in the expression of BiP, the major protein chaperon of the ER." Journal of Cell Biology 119, no. 5 (December 1, 1992): 1069–76. http://dx.doi.org/10.1083/jcb.119.5.1069.
Loomis, Connor, Aliyah Stephens, Remi Janicot, Usman Baqai, Laura Drebushenko, and Jennifer Round. "Identification of MAGUK scaffold proteins as intracellular binding partners of synaptic adhesion protein Slitrk2." Molecular and Cellular Neuroscience 103 (March 2020): 103465. http://dx.doi.org/10.1016/j.mcn.2019.103465.
Figiel, Izabela, Patrycja K. Kruk, Monika Zaręba-Kozioł, Paulina Rybak, Monika Bijata, Jakub Wlodarczyk, and Joanna Dzwonek. "MMP-9 Signaling Pathways That Engage Rho GTPases in Brain Plasticity." Cells 10, no. 1 (January 15, 2021): 166. http://dx.doi.org/10.3390/cells10010166.
Yang, Xiaojuan, and Wim Annaert. "The Nanoscopic Organization of Synapse Structures: A Common Basis for Cell Communication." Membranes 11, no. 4 (March 30, 2021): 248. http://dx.doi.org/10.3390/membranes11040248.
Beumer, Kelly, Heinrich J. G. Matthies, Amber Bradshaw, and Kendal Broadie. "Integrins regulate DLG/FAS2 via a CaM kinase II-dependent pathway to mediate synapse elaboration and stabilization during postembryonic development." Development 129, no. 14 (July 15, 2002): 3381–91. http://dx.doi.org/10.1242/dev.129.14.3381.
Chen, Xiumin, Yuko Fukata, Masaki Fukata, and Roger A. Nicoll. "MAGUKs are essential, but redundant, in long-term potentiation." Proceedings of the National Academy of Sciences 118, no. 28 (July 9, 2021): e2107585118. http://dx.doi.org/10.1073/pnas.2107585118.
Sytnyk, Vladimir, Iryna Leshchyns'ka, Alexander G. Nikonenko, and Melitta Schachner. "NCAM promotes assembly and activity-dependent remodeling of the postsynaptic signaling complex." Journal of Cell Biology 174, no. 7 (September 21, 2006): 1071–85. http://dx.doi.org/10.1083/jcb.200604145.
Yagishita-Kyo, Nan, Minami Harada, Tomoko Uekita, Kei Maruyama, Yuki Ikai, Chihiro Koshimoto, and Sosuke Yagishita. "The effect of sex hormones on the interaction between synaptic adhesion proteins concerned with sociality." Proceedings for Annual Meeting of The Japanese Pharmacological Society 92 (2019): 2—P—003. http://dx.doi.org/10.1254/jpssuppl.92.0_2-p-003.
Taylor, Sara C., Sarah L. Ferri, Mahip Grewal, Zoe Smernoff, Maja Bucan, Joshua A. Weiner, Ted Abel, and Edward S. Brodkin. "The Role of Synaptic Cell Adhesion Molecules and Associated Scaffolding Proteins in Social Affiliative Behaviors." Biological Psychiatry 88, no. 6 (September 2020): 442–51. http://dx.doi.org/10.1016/j.biopsych.2020.02.012.
Ali, Heba, Lena Marth, and Dilja Krueger-Burg. "Neuroligin-2 as a central organizer of inhibitory synapses in health and disease." Science Signaling 13, no. 663 (December 22, 2020): eabd8379. http://dx.doi.org/10.1126/scisignal.abd8379.
Schmerl, Bettina, Niclas Gimber, Benno Kuropka, Alexander Stumpf, Jakob Rentsch, Stella-Amrei Kunde, Judith von Sivers, et al. "The synaptic scaffold protein MPP2 interacts with GABAA receptors at the periphery of the postsynaptic density of glutamatergic synapses." PLOS Biology 20, no. 3 (March 21, 2022): e3001503. http://dx.doi.org/10.1371/journal.pbio.3001503.
Muellerleile, Julia, Matej Vnencak, Mohammad Valeed Ahmed Sethi, Tassilo Jungenitz, Stephan W. Schwarzacher, and Peter Jedlicka. "Increased Network Inhibition in the Dentate Gyrus of Adult Neuroligin-4 Knock-Out Mice." eneuro 10, no. 4 (April 2023): ENEURO.0471–22.2023. http://dx.doi.org/10.1523/eneuro.0471-22.2023.
Hsueh, Yi-Ping, Fu-Chia Yang, Viktor Kharazia, Scott Naisbitt, Alexandra R. Cohen, Richard J. Weinberg, and Morgan Sheng. "Direct Interaction of CASK/LIN-2 and Syndecan Heparan Sulfate Proteoglycan and Their Overlapping Distribution in Neuronal Synapses." Journal of Cell Biology 142, no. 1 (July 13, 1998): 139–51. http://dx.doi.org/10.1083/jcb.142.1.139.
Wright, John W., and Joseph W. Harding. "Contributions of Matrix Metalloproteinases to Neural Plasticity, Habituation, Associative Learning and Drug Addiction." Neural Plasticity 2009 (2009): 1–12. http://dx.doi.org/10.1155/2009/579382.
Lievens, Patricia Marie-Jeanne, Tatiana Kuznetsova, Gaga Kochlamazashvili, Fabrizia Cesca, Natalya Gorinski, Dalia Abdel Galil, Volodimir Cherkas, et al. "ZDHHC3 Tyrosine Phosphorylation Regulates Neural Cell Adhesion Molecule Palmitoylation." Molecular and Cellular Biology 36, no. 17 (May 31, 2016): 2208–25. http://dx.doi.org/10.1128/mcb.00144-16.
Levinson, Joshua N., and Alaa El-Husseini. "New Players Tip the Scales in the Balance between Excitatory and Inhibitory Synapses." Molecular Pain 1 (January 1, 2005): 1744–8069. http://dx.doi.org/10.1186/1744-8069-1-12.
Mizoguchi, Hiroyuki, Kiyofumi Yamada, and Toshitaka Nabeshima. "Matrix Metalloproteinases Contribute to Neuronal Dysfunction in Animal Models of Drug Dependence, Alzheimer's Disease, and Epilepsy." Biochemistry Research International 2011 (2011): 1–10. http://dx.doi.org/10.1155/2011/681385.
Takano, Tetsuya. "Comprehensive identification of molecules at synapses and non-synaptic cell-adhesion structure." Impact 2023, no. 3 (September 21, 2023): 46–48. http://dx.doi.org/10.21820/23987073.2023.3.46.