Artigos de revistas sobre o tema "Synaptic adhesion proteins"
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Leshchyns’ka, Iryna, e Vladimir Sytnyk. "Synaptic Cell Adhesion Molecules in Alzheimer’s Disease". Neural Plasticity 2016 (2016): 1–9. http://dx.doi.org/10.1155/2016/6427537.
Texto completo da fonteZobel, K., S. E. Choi, R. Minakova, M. Gocyla e A. Offenhäusser. "N-Cadherin modified lipid bilayers promote neural network formation and circuitry". Soft Matter 13, n.º 44 (2017): 8096–107. http://dx.doi.org/10.1039/c7sm01214d.
Texto completo da fonteHayano, 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, n.º 29 (julho de 2021): eabf1600. http://dx.doi.org/10.1126/sciadv.abf1600.
Texto completo da fonteBrose, N. "Neuroligin-family synaptic adhesion proteins in autism spectrum disorders". European Neuropsychopharmacology 26 (outubro de 2016): S131. http://dx.doi.org/10.1016/s0924-977x(16)30913-0.
Texto completo da fonteStewart, Luke T. "Cell adhesion proteins and the pathogenesis of autism spectrum disorders". Journal of Neurophysiology 113, n.º 5 (1 de março de 2015): 1283–86. http://dx.doi.org/10.1152/jn.00780.2013.
Texto completo da fonteLee, Tet Woo, Vicky W. K. Tsang e 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, n.º 3 (agosto de 2008): 223–34. http://dx.doi.org/10.1017/s1740925x09990172.
Texto completo da fonteUchida, N., Y. Honjo, K. R. Johnson, M. J. Wheelock e M. Takeichi. "The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones." Journal of Cell Biology 135, n.º 3 (1 de novembro de 1996): 767–79. http://dx.doi.org/10.1083/jcb.135.3.767.
Texto completo da fonteOlsen, Olav, Kimberly A. Moore, Masaki Fukata, Toshinari Kazuta, Jonathan C. Trinidad, Fred W. Kauer, Michel Streuli et al. "Neurotransmitter release regulated by a MALS–liprin-α presynaptic complex". Journal of Cell Biology 170, n.º 7 (26 de setembro de 2005): 1127–34. http://dx.doi.org/10.1083/jcb.200503011.
Texto completo da fonteCostain, Willard J., Ingrid Rasquinha, Jagdeep K. Sandhu, Peter Rippstein, Bogdan Zurakowski, Jacqueline Slinn, John P. MacManus e Danica B. Stanimirovic. "Cerebral Ischemia Causes Dysregulation of Synaptic Adhesion in Mouse Synaptosomes". Journal of Cerebral Blood Flow & Metabolism 28, n.º 1 (16 de maio de 2007): 99–110. http://dx.doi.org/10.1038/sj.jcbfm.9600510.
Texto completo da fonteRibic, Adema, e Thomas Biederer. "Emerging Roles of Synapse Organizers in the Regulation of Critical Periods". Neural Plasticity 2019 (3 de setembro de 2019): 1–9. http://dx.doi.org/10.1155/2019/1538137.
Texto completo da fonteKohsaka, Hiroshi, Etsuko Takasu e Akinao Nose. "In vivo induction of postsynaptic molecular assembly by the cell adhesion molecule Fasciclin2". Journal of Cell Biology 179, n.º 6 (10 de dezembro de 2007): 1289–300. http://dx.doi.org/10.1083/jcb.200705154.
Texto completo da fonteSmith, Ireland R., Emily L. Hendricks, Nina K. Latcheva, Daniel R. Marenda e 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, n.º 5 (6 de março de 2024): 3074. http://dx.doi.org/10.3390/ijms25053074.
Texto completo da fonteMah, W., J. Ko, J. Nam, K. Han, W. S. Chung e E. Kim. "Selected SALM (Synaptic Adhesion-Like Molecule) Family Proteins Regulate Synapse Formation". Journal of Neuroscience 30, n.º 16 (21 de abril de 2010): 5559–68. http://dx.doi.org/10.1523/jneurosci.4839-09.2010.
Texto completo da fonteSchöpf, Clemens L., Cornelia Ablinger, Stefanie M. Geisler, Ruslan I. Stanika, Marta Campiglio, Walter A. Kaufmann, Benedikt Nimmervoll et al. "Presynaptic α2δ subunits are key organizers of glutamatergic synapses". Proceedings of the National Academy of Sciences 118, n.º 14 (29 de março de 2021): e1920827118. http://dx.doi.org/10.1073/pnas.1920827118.
Texto completo da fonteLin, Bin, Amy C. Arai, Gary Lynch e Christine M. Gall. "Integrins Regulate NMDA Receptor-Mediated Synaptic Currents". Journal of Neurophysiology 89, n.º 5 (1 de maio de 2003): 2874–78. http://dx.doi.org/10.1152/jn.00783.2002.
Texto completo da fonteBoll, Inga, Pia Jensen, Veit Schwämmle e Martin R. Larsen. "Depolarization-dependent Induction of Site-specific Changes in Sialylation on N-linked Glycoproteins in Rat Nerve Terminals". Molecular & Cellular Proteomics 19, n.º 9 (9 de junho de 2020): 1418–35. http://dx.doi.org/10.1074/mcp.ra119.001896.
Texto completo da fonteChamma, Ingrid, Florian Levet, Jean-Baptiste Sibarita, Matthieu Sainlos e Olivier Thoumine. "Nanoscale organization of synaptic adhesion proteins revealed by single-molecule localization microscopy". Neurophotonics 3, n.º 4 (3 de novembro de 2016): 041810. http://dx.doi.org/10.1117/1.nph.3.4.041810.
Texto completo da fonteHoner, W. G., P. Falkai, C. Young, T. Wang, J. Xie, J. Bonner, L. Hu, G. L. Boulianne, Z. Luo e W. S. Trimble. "Cingulate cortex synaptic terminal proteins and neural cell adhesion molecule in schizophrenia". Neuroscience 78, n.º 1 (fevereiro de 1997): 99–110. http://dx.doi.org/10.1016/s0306-4522(96)00489-7.
Texto completo da fonteBrose, N. "Synaptic Cell Adhesion Proteins and Synaptogenesis in the Mammalian Central Nervous System". Naturwissenschaften 86, n.º 11 (3 de novembro de 1999): 516–24. http://dx.doi.org/10.1007/s001140050666.
Texto completo da fonteTorres, Viviana I., Daniela Vallejo e 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.
Texto completo da fonteStachowicz, Katarzyna. "Physicochemical Principles of Adhesion Mechanisms in the Brain". International Journal of Molecular Sciences 24, n.º 6 (7 de março de 2023): 5070. http://dx.doi.org/10.3390/ijms24065070.
Texto completo da fonteBhouri, Mehdi, Wade Morishita, Paul Temkin, Debanjan Goswami, Hiroshi Kawabe, Nils Brose, Thomas C. Südhof, Ann Marie Craig, Tabrez J. Siddiqui e 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, n.º 23 (21 de maio de 2018): E5382—E5389. http://dx.doi.org/10.1073/pnas.1803280115.
Texto completo da fonteMitoma, Hiroshi, Jerome Honnorat, Kazuhiko Yamaguchi e Mario Manto. "Fundamental Mechanisms of Autoantibody-Induced Impairments on Ion Channels and Synapses in Immune-Mediated Cerebellar Ataxias". International Journal of Molecular Sciences 21, n.º 14 (13 de julho de 2020): 4936. http://dx.doi.org/10.3390/ijms21144936.
Texto completo da fontePehkonen, Henna, Ivan de Curtis e Outi Monni. "Liprins in oncogenic signaling and cancer cell adhesion". Oncogene 40, n.º 46 (15 de outubro de 2021): 6406–16. http://dx.doi.org/10.1038/s41388-021-02048-1.
Texto completo da fonteSandau, Ursula S., Alison E. Mungenast, Jack McCarthy, Thomas Biederer, Gabriel Corfas e 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, n.º 6 (12 de abril de 2011): 2353–63. http://dx.doi.org/10.1210/en.2010-1434.
Texto completo da fonteCijsouw, Tony, Austin Ramsey, TuKiet Lam, Beatrice Carbone, Thomas Blanpied e Thomas Biederer. "Mapping the Proteome of the Synaptic Cleft through Proximity Labeling Reveals New Cleft Proteins". Proteomes 6, n.º 4 (28 de novembro de 2018): 48. http://dx.doi.org/10.3390/proteomes6040048.
Texto completo da fonteHu, Xiaoge, Jian-hong Luo e 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.
Texto completo da fonteRamsey, Austin M., Ai-Hui Tang, Tara A. LeGates, Xu-Zhuo Gou, Beatrice E. Carbone, Scott M. Thompson, Thomas Biederer e Thomas A. Blanpied. "Subsynaptic positioning of AMPARs by LRRTM2 controls synaptic strength". Science Advances 7, n.º 34 (agosto de 2021): eabf3126. http://dx.doi.org/10.1126/sciadv.abf3126.
Texto completo da fonteLu, Cecilia S., Bo Zhai, Alex Mauss, Matthias Landgraf, Stephen Gygi e 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, n.º 1652 (26 de setembro de 2014): 20130517. http://dx.doi.org/10.1098/rstb.2013.0517.
Texto completo da fonteZambonino, Marjorie, e Pamela Pereira. "The structure of Neurexin 1α (n1α) and its role as synaptic organizer". Bionatura 4, n.º 2 (15 de maio de 2019): 883–86. http://dx.doi.org/10.21931/rb/2019.04.02.12.
Texto completo da fonteKreienkamp, H. J., M. Soltau, D. Richter e T. Böckers. "Interaction of G-protein-coupled receptors with synaptic scaffolding proteins". Biochemical Society Transactions 30, n.º 4 (1 de agosto de 2002): 464–68. http://dx.doi.org/10.1042/bst0300464.
Texto completo da fonteGoethe, Eric A., Benjamin Deneen, Jeffrey Noebels e Ganesh Rao. "The Role of Hyperexcitability in Gliomagenesis". International Journal of Molecular Sciences 24, n.º 1 (1 de janeiro de 2023): 749. http://dx.doi.org/10.3390/ijms24010749.
Texto completo da fonteKuhl, D., T. E. Kennedy, A. Barzilai e 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, n.º 5 (1 de dezembro de 1992): 1069–76. http://dx.doi.org/10.1083/jcb.119.5.1069.
Texto completo da fonteLoomis, Connor, Aliyah Stephens, Remi Janicot, Usman Baqai, Laura Drebushenko e Jennifer Round. "Identification of MAGUK scaffold proteins as intracellular binding partners of synaptic adhesion protein Slitrk2". Molecular and Cellular Neuroscience 103 (março de 2020): 103465. http://dx.doi.org/10.1016/j.mcn.2019.103465.
Texto completo da fonteFigiel, Izabela, Patrycja K. Kruk, Monika Zaręba-Kozioł, Paulina Rybak, Monika Bijata, Jakub Wlodarczyk e Joanna Dzwonek. "MMP-9 Signaling Pathways That Engage Rho GTPases in Brain Plasticity". Cells 10, n.º 1 (15 de janeiro de 2021): 166. http://dx.doi.org/10.3390/cells10010166.
Texto completo da fonteYang, Xiaojuan, e Wim Annaert. "The Nanoscopic Organization of Synapse Structures: A Common Basis for Cell Communication". Membranes 11, n.º 4 (30 de março de 2021): 248. http://dx.doi.org/10.3390/membranes11040248.
Texto completo da fonteBeumer, Kelly, Heinrich J. G. Matthies, Amber Bradshaw e Kendal Broadie. "Integrins regulate DLG/FAS2 via a CaM kinase II-dependent pathway to mediate synapse elaboration and stabilization during postembryonic development". Development 129, n.º 14 (15 de julho de 2002): 3381–91. http://dx.doi.org/10.1242/dev.129.14.3381.
Texto completo da fonteChen, Xiumin, Yuko Fukata, Masaki Fukata e Roger A. Nicoll. "MAGUKs are essential, but redundant, in long-term potentiation". Proceedings of the National Academy of Sciences 118, n.º 28 (9 de julho de 2021): e2107585118. http://dx.doi.org/10.1073/pnas.2107585118.
Texto completo da fonteSytnyk, Vladimir, Iryna Leshchyns'ka, Alexander G. Nikonenko e Melitta Schachner. "NCAM promotes assembly and activity-dependent remodeling of the postsynaptic signaling complex". Journal of Cell Biology 174, n.º 7 (21 de setembro de 2006): 1071–85. http://dx.doi.org/10.1083/jcb.200604145.
Texto completo da fonteYagishita-Kyo, Nan, Minami Harada, Tomoko Uekita, Kei Maruyama, Yuki Ikai, Chihiro Koshimoto e 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.
Texto completo da fonteTaylor, Sara C., Sarah L. Ferri, Mahip Grewal, Zoe Smernoff, Maja Bucan, Joshua A. Weiner, Ted Abel e Edward S. Brodkin. "The Role of Synaptic Cell Adhesion Molecules and Associated Scaffolding Proteins in Social Affiliative Behaviors". Biological Psychiatry 88, n.º 6 (setembro de 2020): 442–51. http://dx.doi.org/10.1016/j.biopsych.2020.02.012.
Texto completo da fonteAli, Heba, Lena Marth e Dilja Krueger-Burg. "Neuroligin-2 as a central organizer of inhibitory synapses in health and disease". Science Signaling 13, n.º 663 (22 de dezembro de 2020): eabd8379. http://dx.doi.org/10.1126/scisignal.abd8379.
Texto completo da fonteSchmerl, 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, n.º 3 (21 de março de 2022): e3001503. http://dx.doi.org/10.1371/journal.pbio.3001503.
Texto completo da fonteMuellerleile, Julia, Matej Vnencak, Mohammad Valeed Ahmed Sethi, Tassilo Jungenitz, Stephan W. Schwarzacher e Peter Jedlicka. "Increased Network Inhibition in the Dentate Gyrus of Adult Neuroligin-4 Knock-Out Mice". eneuro 10, n.º 4 (abril de 2023): ENEURO.0471–22.2023. http://dx.doi.org/10.1523/eneuro.0471-22.2023.
Texto completo da fonteHsueh, Yi-Ping, Fu-Chia Yang, Viktor Kharazia, Scott Naisbitt, Alexandra R. Cohen, Richard J. Weinberg e 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, n.º 1 (13 de julho de 1998): 139–51. http://dx.doi.org/10.1083/jcb.142.1.139.
Texto completo da fonteWright, John W., e 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.
Texto completo da fonteLievens, 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, n.º 17 (31 de maio de 2016): 2208–25. http://dx.doi.org/10.1128/mcb.00144-16.
Texto completo da fonteLevinson, Joshua N., e Alaa El-Husseini. "New Players Tip the Scales in the Balance between Excitatory and Inhibitory Synapses". Molecular Pain 1 (1 de janeiro de 2005): 1744–8069. http://dx.doi.org/10.1186/1744-8069-1-12.
Texto completo da fonteMizoguchi, Hiroyuki, Kiyofumi Yamada e 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.
Texto completo da fonteTakano, Tetsuya. "Comprehensive identification of molecules at synapses and non-synaptic cell-adhesion structure". Impact 2023, n.º 3 (21 de setembro de 2023): 46–48. http://dx.doi.org/10.21820/23987073.2023.3.46.
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