Browsing by Titles

Showing results 1 to 5 of 5

  • Kim, Hyeonho
  • Jeon, Younghyeon
  • Kim, Seunghye
  • Guo, Yuxuan
  • Kim, Dongwook
  • Jang, Gyubin
  • Brasch, Julia
  • Um, Ji Won
  • Ko, Jaewon
  • 2025-07
  • Kim, Hyeonho. (2025-07). EphB2 receptor tyrosine kinase-mediated excitatory synaptic functions are negatively modulated by MDGA2. Progress in Neurobiology, 250. doi: 10.1016/j.pneurobio.2025.102772
  • Elsevier
  • View : 338
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  • Han, Kyung Ah
  • Kim, YJ
  • Yoon, Taek Han
  • Kim, Hyeonho
  • Bae, Sungwon
  • Um, Ji Won
  • Choi, SY
  • Ko, Jaewon
  • 2020-10
  • Han, Kyung Ah. (2020-10). LAR-RPTPs Directly Interact with Neurexins to Coordinate Bidirectional Assembly of Molecular Machineries. doi: 10.1523/JNEUROSCI.1091-20.2020
  • Society for Neuroscience
  • View : 864
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  • Kim, Jinhu
  • Park, Dongseok
  • Seo, Na-Young
  • Yoon, Taek Han
  • Kim, Gyu Hyun
  • Lee, Sang-Hoon
  • Seo, Jinsoo
  • Um, Ji Won
  • Lee, Kea Joo
  • Ko, Jaewon
  • 2022-01
  • Kim, Jinhu. (2022-01). LRRTM3 regulates activity-dependent synchronization of synapse properties in topographically connected hippocampal neural circuits. doi: 10.1073/pnas.2110196119
  • National Academy of Sciences
  • View : 861
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SALM4 negatively regulates NMDA receptor function and fear memory consolidation

  • Lie, Eunkyung
  • Yeo, Yeji
  • Lee, Eun-Jae
  • Shin, Wangyong
  • Kim, Kyungdeok
  • Han, Kyung Ah
  • Yang, Esther
  • Choi, Tae-Yong
  • Bae, Mihyun
  • Lee, Suho
  • et al
  • 2021-09
  • Lie, Eunkyung. (2021-09). SALM4 negatively regulates NMDA receptor function and fear memory consolidation. Communications Biology, 4(1), 1138. doi: 10.1038/s42003-021-02656-3
  • Nature Publishing Group
  • View : 725
  • Download : 250

Slitrk2 controls excitatory synapse development via PDZ-mediated protein interactions

  • Han, Kyung Ah
  • Kim, Jinhu
  • Kim, Hyeonho
  • Kim, Dongwook
  • Lim, Donseok
  • Ko, Jaewon
  • Um, Ji Won
  • 2019-11
  • Han, Kyung Ah. (2019-11). Slitrk2 controls excitatory synapse development via PDZ-mediated protein interactions. doi: 10.1038/s41598-019-53519-1
  • Nature Publishing Group
  • View : 628
  • Download : 121
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