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Impaired formation of high-order gephyrin oligomers underlies gephyrin dysfunction-associated pathologies

  • Kim, Seungjoon
  • Kang, Mooseok
  • Park, Dongseok
  • Lee, Ae-Ree
  • Betz, Heinrich
  • Ko, Jaewon
  • Chang, Iksoo
  • Um, Ji Won
  • 2021-02
  • Kim, Seungjoon. (2021-02). Impaired formation of high-order gephyrin oligomers underlies gephyrin dysfunction-associated pathologies. doi: 10.1016/j.isci.2021.102037
  • Cell Press
  • View : 836
  • Download : 573
  • Kim, Dong-Il
  • Kang, Mooseok
  • Kim, Sangyeol
  • Lee, Juhwan
  • Park, Yongsoo
  • Chang, Iksoo
  • Suh, Byung-Chang
  • 2015-09
  • Biophysical Journal, v.109, no.5, pp.922 - 935
  • Cell Press
  • View : 875
  • Download : 0

Polymorphism of fibrillar structures depending on the size of assembled A beta(17-42) peptides

  • Cheon, Mookyung
  • Kang, Mooseok
  • Chang, Iksoo
  • 2016-11
  • Cheon, Mookyung. (2016-11). Polymorphism of fibrillar structures depending on the size of assembled A beta(17-42) peptides. Scientific Reports, 6. doi: 10.1038/srep38196
  • Nature Publishing Group
  • View : 956
  • Download : 163

Structural and molecular insight into the pH-induced low-permeability of the voltage-gated potassium channel Kv1.2 through dewetting of the water cavity

  • Lee, Juhwan
  • Kang, Mooseok
  • Kim, Sangyeol
  • Chang, Iksoo
  • 2020-04
  • Lee, Juhwan. (2020-04). Structural and molecular insight into the pH-induced low-permeability of the voltage-gated potassium channel Kv1.2 through dewetting of the water cavity. PLoS Computational Biology, 16(4), e1007405. doi: 10.1371/journal.pcbi.1007405
  • Public Library of Science
  • View : 681
  • Download : 94
  • Lee, Juhwan
  • Sim, Kyoung Mi
  • Kang, Mooseok
  • Oh, Hyun Ju
  • Choi, Ho Jung
  • Kim, Yeong Eun
  • Pack, Chan-Gi
  • Kim, Kyunggon
  • Kim, Kyung Mo
  • Oh, Seak Hee
  • et al
  • 2024-01
  • Lee, Juhwan. (2024-01). Understanding the molecular mechanism of pathogenic variants of BIR2 domain in XIAP-deficient inflammatory bowel disease. Scientific Reports, 14(1). doi: 10.1038/s41598-023-50932-5
  • Nature Publishing Group
  • View : 290
  • Download : 29
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