Y
Yunhee Kang
Researcher at Emory University
Publications - 28
Citations - 2093
Yunhee Kang is an academic researcher from Emory University. The author has contributed to research in topics: Postsynaptic potential & Inhibitory postsynaptic potential. The author has an hindex of 16, co-authored 23 publications receiving 1730 citations. Previous affiliations of Yunhee Kang include Washington University in St. Louis & University of British Columbia.
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Journal ArticleDOI
Neurexin-neuroligin signaling in synapse development
Ann Marie Craig,Yunhee Kang +1 more
TL;DR: Initial knockdown and knockout studies indicate that neurexins and neuroligins have an essential role in synaptic transmission, particularly at GABAergic synapses, but further studies are needed to assess the in vivo functions of these complex protein families.
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LRRTMs and Neuroligins Bind Neurexins with a Differential Code to Cooperate in Glutamate Synapse Development
TL;DR: It is proposed that neurexins are master regulators of the cooperative activities of LRRTMs and neuroligins in synapse regulation, and in neuron cultures, LRRTM2 is more potent than neuroligin-1 in promoting synaptic differentiation, and these two families of neurxin-binding partners cooperate in an additive or synergistic manner.
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Fat Mass and Obesity-associated (FTO) Protein Regulates Adult Neurogenesis.
Liping Li,Liping Li,Liqun Zang,Liqun Zang,Feiran Zhang,Junchen Chen,Junchen Chen,Hui Shen,Hui Shen,Liqi Shu,Liqi Shu,Feng Liang,Feng Liang,Chunyue Feng,Deng Chen,Huikang Tao,Tianlei Xu,Ziyi Li,Yunhee Kang,Hao Wu,Lichun Tang,Pumin Zhang,Peng Jin,Qiang Shu,Xuekun Li,Xuekun Li +25 more
TL;DR: It is shown that FTO is expressed in adult neural stem cells and neurons and displays dynamic expression during postnatal neurodevelopment and this results suggest FTO plays important roles in neurogenesis, as well as in learning and memory.
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Structure Function and Splice Site Analysis of the Synaptogenic Activity of the Neurexin-1β LNS Domain
TL;DR: Differential neurexin-neuroligin binding affinities and splice variations may play an instructive role in postsynaptic differentiation, and mutation of two predicted Ca2+-binding residues disrupts post synaptogenic protein clustering and binding to neuroligins, consistent with previous findings that neureXin-NEurolig in binding is Ca2- dependent.
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Fragile X mental retardation protein modulates the stability of its m6A-marked messenger RNA targets.
Feiran Zhang,Yunhee Kang,Mengli Wang,Yujing Li,Tianlei Xu,Wei Yang,Hongjun Song,Hao Wu,Qiang Shu,Peng Jin +9 more
TL;DR: Biochemical analyses indicate that FMRP regulates the stability of its m6A‐marked mRNA targets through YTHDF2, which could potentially contribute to the molecular pathogenesis of FXS, and transcriptome‐wide gene expression profiling suggests that M6A is a widespread epitranscriptomic modification in brain.