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Dae Gyu Kim

Gangnam Severance Hospital

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Sung‐Hoon Kim

Kyung Hee University

Jung Min Han

Seoul National University

Myung Hee Kim

Korea Research Institute of Bioscience and Biotechnology

Beom Sik Kang

Kyungpook National University

Ha Yeon Cho

Kyungpook National University

Song-Yee Jang

Seong‐Jin Kim

CHA University

Ji‐Hyun Lee

Dong-A University

Min Guo

Shaoxing University

Jin Young Lee

Loyola University Maryland

Cooperative Institutions

Seoul National University

Yonsei University

Korea University

Dongguk University

Gangnam Severance Hospital

Korea University of Science and Technology

Sungkyunkwan University

Seoul National University Hospital

CHA University

Ewha Womans University

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Supplementary Figure S2 from Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2

Dae Gyu Kim Jin Young Lee Ji‐Hyun Lee Ha Yeon Cho Beom Sik Kang

<p>The significance of AIMP2 for Smurf2-dependent downregulation of FBP and the interaction of Smurf2 and FBP.</p>

10.1158/0008-5472.22411158.v1

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Supplementary Figure S2 from Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2

Dae Gyu Kim Jin Young Lee Ji‐Hyun Lee Ha Yeon Cho Beom Sik Kang

<p>The significance of AIMP2 for Smurf2-dependent downregulation of FBP and the interaction of Smurf2 and FBP.</p>

10.1158/0008-5472.22411158

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Supplementary Figure S4 from Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2

Dae Gyu Kim Jin Young Lee Ji‐Hyun Lee Ha Yeon Cho Beom Sik Kang

<p>The effect of AIMP2 on TGF-β receptor I stability, Smad2 phosphorylation and TGF-β target gene expression.</p>

10.1158/0008-5472.22411152

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Supplementary Figure S5 from Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2

Dae Gyu Kim Jin Young Lee Ji‐Hyun Lee Ha Yeon Cho Beom Sik Kang

<p>Identification of TGF-β1-induced phosphorylation site in AIMP2.</p>

10.1158/0008-5472.22411149.v1

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A Study on Influence of Naeil Cheum Deduction System on Job Satisfaction of small and medium-sized enterprises in Daegu and Gyeongbuk region

Industry Promotion Research (2017)

Dae Gyu Kim Sang Ho Lim

10.21186/ipr.2017.2.1.039

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2-Aminophenylpyrimidines as Novel Inhibitors of Aminoacyl-tRNA Synthetase Interacting Multifunctional Protein 2 (AIMP2)-DX2 for Lung Cancer Treatment

Journal of Medicinal Chemistry (2020)

Seungbeom Lee Dae Gyu Kim Kyeojin Kim Taewoo Kim Semi Lim

Aminoacyl-tRNA synthetase interacting multifunctional proteins (AIMPs) have recently been considered novel therapeutic targets in several cancers. In this publication we report the development of novel 2-aminophenylpyrimidines as new AIMP2-DX2 inhibitors. In particular, aminophenylpyrimidine 3 not only exhibited promising in vitro and in vivo potency but also exerted selective inhibition of H460 and A549 cells and AIMP2-DX2 rather than WI-26 cells and AIMP2. Aminophenylpyrimidine 3 offers possible therapeutic potential in the treatment of lung cancer.

Amino Acyl-tRNA Synthetases

10.1021/acs.jmedchem.9b01765

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Supplementary Figure S7 from Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2

Dae Gyu Kim Jin Young Lee Ji‐Hyun Lee Ha Yeon Cho Beom Sik Kang

<p>Effect of AIMP2 phosphorylation on its molecular interactions.</p>

10.1158/0008-5472.22411143.v1

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Supplementary Figure S6 from Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2

Dae Gyu Kim Jin Young Lee Ji‐Hyun Lee Ha Yeon Cho Beom Sik Kang

<p>Functional significance of TGF-β1-induced phosphorylation of AIMP2.</p>

10.1158/0008-5472.22411146

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Supplementary Figure S5 from Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2

Dae Gyu Kim Jin Young Lee Ji‐Hyun Lee Ha Yeon Cho Beom Sik Kang

<p>Identification of TGF-β1-induced phosphorylation site in AIMP2.</p>

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10.1158/0008-5472.22411149

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Targeting the interaction of AIMP2-DX2 with HSP70 suppresses cancer development

Nature Chemical Biology (2019)

Semi Lim Hye Young Cho Dae Gyu Kim Younah Roh Se-Young Son

10.1038/s41589-019-0415-2

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