D
Dae Gwin Jeong
Researcher at Korea Research Institute of Bioscience and Biotechnology
Publications - 51
Citations - 1626
Dae Gwin Jeong is an academic researcher from Korea Research Institute of Bioscience and Biotechnology. The author has contributed to research in topics: Protein tyrosine phosphatase & Virtual screening. The author has an hindex of 22, co-authored 51 publications receiving 1509 citations. Previous affiliations of Dae Gwin Jeong include Korea University of Science and Technology & Universidad Mayor.
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Journal ArticleDOI
Protein tyrosine phosphatase 1B inhibitors from Morus root bark.
Long Cui,MinKyun Na,Hyuncheol Oh,Eun Young Bae,Dae Gwin Jeong,Seong Eon Ryu,Sohee Kim,Bo Yeon Kim,Won Keun Oh,Jong Seog Ahn +9 more
TL;DR: An organic layer prepared from the Chinese crude drug 'Sang-Bai-Pi' (Morus root bark) was studied in order to identify the inhibitory compounds for protein tyrosine phosphatase 1B (PTP1B).
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Structure of Human FIH-1 Reveals a Unique Active Site Pocket and Interaction Sites for HIF-1 and von Hippel-Lindau *
TL;DR: The crystal structure of human FIH-1 is reported, revealing the unique environment of the active site and cofactor-binding region revealed in the structure that should allow design of selective drugs that can be used in ischemic diseases to promote hypoxia responses.
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Dephosphorylation of the C-terminal Tyrosyl Residue of the DNA Damage-related Histone H2A.X Is Mediated by the Protein Phosphatase Eyes Absent
Navasona Krishnan,Dae Gwin Jeong,Suk-Kyeong Jung,Seong Eon Ryu,Andrew Xiao,C. David Allis,Seung Jun Kim,Nicholas K. Tonks +7 more
TL;DR: This study provides the first indication of a physiological substrate for the EYA phosphatases and suggests a novel role for these enzymes in regulation of the DNA damage response.
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Synthesis and biological evaluation of rhodanine derivatives as PRL-3 inhibitors.
Jin Hee Ahn,Seung Jun Kim,Woul Seong Park,Sung Yun Cho,Jae Du Ha,Sung-Soo Kim,Seung Kyu Kang,Dae Gwin Jeong,Suk-Kyeong Jung,Sang-Hyeup Lee,Hwan Mook Kim,Song Kyu Park,Ki Ho Lee,Chang Woo Lee,Seong Eon Ryu,Joong-Kwon Choi +15 more
TL;DR: A series of rhodanine derivatives was synthesized and evaluated for their ability to inhibit PRL-3, and compound 5e was the most active in this series exhibiting an IC50 value of 0.9 microM in vitro and showed a reduced invasion in cell-based assay.
Journal ArticleDOI
Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms.
Dae Gwin Jeong,Seung Jun Kim,Jae-Hoon Kim,Jeong Hee Son,Mi Rim Park,Sang Myoun Lim,Tae-Sung Yoon,Seong Eon Ryu +7 more
TL;DR: The crystal structure of human PRL-1 determined at 2.7A resolution reveals the shallow active-site pocket with highly hydrophobic character and a trimer in the crystal and the trimer exists in the membrane fraction of cells, suggesting the possible biological regulation of PRL -1 activity by oligomerization.