Výsledky vyhledávání - "Suk-Kyeong Jung"

Akademický článek

Structure-Based Virtual Screening Approach to the Discovery of Novel Inhibitors of Eyes Absent 2 Phosphatase with Various Metal Chelating Moieties.

Autor: Hwangseo Park¹ hspark@sejong.ac.kr, Suk-Kyeong Jung², Yu, Keum R.², Kim, Ju H.², Yong-Sam Kim³, Ko, Jeong H.³, Park, Byoung C.³, Kim, Seung J.² ksj@kribb.re.kr

Publikováno v: Chemical Biology & Drug Design. Oct2011, Vol. 78 Issue 4, p642-650. 9p. 6 Diagrams, 2 Charts, 1 Graph.

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Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates

Autor: Bonsu Ku, Kwang-Hee Bae, Sang Chul Lee, Suk-Kyeong Jung, Hyeyun Jung, Raymond L. Erikson, Sa Yeon Cho, Keum Ran Yu, Hwangseo Park, Young Jun Kim, Seung Jun Kim, Sang J. Chung, Seong Eon Ryu, Bo Yeon Kim

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 69:1522-1529

Unlike other classical protein tyrosine phosphatases (PTPs), PTPRQ (PTP receptor type Q) has dephosphorylating activity towards phosphatidylinositide (PI) substrates. Here, the structure of the catalytic domain of PTPRQ was solved at 1.56 Å resoluti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b640602c2fa6ded6408abc5f1359b5e3
https://doi.org/10.1107/s0907444913010457

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Exploring binding sites other than the catalytic core in the crystal structure of the catalytic domain of MKP-4

Autor: Byoung Cheol Park, Seong Eon Ryu, Seung Jun Kim, Dae Gwin Jeong, Tae-Sung Yoon, Hwangseo Park, Suk Kyeong Jung

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 67:25-31

Map kinase phosphatase 4 (MKP-4), which has been implicated in signalling pathways that negatively regulate glucose uptake, belongs to the dual-specificity phosphatase (DUSP) family. An inherent property of MKPs is an ability to undergo structural re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::438af0aaa61ff6871e292543caedc8e3
https://doi.org/10.1107/s0907444910042381

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Discovery of Novel and Potent Cdc25 Phosphatase Inhibitors Based on the Structure-Based De Novo Design

Autor: Suk Kyeong Jung, Dae Gwin Jeong, Seung Jun Kim, Young Jae Bahn, Seong Eon Ryu, Hwangseo Park

Publikováno v: Bulletin of the Korean Chemical Society. 30:1313-1316

Cdc25 phosphatases have been considered as attractive drug targets for anticancer therapy due to the correlation of their overexpression with a wide variety of cancers. We have been able to identify five novel Cdc25 phosphatase inhibitors with microm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a162e8d98e59c6d5eee6725f43886807
https://doi.org/10.5012/bkcs.2009.30.6.1313

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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

Autor: Dae Gwin Jeong, Seung Jun Kim, Seong Eon Ryu, Navasona Krishnan, C. David Allis, Nicholas K. Tonks, Suk-Kyeong Jung, Andrew Xiao

Publikováno v: Journal of Biological Chemistry. 284:16066-16070

In mammalian cells, the DNA damage-related histone H2A variant H2A.X is characterized by a C-terminal tyrosyl residue, Tyr-142, which is phosphorylated by an atypical kinase, WSTF. The phosphorylation status of Tyr-142 in H2A.X has been shown to be a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abad911220779e46304d921e643396ab
https://doi.org/10.1074/jbc.c900032200

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Discovery of Novel Cdc25 Phosphatase Inhibitors with Micromolar Activity Based on the Structure-Based Virtual Screening

Autor: Young Jae Bahn, Hwangseo Park, Dae Gwin Jeong, Seong Eon Ryu, Seung Jun Kim, Tae-Sung Yoon, Il Seo, Sang-Hyeup Lee, Suk-Kyeong Jung

Publikováno v: Journal of Medicinal Chemistry. 51:5533-5541

Cdc25 phosphatases have been considered as attractive drug targets for anticancer therapy because of the correlation of their overexpression with a wide variety of cancers. We have been able to identify five novel Cdc25 phosphatase inhibitors with mi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c1fe822e838953e0177cd4b19e781ba
https://doi.org/10.1021/jm701157g

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Structural basis for the cold adaptation of psychrophilic M37 lipase fromPhotobacterium lipolyticum

Autor: Byoung Chul Park, Jae-Hoon Kim, Mi Sook Lee, Seong Eon Ryu, Seung Jun Kim, Suk-Kyeong Jung, Dae Gwin Jeong, Hyung-Kwoun Kim, Jung Kee Lee

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 71:476-484

The M37 lipase from Photobacterium lipolyticum shows an extremely low activation energy and strong activity at low temperatures, with optimum activity seen at 298 K and more than 75% of the optimum activity retained down to 278 K. Though the M37 lipa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fee1d2d54c4d7922df3c710a9bac8810
https://doi.org/10.1002/prot.21884

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Crystal Structure of the Catalytic Domain of Human MAP Kinase Phosphatase 5: Structural Insight into Constitutively Active Phosphatase

Autor: Dae Gwin Jeong, Seung Jun Kim, Tae-Sung Yoon, Jae-Hoon Kim, Jeong Hee Son, Suk-Kyeong Jung, Seong Eon Ryu, Mi Young Shim

Publikováno v: Journal of Molecular Biology. 360:946-955

MAP kinase phosphatase 5 (MKP5) is a member of the mitogen-activated protein kinase phosphatase (MKP) family and selectively dephosphorylates JNK and p38. We have determined the crystal structure of the catalytic domain of human MKP5 (MKP5-C) to 1.6

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ab8ef215e16bd76a050ca394507cf87
https://doi.org/10.1016/j.jmb.2006.05.059

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