Jeong‐Heon Ko

Korea Research Institute of Bioscience and Biotechnology

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Yong-Sam Kim

Korea Research Institute of Bioscience and Biotechnology

Cheorl‐Ho Kim

Korea Forest Service

Jong Shin Yoo

Korea Basic Science Institute

Jeong Gu Kang

Korea Research Institute of Bioscience and Biotechnology

Young‐Choon Lee

Dong-A University

Jeong Mi Lee

Genome Research Foundation

Jeong Hwa Lee

Catholic University of Korea

Su Bin Moon

Korea Research Institute of Bioscience and Biotechnology

Hyun Jung Chin

Korea Research Institute of Bioscience and Biotechnology

Sung‐Koo Kang

Bucheon University

Cooperative Institutions

Korea Research Institute of Bioscience and Biotechnology

Seoul National University

Korea University of Science and Technology

Sungkyunkwan University

Chungnam National University

Catholic University of Korea

Genome Research Foundation

Dongguk University

Korea Basic Science Institute

Yonsei University

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Inhibition of MKK7–JNK by the TOR Signaling Pathway Regulator-Like Protein Contributes to Resistance of HCC Cells to TRAIL-Induced Apoptosis

Gastroenterology (2012)

In Sung Song Soo Young Jun Hee–Jun Na Hyun–Taek Kim So Young Jung

Propidium iodide

Protein phosphatase 1

10.1053/j.gastro.2012.07.103

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Citations (51)

Expression of the human CMP-NeuAc:GM3 α2,8-sialyltransferase (GD3 synthase) gene through the NF-κB activation in human melanoma SK-MEL-2 cells

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression (2007)

Nam‐Young Kang Cheorl‐Ho Kim Kyoung-Sook Kim Jeong‐Heon Ko Jai‐Heon Lee

Chromatin immunoprecipitation

Transcription

10.1016/j.bbaexp.2007.08.001

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Citations (40)

Correction for Kim et al., Identification of Mycobacterial Antigens in Human Urine by Use of Immunoglobulin G Isolated from Sera of Patients with Active Pulmonary Tuberculosis

Journal of Clinical Microbiology (2016)

Sun Hee Kim Nan-Ee Lee Jong Seok Lee Jeong Hwan Shin Ju Yeon Lee

Volume 54, no. 6, p. [1631–1637][1], 2016. Page 1631: The byline should appear as shown above. [1]: /lookup/doi/10.1128/JCM.00236-16

Identification

Immunoglobulin M

10.1128/jcm.01059-16

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Developments of cancer biomakers : a glyco-oriented approach

한국당과학회 학술대회 (2009)

Jeong‐Heon Ko

Cancer is often difficult to early diagnose, but early diagnosis is a crucial factor for good outcome in the cancer. N-acetylglucosaminyltransferase V catalyzes an addition of b1,6-N-acetylglucosamine (GlcNAc) to the core N-glycan, many lines of evidence have demonstrated the role of N-acetylglucosaminyltransferase V (GnT-V) in the pathogenecity of colon cancer cell. One of the related example is an aberrant TIMP-1-mediated cancer progression in which deterioration of the quality of TIMP-1 is induced by glycosyl alterations through GnT-V catalysis, leading to mitigated MMP inhibition responsible for an strengthened invasive/metastatic potential of cancer cells. Accordingly the identification of target proteins for GnT-V has been an important subject for cancer biomarker discovery. We developed a protocol in which L-PHA, a lectin recognizing b1,6-GlcNAc, is conjugated to avidin-agarose complex to capture b1,6-GlcNAc-carrying serological glycoproteins and the captured glycoproteins were identified using an LTQ-FTICR mass spectrometer. Candidate proteins showing differential amounts between normal and cancer sera were confirmed by western blot analysis and will be subject to validation for valid biomarker for colon cancer.

Glycoproteomics

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Overexpression of membrane sialic acid-specific sialidase Neu3 inhibits matrix metalloproteinase-9 expression in vascular smooth muscle cells

Biochemical and Biophysical Research Communications (2007)

Sung‐Kwon Moon Seung-Hak Cho Kyung‐Woon Kim Jae Heung Jeon Jeong‐Heon Ko

Sialidase

10.1016/j.bbrc.2007.02.155

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Citations (26)

Machine Learning Classifies Core and Outer Fucosylation of N-Glycoproteins Using Mass Spectrometry

Scientific Reports (2020)

Heeyoun Hwang Hoi Keun Jeong Hyun Kyoung Lee Gun Wook Park Ju Yeon Lee

Abstract Protein glycosylation is known to be involved in biological progresses such as cell recognition, growth, differentiation, and apoptosis. Fucosylation of glycoproteins plays an important role for structural stability and function of N-linked glycoproteins. Although many of biological and clinical studies of protein fucosylation by fucosyltransferases has been reported, structural classification of fucosylated N-glycoproteins such as core or outer isoforms remains a challenge. Here, we report for the first time the classification of N-glycopeptides as core- and outer-fucosylated types using tandem mass spectrometry (MS/MS) and machine learning algorithms such as the deep neural network (DNN) and support vector machine (SVM). Training and test sets of more than 800 MS/MS spectra of N-glycopeptides from the immunoglobulin gamma and alpha 1-acid-glycoprotein standards were selected for classification of the fucosylation types using supervised learning models. The best-performing model had an accuracy of more than 99% against manual characterization and area under the curve values greater than 0.99, which were calculated by probability scores from target and decoy datasets. Finally, this model was applied to classify fucosylated N-glycoproteins from human plasma. A total of 82N-glycopeptides, with 54 core-, 24 outer-, and 4 dual-fucosylation types derived from 54 glycoproteins, were commonly classified as the same type in both the DNN and SVM. Specifically, outer fucosylation was dominant in tri- and tetra-antennary N-glycopeptides, while core fucosylation was dominant in the mono-, bi-antennary and hybrid types of N-glycoproteins in human plasma. Thus, the machine learning methods can be combined with MS/MS to distinguish between different isoforms of fucosylated N-glycopeptides.

Fucosylation

10.1038/s41598-019-57274-1

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Citations (31)

Bombycis corpusExtract (BCE) Protects Hippocampal Neurons Against Excitatory Amino Acid-Induced Neurotoxicity

Immunopharmacology and Immunotoxicology (2003)

Byung‐Soo Koo Hyun-Guk An Sung‐Kwon Moon Young‐Choon Lee Hyung‐Min Kim

Bombycis corpus (BC) or Bombyx Batryticatus, a batryticated silkworm and white-stiff silkworm, is a drug consisting of the dried larva of silkworm, Mobyz mori L., dead and stiffened due to the infection of Beauveria (Bals.) Vuill. In a previous paper (Kim et al., Pharmacol. Res., 43, 12–16, 2001), BC was shown to protect amyloid-β-induced cytotoxicity. In the present study, we have found that BCE can prevent or reduce the neurotoxic actions in the hippocampus of the glutamate agonists N-methyl-D-aspartic acid (NMDA) in vitro or alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) and kainic acid in vitro. Pre-treatment with BCE (0, 1, 2, 5, and 10 μg/ml for 6–8 h) protected primary hippocampal cultures from embryonic day 18 (E18) embryos against NMDA-induced toxicity (0.1, 1, 10, and 50 mM/ml). BCE added either with NMDA (1 mM) or 1 h later had lesser, but still significant, protective actions. BCE also reduced NMDA-induced toxicity (1 mM). BCE (10 μg/ml) protected cultured neurons against the neurotoxic actions of either AMPA (25 μM) or kainic acid (1 mM) as well. Because the release of glutamate has been implicated in the neural damage after cerebral ischemia and other neural insults, these results suggest that BCE may contribute significantly to protect human brain to such damage.

Neurotoxicity

Excitotoxicity

10.1081/iph-120020469

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Citations (17)

14-3-3β Depletion Drives a Senescence Program in Glioblastoma Cells Through the ERK/SKP2/p27 Pathway

Molecular Neurobiology (2017)

Sung Bin Seo Je‐Jung Lee Hye Hyeon Yun Chang‐Nim Im Yong-Sam Kim

Senescence

10.1007/s12035-017-0407-8

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Citations (23)