Faculty

김철호 교수님(Cheorl Ho Kim)

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작성일 21-04-27 17:27

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 김철호 (Cheorl Ho Kim)

 직함

 교수

 전공

 분자당생물학

 연구실

 분자세포당생물학연구실

 전화

 031-290-7002

 사무실

 제2과학관 32102

 이메일

 chkimbio@skku.edu 

 

  

 Research Background

"Thedeciphering (signaling) of the carbohydrate code in cells will undoubtedly opennew vistas in biology." Stryer's Biochemsitry,4th edition. Chapter18(CARBOHYDRATE), PAGE 479 Functional glycobiology and glycomic studies on human diseases andbiodiversity by supra molecular system and establishment of novel industrialbasisChange of the cell surface glycosylation is one of the most important modifications that occur in cellular transformation such as development, differentiation, growth, aging, immune system and oncogenesis. Membrane domain is a transient supra-molecular organization assembled by specific glycoconjugates and sphingolipids. Although domain formation is promoted by purely physical interactions between components, synthesis and distribution of these components are under strict genetic control. Both glycoproteins and glycolipids carbohydrate moieties are affected by cellular transformation, leading to the appearance of carbohydrate tumor associated antigens (CTAA). These changes in glycosylation have been described for a large number of cancer types and are usually associated with a poor prognosis for the patients. Most of the CTAA are sialylated antigens and the increase of sialylation is a well-known general feature of transformed cells. As an example, the mucin-type Sialyl-Tn antigen is increased in pancreas, gastric, colon, uterus and breast cancers and associated with a poor prognosis for the patients. Modifications of cellular glycosylation are a common phenotypic change in malignancy. However, only a limited number of biosynthetic pathways are frequently altered in cancer.    

 
Increased 1,6-branching of N-linked glycans, increased Sialyl-LewisX [NeuAc 2-3Gal 1-4(Fuc 1-3)GlcNAc] and Sialyl-Lewisa
[NeuAc 2-3Gal 1-3(Fuc 1-4)GlcNAc] epitopes, or the general increase in sialylation of cell surface glycoproteins are commonly observed in N-linked and O-linked oligosaccharides of carcinoma cell glycoproteins. These changes in glycosylation are related to grade, invasion, metastasis and with a poor prognosis. A family of enzymes named sialyltransferases catalyzes the biosynthesis of sialylated oligosaccharide sequences. These enzymes use CMP-sialic acid as the activated sugar donor. Twenty different sialyltransferases acting on glycoproteins and/or glycolipids have been characterized and cDNAs have been cloned from human tissues or cells. Changes in sialyltransferase expression have been observed in cancer tissues or cells and the regulation of their expression is achieved mainly at the transcriptional level. For example, transfection of rat fibroblasts with the ras oncogene leads to an increase of the galactoside 2,6-sialyltransferase (EC 2.4.99.1, ST6Gal I) mRNA, and of the invasion potential of these cells. Carbohydrate changes also occur in breast cancer. Sialyl-LewisX, Sialyl-Lewisa and Sialyl-Tn [NeuAc2-6GalNAc1-O-Ser/Thr] are tumor-associated antigens found in breast cancer. As previously described, breast cancer cells showed an elevated activity in the transfer of sialic acid onto Gal1-3GalNAc-R acceptor substrates. We have shown that the increased expression of sialyltransferases, the enzymes involved in the biosynthesis of sialylated antigens, can be correlated with the over-expression of CTAA and could be used as tumor makers for the following of breast and colon cancer patients, especially for node-negative patients.   
 
On the other hand, gangliosides, the glycosphingolipids carrying one or more sialic acid residues in their carbohydrate moiety, are often found in growing and developing tissues. GD2, GD3 and GT3 are considered as oncofetal markers in animal and human tumors like neuronal tumors, melanoma or breast cancer. The biosynthesis of gangliosides is achieved by a series of highly specific glycosyltransferases, including sialyltransferases. In cell levels, membrane domain is a transient supra-molecular organization assembled by specific glycoconjugates and sphingolipids (Fig. 1). Although domain formation is promoted by purely physical interactions between components, synthesis and distribution of these components are under strict genetic control. We will genetically analyze expression of  omain components, and also study cell biology and biophysics of assembly and function of glyco-chains and sphingolipids. Hopefully, this will reveal supramolecular assembly in glycoprotein and sphingolipid membrane domains and eventually lead to establishing a novel industrial basis. The Global Research Laboratory Project that we would like to initiate between both laboratories focuses on the Sialylated microdomain with regard to the cellular function by the biosynthesis of the gangliosides (for example, GD3 using the ST8Sia I or GD3 synthase) and glycol-functional conjugates. Certainly, the applicants believe that this approach is new conception in the biology and medicine, potentially, applicable to search of markers and drugs of the development of human cancer with the increased aggressivity of the tumor.
 
A) A study plan on glyco-chain expression: Glyco-chains are biological chain-structures composed of monosaccharides, like galactose and glucose. Structural diversity of glyco-chains contributes to the efficiency of signal diciphering and transmission. Supra-biomolecular system composed of several membrane molecules through non-covalent bonding is recently recognized to play important roles for the signaling, and glyco-chains are involved in this supra-biomolecular system. Glyco-chain functions are supported by regulation mechanisms which control the stage- and cell-specific expressions. This research aims at the elucidation of molecular mechanisms responsible for glyco-chain expression involved in the supra-biomolecular system, and contributes to the establishing of integrative glycobiology and glycomics. (1) Expression analysis of glyco-chain related genes using DNA and Proteomic microarray. (2) Studies on the molecules controlling the expression of sialic acid species.

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B) A study plan on glyco-chain function: Sialic acid is transferred from CMP-sialic acid to an acceptor glycan through the catalysis of sialyltransferase. Some of glyco-chains on cellular surface are regarded to be potential signaling molecules in cellular communications. Glyco-chains are biosynthesized through the catalysis of membrane-bound glycosyltransferases. We would like to address the pathological significance of glycosyltransferase function and resulting abnormalities of glyco-chain metabolism. We also hope to apply our future results for developing new diagnostic means and therapeutics of the disease.(1) Analysis on controlling mechanisms of glyco-chains through glycosyltransferases. (2) Functions of glyco-chains in the cancer biology and immune systems.

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C) A study plan on sphingolipid expression and function: Sphingolipids and glycolipids are a family of biomembrane components. Supra-biomolecular system including sphingolipids and glycolipids is considered to play important roles for signal transduction. This complex suggests that the targeting of lipids is highly regulated and that cells require complex supramolecular organization within membranes. In particular, sphingolipid/cholesterol supramolecular domains have been recently revealed to play an important role in membrane biogenesis as well as signal transduction. Metabolic precursors of sphingolipids are also considered to be bioactive substances and induce differentiation and programmed cell death. This research team focuses on enzymes involved in the sphingolipid and glycolipid biosynthesis by means of biochemistry and molecular biology and try to modulate functions of membrane bound molecules by manipulating sphingolipids and glycolipids. The development of micro-analysis by mass spectrometry for glycolipids and glycopeptides is also the subject of this research team. We try to identify genes involved in the formation and maintenance of domains in order to understand the principle which governs the formation of sphingolipid domains. We hope our study eventually leads to the establishment of an innovative industrial basis such as "domain sensor".(1) Studies on enzymes regulating sphingolipid expression. (2) Functional modulation of membrane molecules with sphingolipids. (3) Establishment of micro-analysis of sphingolipids. (4) Role of lipid domains in the endocytic pathway.
 

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Excellency of Laboratory : Laboratory has been recognized as a pioneer group in Glycobiology and Glycomics study through the world, as evidenced and demonstrated by the following confirmations: The Lab has the authors of over 300 peer-reviewed articles published in international scientific journals. His distinguished discoveries recognized in the biomedical area are well documented in the Academic Society from the following outstanding findings: Viral hepatocarcinoma and PTEN (Cancer Research 2003), asialo-1 acid glycoprotein in liver cirrhosis and carcinoma (Hepatology Research, 2003), UDP-N-GlcNAc:β-D-Man-1,4-N-GlcNAc-T-III in hepatitis (Glycoconjugate J, 2003), plasma MMP-9/2 and α-fetoproteins in HBV chronic hepatitis (J. Gastroenterol. and Hepatology. 2004), HBV metastatic potential (FASEB J. 2004), Hepatic V and GnT-III-Apolipoprotein B (JBC. 2004), Disialo GD3 in VSMC responses (JBC. 2004), therapeutic hepatocarcinoma cells (FASEB J. 2004), Transglutaminase 2 signaling in leukemia (FEBS Lett. 2004), bisecting N-GlcNAc-T-III in HBV (J Gastroenterol Hepatol, 2004), Monosialyl GM3 in leukemic differentiation (Glycobiology 2005), MMP-9 in In Vitro Fertilization (British J Obstetrics and Gynecology 2005), disialo GD3 Fas-induced T cells (Glycobiology 2006), GM3 in PTEN-mediated progression (Glycobiology 2006), ROS in sialic GD3-cell function (FASEB J 2006), AP-2a in GM3-PTEN (Glycobiology 2008), sialidase in leukemia (Biochimica et Biophysica Acta 2008), GM3-VEGFR-2 interaction (Glycobiology 2009), GD3 in breast cancer cells (Biological Chemistry 2009), pig CMAH and N-glycolylneuraminic acid (Biochemical J 2010), pST6GalNAc IV for Neu5Acalpha2-3Galbeta1-3GalNAc (Glycoconjugate J 2011), GM3 in TGF-β1-induced EMT (Biochemical J. 2013), VEGFR-2 in neovascularization (J Molecular Medicine 2013), monosialyl GMs and TGF.receptor interaction (Int. J. of Biochem. Cell Biol. 2014), Sialyl Leuis A/X preference of HBx (Molecular Cancer 2014).
 

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Cer, ceramide; SA, sialic acid; GalNAcT, N-acetylgalactosaminyltransferase I or GM2/GD2/GT2-synthase; GalT1, galactosyltransferase I; GalT2, galactosyltransferase IIor GM1-synthase; GalT3, galactosyltransferase III; GlcT, glucosyltransferase; ST1, sialyltransferase I or GM3-synthase; ST2, sialyltransferase II or GD3-synthase; ST3, sialyltransferase III or GT3-synthase; ST4; sialyltransferase IV or GD1a-synthase; ST5,sialyltransferase V or GT1a-synthase.
 
        
 Peer review paper
 
       1.     Park JY, Choi HJ, Park T, Lee MJ, Lim HS, Yang WS, Hwang CW, Park D, Kim CH. 2021. Inhibitory Effect of Avenanthramides (Avn) on

         Tyrosinase Activity and Melanogenesis in α-MSH-Activated SK-MEL-2 Cells: In Vitro and In Silico Analysis. Int J Mol Sci. 2021 Jul 22;22(15):7814.

   2.     Kim IS, Kim CH, Yang WS. Physiologically Active Molecules and Functional Properties of Soybeans in Human Health-A Current 

          Perspective. Int J Mol Sci. 2021 Apr 14;22(8):4054.

   3.     Kim C.H. 2021. Anti-SARS-CoV-2 Natural Products as Potentially Therapeutic Agents. Front Pharmacol. 2021 May 27;12:590509.   

4.     Kim IS, Kim CH, Yang WS. 2021. Physiologically Active Molecules and Functional Properties of Soybeans in Human Health-A Current Perspective. Int J Mol Sci. 2021 Apr 14;22(8):4054.  

5.     Kim IS, Hwang CW, Yang WS, Kim CH. 2021. Current Perspectives on the Physiological Activities of Fermented Soybean-Derived CGJ. Int J Mol Sci. 2021 May 27;22(11):5746.

6.     Park J, Choi H, Abekura F, Lim HS, Im JH, Yang WS, Hwang CW, Chang YC, Lee YC, Park NG, Kim CH. 2021. Avenanthramide C Suppresses Matrix Metalloproteinase-9 Expression and Migration Through the MAPK/NF- κB Signaling Pathway in TNF-α-Activated HASMC Cells. Front Pharmacol. 2021 Mar 25;12:621854. \

  7.     Cho SH, Kim JB, Kim CH, Bak YS. 2021. Evaluation of Microbiological Contamination of Dummies Used in Cardiopulmonary

         Resuscitation  in Korea. Curr Pharm Biotechnol. 2021;22(2):281-287.

  8.     Lee KM, Kim CH, Kim JH, Kim SS, Cho SH. 2021.e-Membranome: A Database for Genome-Wide Analysis of Escherichia coli Outer

        Membrane Proteins. Curr Pharm Biotechnol. 2021;22(4):501-507.

9.     Lim H, Park JY, Abekura F, Choi H, Kim HD, Magae J, Chang YC, Lee YC, Kim CH. 2021. 4-O-methylascochlorin attenuates inflammatory responses induced by lipopolysaccharide in RAW 264.7 macrophages. Int Immunopharmacol. 2021 Jan;90:107184.

10.   An SY, Lee M, Yoon HK, Abekura F, Kim KS, Kim DH, Kim HJ, Lee K, Kim CH, Lee YC. 2020. Regulation of human β-galactoside α2,6-sialyltransferase (hST6Gal I) gene expression during differentiation of human osteoblastic MG-63 cells. Glycoconj J. 2020 Dec;37(6):681-690. Doi: 10.1007/s10719-020-09959-3. Epub 2020 Oct 27.

11.   Cho SH, Bak YS, Kim CH, Kim JB. 2000. Evaluation of Microbiological Contamination of Dummies used in Cardio-pulmonary Resuscitation in Korea. Curr Pharm Biotechnol. 2020 Aug 6. Doi: 10.2174/1389201021666200807105136.

12.   Kwak CH, Song KH, Kim CH.  Gram-Negative Bacterial Endotoxin LPS Induces NeuGc Loss through Ets1-Dependent Downregulation of Intestine-Specific pcmah Transcript in Porcine Intestinal Cells. Int J Mol Sci. 2020 Jul 10;21(14):4892. Doi: 10.3390/ijms21144892. NRF

13.   Kim CH. SARS-CoV-2 Evolutionary Adaptation toward Host Entry and Recognition of Receptor O-Acetyl Sialylation in Virus-Host Interaction.  Int J Mol Sci. 2020 Jun 26;21(12):4549. Doi: 10.3390/ijms21124549.  

14.   Lee KM, Cho SH, Kim CH, Kim JH, Kim SS. E-Membranome: a Database for Genome-Wide Analysis of Escherichia coli Outer Membrane Proteins. Curr Pharm Biotechnol. 2020 Jun 9. Doi: 10.2174/1389201021666200610105549. 

15.   Kim HW, Jeong YJ, Hwang SK, Park YY, Choi YH, Kim CH, Magae J, Chang YC. Ascofuranone inhibits epidermal growth factor-induced cell migration by blocking epithelial-mesenchymal transition in lung cancer cells. Eur J Pharmacol. 2020 Aug 5;880:173199. Doi: 10.1016/j.ejphar.2020.173199. Epub 2020 May 18.

16.   Cho SH, Lee KM, Kim CH, Kim SS. Construction of a Lectin-Glycan Interaction Network from Enterohemorrhagic Escherichia coli Strains by Multi-omics Analysis. Int J Mol Sci. 2020 Apr 12;21(8):2681. Doi: 10.3390/ijms21082681.

17.   Jang HY, Hong OY, Youn HJ, Kim MG, Kim CH, Jung SH, Kim JS. 15d-PGJ2 inhibits NF-κB and AP-1-mediated MMP-9 expression and invasion of breast cancer cell by means of a heme oxygenase-1-dependent mechanism. BMB Rep. 2020 Apr;53(4):212-217. Doi: 10.5483/BMBRep.2020.53.4.164.

18.   Ha SH, Kwak CH, Park JY, Abekura F, Lee YC, Kim JS, Chung TW, Kim CH. 3’-sialyllactose targets cell surface protein, SIGLEC-3, and induces megakaryocyte differentiation and apoptosis by lipid raft-dependent endocytosis. Glycoconj J. 2020 Apr;37(2):187-200. Doi: 10.1007/s10719-019-09902-1. Epub 2020 Jan 4. NRF

19.   Chung TW, Park MJ, Lee H, Kim KJ, Kim CH, Choi HJ, Ha KT. Enhancement of Endometrial Receptivity by Cnidium officinale through Expressing LIF and Integrins. Evid Based Complement Alternat Med. 2019 Nov 16;2019:7560631. Doi: 10.1155/2019/7560631. eCollection 2019.

20.   Jeong YJ, Park YY, Park KK, Choi YH, Kim CH, Chang YC. Bee Venom Suppresses EGF-Induced Epithelial-Mesenchymal Transition and Tumor Invasion in Lung Cancer Cells. Am J Chin Med. 2019;47(8):1869-1883. Doi: 10.1142/S0192415X19500952.

21.   Ha SH, Choi H, Park JY, Abekura F, Lee YC, Kim JR, Kim CH. Mycobacterium tuberculosis-Secreted Protein, ESAT-6, Inhibits Lipopolysaccharide-Induced MMP-9 Expression and Inflammation Through NF-κB and MAPK Signaling in RAW 264.7 Macrophage Cells. Inflammation. 2019 Nov 13. Doi: 10.1007/s10753-019-01087-x. 

22.   Nam JH, Cha B, Park JY, Abekura F, Kim CH, Kim JR. Mitogen-Induced Interferon Gamma Production in Human Whole Blood: The Effect of Heat and Cations. Curr Pharm Biotechnol. 2019;20(7):562-572. Doi: 10.2174/1389201020666190528093432.

23.   Kwak CH, Lee JH, Kim EY, Han CW, Kim KJ, Lee H, Cho M, Jang SB, Kim CH, Chung TW, Ha KT. Huzhangoside A Suppresses Tumor Growth through Inhibition of Pyruvate Dehydrogenase Kinase Activity. Cancers (Basel). 2019 May 23;11(5). Pii: E712. Doi: 10.3390/cancers11050712.

24.   Park J, Kim HD, Lee SH, Kwak CH, Chang YC, Lee YC, Chung TW, Magae J, Kim CH. Ascochlorin induces caspase-independent necroptosis in LPS-stimulated RAW 264.7 macrophages. J Ethnopharmacol. 2019 Jul 15;239:111898. Doi: 10.1016/j.jep.2019.111898. Epub 2019 Apr 24.

25.   Park J, Ha SH, Abekura F, Lim H, Magae J, Ha KT, Chung TW, Chang YC, Lee YC, Chung E, Ku J, Kim CH. 4-O-Carboxymethylascochlorin Inhibits Expression Levels of on Inflammation-Related Cytokines and Matrix Metalloproteinase-9 Through NF-κB/MAPK/TLR4 Signaling Pathway in LPS-Activated RAW264.7 Cells. Front Pharmacol. 2019 Mar 27;10:304. Doi: 10.3389/fphar.2019.00304. eCollection 2019.

26.   Yang WS, Kim JC, Lee JY, Kim CH, Hwang CW. Antihyperlipidemic and Antioxidative Potentials of Onion (Allium cepa L.) Extract Fermented with a Novel Lactobacillus casei HD-010. Evid Based Complement Alternat Med. 2019 Mar 3;2019:3269047. Doi: 10.1155/2019/3269047. eCollection 2019.

27.   Song KH, Kwak CH, Chung TW, Ha SH, Park JY, Ha KT, Cho SH, Lee YC, Kim CH. Intestine specific regulation of pig cytidine-5’-monophospho-N-acetylneuraminic acid hydroxylase gene for N-glycolylneuraminic acid biosynthesis. Sci Rep. 2019 Mar 12;9(1):4292. Doi: 10.1038/s41598-019-40522-9.

28.   Kim JC, Jeon JY, Yang WS, Kim CH, Eom DW. Combined Amelioration of Ginsenoside (Rg1, Rb1, and Rg3)-enriched Korean Red Ginseng and Probiotic Lactobacillus on Non-alcoholic Fatty Liver Disease. Curr Pharm Biotechnol. 2019;20(3):222-231.  

29.   Chung SY, Kwon TS, Bak YS, Park JJ, Kim CH, Cho SH and Kim W. 2019.Comparative genomic analysis of enterotoxigenic Escherichia coli O159 strains isolated from diarrheal patients in Korea. Gut Pathogens201911:9. https://doi.org/10.1186/s13099-019-0289-6

30.   Abekura F, Park J, Kwak CH, Ha SH, Cho SH, Chang YC, Ha KT, Chang HW, Lee YC, Chung TW, Kim CH. 2019. Esculentoside B inhibits inflammatory response through JNK and downstream NF-κB signaling pathway in LPS-triggered murine macrophage RAW 264.7 cells. Int Immunopharmacol. 2019 Mar;68:156-163. Doi: 10.1016/j.intimp.2019.01.003. Epub 2019 Jan 9.

 
 Funding history
• 2019 - 2021    Development of Cardiovascular vessel-regulating functional compounds. PI, ITEP
• 2015 - 2021      Development of Tumor Specific sialic acid-glycans and tumor control. PI, NRF
• 2013 - 2014 Biosyntetic evolution of Sialic acid-containing glycome and VEGFR-regulating Sialyl glycomics identification,PI, KRF, Korea
• 2009 - 2012 Chnodermal animal-nased glycan derived biology. PI, KIMST
• 2006 - 2009 Sialoantigenic Xenotransplantation Antigens, PI, Ministry of Education, Science and Technology, KRA, Ministry of Agriculture,
Fisheries and Foods, Korea
• 2002 - 2006 Complex Glycan Biosynthesis Regulation, NRL, KISTEP, PI, MOST, Korea.
• 1995 - 1996 G7 Project for GlcNAc-III Liver Disease. PI. MOST, Korea
• 1990 - 1996 Cancer metastatic N-GlcNAc-V glycan synthesis. PI. MOST, Korea.

 Education and experiences
• 1990 PhD University of Tokyo, Tokyo, Japan
• 1987 MSc University of Tokyo, Tokyo, Japan
• 1984 BSc Chung-Ang University, Seoul, Korea
• 2006 - Present  Professor, Chair, Dept. Biological Sciences, Sungkyunkwan University
• 2015 – 2016       Visiting Scholar, The Ohio State University, USA (KC Lee)
• 2010 – 2011       Visiting Scholar, Glycoscience, Tokai University, Japan (A. Suzuki)
• 1996 – 2006  Assistant Prof., Assoc. Prof, Full Professor and Chair, College of Oriental Medicine, Dongguk University, Gyung-ju
• 1990 – 1996.2 Senior Researcher and Genome Program Head, Genetic Engineering Center, Korea Institute of Science and
Technology KIST (Later, KRIBB)
• 1987.4 – 1989.9 Lecturer, Tokyo College of Pharmaco and Medico-Technology, Tokyo, Japan

 Professional activities
Member:   Korea Society for Molecular and Cellular Biolology, KSBMB, American Society of Biochemistry and Molecular Biology,
Society for Glycobiology, etc.
Editorial: Co-Editor, Current Pharmaceutical Biotechnology (IF 2.8, 2015-present), Editor, The Peer Journal, USA (IF 2.98, 2011– Present), eCAM, Editor (IF 2.8, 2012-present). International Journal of Molecular Science, Molecular Biology Section, Biochemistry Section, Editor (IF 5.9, 2015-present), Frontiers in Pharmacology, Associate Editor (IF, 5.8, 2017-present)
Committee
Member:
Chairman, Bomun Conference Committee of KSBMB (2005-2006), President, KSBMB YeoungNam District Branch (2006-2007), Organizer for "1st to 6th Korea-Japan and Korea-Japan Collaborative Symposium on Glycobiolgoy", 2001. 2. (Taejon),2002.8 (Wako), 2003.3 (Busan), 2004.7 (Wako), 2004. 10 (Daejon), 2005.8.25(Wako). International Scientific Advisory Board Member, International Symposium for Glycosyltransferase (GlycoT 2006), IUBMB symposium, Tsukuba, Japan 2006.6.24-27, Organization Committe for "1st Korea-France Collaborative Symposium on Glycobiolgoy", 2007. 11.31, International Scientific Advisory Board Member, International Symposium for Glycosyltransferase (GlycoT 2008), Emory University, GA, USA, 2008.5.17-22. Korea New Drug Development Research Commision (2008-2012), The 120 Years Celebrating Committee Member, The University of Tokyo Establishment, Tokyo 2013.12.

 Lecture
• 당쇄신호전달 (Glycosignal Transduction): 대학원 대상, 가을 학기

• 분자세포당생물학 (Molecular Cellular Glycogiology): 학부 대상, 가을 학기 
• 분자당쇄생물학 (Glycobioogy): 대학원 대상, 봄 학기
• 질병생물학 (Diseasea Biology): 학부 대상, 봄 학기

 

 People
           

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 박준영 (Dr. Jun Young Park) 이학박사
과정 박사후연구원 (Post-doc)
연구실 분자세포당생물학연구실
전화 031-290-7012
사무실 제2과학관 32103
이메일 wnsdud2057@skku.edu
연구주제 Sialyl-glycolipid biosynthesis and cellular function

               

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아베쿠라 후쿠시                   

과정 석박통합과정
연구실 분자세포당생물학연구실
전화 031-290-7012
사무실 제2과학관 32103
이메일 pokusa6@hotmail.com
연구주제 The functional role of phenolic compound on the innate immune system                           

                    

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임학성

과정 석박통합과정
연구실 분자세포당생물학연구실
전화                         031-290-7012
사무실 제2과학관 32103
이메일 hakseonglim@naver.com
연구주제 The functional role of Siglec-3 in neuronal cells             

                    

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김희도

과정 석박통합과정
연구실                         분자세포당생물학연구실
전화 031-290-7012
사무실 제2과학관 32103
이메일 hdk0330@naver.com
연구주제 The functional role of 3'-sialyllactose in cells

 

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최현주 

과정 석박통합과정
연구실 분자세포당생물학연구실
전화 031-290-7012
사무실 제2과학관 32103
연구주제                         Role of Matrix Metalloproteinase (Blood)


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최연우                  

과정 석사과정
연구실 분자세포당생물학연구실
전화 031-290-7012
사무실 제2과학관 32103
연구주제 Anti-inflammation


                 
 
 Alumni

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 하선형 (Sun Hyung Ha)

 

과정 석박통합과정
연구실 분자세포당생물학연구실
전화 031-290-7012
사무실 제2과학관 32103
이메일 sunspring5@naver.com
연구주제 Sialylglycan biosynthesis and cellular function

 


 

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