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Ma, Che Alex 馬徹

MaC_6x7副研究員


Email: cma@gate.sinica.edu.tw
Telephone: 02-27871233
[ CV ]

 

EDUCATION AND POSITIONS HELD:

  • B.S., Chemistry, National Taiwan University, 1992
  • M.S., Chemistry, University of Pennsylvania, 1996
  • Ph.D., Chemistry, University of Pennsylvania, 2000
  • Postdoctoral Fellow, University of California at San Diego, 2001
  • Postdoctoral Fellow, The Scripps Research Institute, 2001–2004
  • Assistant Research Fellow, Genomics Research Center, Academia Sinica, Taiwan, 2004-2010
  • Associate Research Fellow, Genomics Research Center, Academia Sinica, Taiwan, 2010- present

HONORS:

  • University of Pennsylvania, Teaching Assistant Award, 1995
  • Keystone Symposia Scholarship, Frontiers of Structural Biology, 2003
  • The Skaggs Postdoctoral Fellowship, 2001–2003
  • TWAS Young Affiliate, 2009-2013
  • Academia Sinica Significant Research Achievements, 2009
  • Academia Sinica Research Award for Junior Research Investigators, 2010
  • Two research highlights in Taiwan Yearbook of Technology, 2010
  • The Young Scholar Award of Tien-De Li Biomedical Foundation, 2011

RESEARCH INTERESTS:

Structure of membrane proteins in drug discovery

The research focus of our laboratory is to study the structure and function of membrane proteins, and to understand their relationships in human diseases. Major efforts have been made over the last few years into the two topics in infectious diseases. First, in order to overcome the problems of drug-resistant bacterial infection, a new enzyme target for antibiotic development, the membrane-bound bifunctional transglycosylase, has been chosen for structural and functional analysis. We have successfully determined the X-ray crystal structure of this membrane-bound enzyme in complex with its inhibitor moenomycin, and studied its mechanism of peptidoglycan synthesis. In addition, a high-throughput screening method for finding new antibiotics has been developed using the purified full-length membrane protein. In parallel, structure-based drug design with our crystal structure is ongoing. Second, we have studied the effect of glycosylation on influenza virus major surface protein hemagglutinin (HA) with regards to its role in receptor binding and immune response, and developed a new strategy for molecular vaccine design.

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Structure of PBP1b-moenomycin complex provides critical information for new antibiotic development.

膜蛋白結構生物學與新藥研發

我們的研究重點是使用x光結晶學以及核磁共振光譜學來探討膜蛋白的結構。膜蛋白是使細胞能夠正常運作的重要組成之一,它們負責細胞內外像是離子傳導、分子傳輸、以及訊息接受等等的重要工作。膜蛋白的正常運作對於我們的健康非常重要,異常的膜蛋白與許多嚴重疾病有密切的關係。我們希望運用x光結晶學來決定具有醫療重要性的膜蛋白之結構。核磁共振光譜學將有助於針對這些結構的新藥開發。

RESEARCH HIGHLIGHTS:

SELECTED PUBLICATIONS:

  • Chia-Ying Huang, Hao-Wei Shih, Li-Ying Lin, Yi-Wen Tien, Ting-Jen Rachel Cheng, Wei-Chieh Cheng, Chi-Huey Wong*, and Che Ma*, 2012, “Crystal structure of Staphylococcus aureus transglycosylase in complex with a lipid II analog and elucidation of peptidoglycan synthesis mechanism”, Proceedings of the National Academy of Sciences of the United States of America, 109(17), 6496-6501. (SCI)
  • Chen JR, Ma C, Wong CH, 2011, “Vaccine design of hemagglutinin glycoprotein against influenza.”, Trends in biotechnology, 29, 426-434. (SCI)
  • M.-T. Sung, Y.-T. Lai, C.-Y. Huang, L.-Y. Chou, H.-W. Shih, W.-C. Cheng, C.-H. Wong and C. Ma*, 2009, “Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli”, Proceedings of the National Academy of Sciences of the United States of America, 106, 8824-8829. (SCI)
  • C.-C. Wang, J.-R. Chen, Y.-C. Tseng, C.-H. Hsu, Y.-F. Hung, S.-W. Chen, C.-M. Chen, K.-H. Khoo, T.-J. Cheng, Y.-S. E. Cheng, J.-T. Jan, C.-Y. Wu, C. Ma* and C.-H. Wong, 2009, “Glycans on influenza hemagglutinin affect receptor binding and immune response”, Proceedings of the National Academy of Sciences of the United States of America, 106, 18137-18142. (SCI)
  • T.-J. R. Cheng, M.-T. Sung, H.-Y. Liao, Y.-F. Chang, C.-W. Chen, C.-Y. Huang, L.-Y. Chou, Y.-D. Wu, Y.-H. Chen, Y.-S. E. Cheng, C.-H. Wong, C. Ma* and W.-C. Cheng, 2008, “Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics”, Proceedings of the National Academy of Sciences of the United States of America, 105, 431-436. (SCI)
  • Z. G. Zhang, C. Ma, O. Pornillos, X. Xiu, G. Chang and M. H. Saier, Jr., 2007, “Functional characterization of the heterooligomeric EbrAB multidrug efflux transporter of Bacillus subtilis”, Biochemistry, 46, 5218-5225.
  • Y. J. Chen, O. Pronillos, S. Lieu, C. Ma, A. P. Chen and G. Chang, 2007, “X-ray structure of EmrE supports dual topology model”, Proceedings of the National Academy of Sciences of the United States of America, 104, 18999-19004. (SCI)
  • C. Ma and G. Chang, 2004, “Crystallography of the integral membrane protein EmrE from Escherichia coli”, Acta Crystallogr. D: Biol. Crystallogr., 60, 2399-2402. (SCI)
  • G. Veglia, A. C. Zeri, C. Ma and S. J. Opella, 2002, “Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins”, Biophys. J., 82, 2176-2183. (SCI)
  • C. Ma, F. M. Marassi, D. H. Jones, S. K. Straus, S. Bour, K. Strebel, U. Schubert, M. Oblatt-Montal, M. Montal and S. J. Opella, 2002, “Expression, purification, and activities of full-length and truncated versions of the integral membrane protein Vpu from HIV-1”, Protein Sci., 11, 546-557. (SCI)
  • C. Ma and S. J. Opella, 2000, “Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy”, J. Magn. Reson., 146, 381-384. (SCI)