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Kwangseog Ahn

School of Biological Sciences, Seoul National University, Seoul, Korea; Center for RNA Research, Institute for Basic Science, Korea

Personal information

Education

Ph.D. in Cell Biology, Department of Physiology and Biophysics, University of Illinois at Urbana-Champaign, 1994

Current position

Professor in Immunology, School of Biological Sciences, Seoul National University, Seoul, Republic of Korea

Publications (since 2006)

  1. Choi, J., Ryoo, J., Oh, C., Hwang, S. and Ahn, K. (2015). SAMHD1 specifically restricts retroviruses through its RNase activity. Retrovirology 12: 46.
  2. Kim, S., Seo, D., Kim, D., Hong, Y., Chang, H., Baek, D., Kim, V. N., Lee, S. and Ahn, K. (2015). Temporal Landscape of MicroRNA-Mediated Host-Virus Crosstalk during Productive Human Cytomegalovirus Infection. Cell Host Microbe 17(6): 838-851.
  3. Ryoo, J., Choi, J., Oh, C., Kim, S., Seo, M., Kim, S. Y., Seo, D., Kim, J., White, T. E., Brandariz-Nunez, A., Diaz-Griffero, F., Yun, C. H., Hollenbaugh, J. A., Kim, B., Baek, D. and Ahn, K. (2014). The ribonuclease activity of SAMHD1 is required for HIV-1 restriction. Nat Med 20(8): 936-941.
  4. Lee, S., Song, J., Kim, S., Kim, J., Hong, Y., Kim, Y., Kim, D., Baek, D. and Ahn, K. (2013). Selective degradation of host MicroRNAs by an intergenic HCMV noncoding RNA accelerates virus production. Cell Host Microbe 13(6): 678-690.
  5. Cho, S., Kim, B. Y., Ahn, K. and Jun, Y. (2013). The C-terminal amino acid of the MHC-I heavy chain is critical for binding to Derlin-1 in human cytomegalovirus US11-induced MHC-I degradation. PLoS One 8(8): e72356.
  6. Kim, Y., Lee, S.*, Kim, S.*, Kim, D., Ahn, J. H. and Ahn, K. (2012). Human cytomegalovirus clinical strain-specific microRNA miR-UL148D targets the human chemokine RANTES during infection. PLoS Pathog 8(3): e1002577.
  7. Kim, S., Lee, S., Shin, J., Kim, Y., Evnouchidou, I., Kim, D., Kim, Y. K., Kim, Y. E., Ahn, J. H., Riddell, S. R., Stratikos, E., Kim, V. N. and Ahn, K. (2011). Human cytomegalovirus microRNA miR-US4-1 inhibits CD8(+) T cell responses by targeting the aminopeptidase ERAP1. Nat Immunol 12(10): 984-991.
  8. Jun, Y. and Ahn, K. (2011). Tmp21, a novel MHC-I interacting protein, preferentially binds to Beta2-microglobulin-free MHC-I heavy chains. BMB Rep 44(6): 369-374.
  9. Cho, S., Ryoo, J., Jun, Y. and Ahn, K. (2011). Receptor-mediated ER export of human MHC class I molecules is regulated by the C-terminal single amino acid. Traffic 12(1): 42-55.
  10. Cho, K., Cho, S., Lee, S. O., Oh, C., Kang, K., Ryoo, J., Lee, S., Kang, S. and Ahn, K. (2011). Redox-regulated peptide transfer from the transporter associated with antigen processing to major histocompatibility complex class I molecules by protein disulfide isomerase. Antioxid Redox Signal 15(3): 621-633.
  11. Lee, S. O., Cho, K., Cho, S., Kim, I., Oh, C. and Ahn, K. (2010). Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation. EMBO J 29(2): 363-375.
  12. Kim, E., Kwak, H. and Ahn, K. (2009). Cytosolic aminopeptidases influence MHC class I-mediated antigen presentation in an allele-dependent manner. J Immunol 183(11): 7379-7387.
  13. Lee, S., Park, B., Kang, K. and Ahn, K. (2009). Redox-regulated export of the major histocompatibility complex class I-peptide complexes from the endoplasmic reticulum. Mol Biol Cell 20(14): 3285-3294.
  14. Kang, K., Park, B., Oh, C., Cho, K. and Ahn, K. (2009). A role for protein disulfide isomerase in the early folding and assembly of MHC class I molecules. Antioxid Redox Signal 11(10): 2553-2561.
  15. Kim, Y., Kang, K., Kim, I., Lee, Y. J., Oh, C., Ryoo, J., Jeong, E. and Ahn, K. (2009). Molecular mechanisms of MHC class I-antigen processing: redox considerations. Antioxid Redox Signal 11(4): 907-936.
  16. Kim, Y., Park, B., Cho, S., Shin, J., Cho, K., Jun, Y. and Ahn, K. (2008). Human cytomegalovirus UL18 utilizes US6 for evading the NK and T-cell responses. PLoS Pathog 4(8): e1000123.
  17. Park, B., Lee, S., Kim, E., Cho, K., Riddell, S. R., Cho, S. and Ahn, K. (2006). Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127(2): 369-382.
  18. Shin, J., Park, B., Lee, S., Kim, Y., Biegalke, B. J., Kang, S. and Ahn, K. (2006). A short isoform of human cytomegalovirus US3 functions as a dominant negative inhibitor of the full-length form. J Virol 80(11): 5397-5404.