Professor NGO Chi Ki Jacky


(Office): Rm E403, Science Centre East Block

(Lab): Rm 118, Run Run Shaw Science Building

People NCK


(Office): (852) 3943 6346

(Lab): (852) 3943 1349

Fax (852) 2603 7246
Email This email address is being protected from spambots. You need JavaScript enabled to view it.
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2006 Ph.D., University of California San Diego
2003 M.Sc., University of California San Diego
2000 B.Sc., University of California San Diego


  •  Associate Professor, School of Life Sciences

Research Interests

  • Determining the structure, function, and mechanism of proteins that involve in the regulation of pre-mRNA splicing using a multidisciplinary approach combining X-ray crystallography and cryo-EM with biochemical and biological studies.
  • Target-based discovery and development of inhibitors for molecular targets in cancers and neurodegenerative diseases; and investigation of the structures and mechanisms of the inhibitors.

Representative Publications

  • Zhang, Q., An, Y., Chen, Z.F.S., Koon, A.C., Lau, K.F., Ngo, J.C.K.*, and Chan, H.Y.E. (2019) A peptidylic inhibitor for neutralizing r(GGGGCC)exp-associated neurodegeneration in C9ALS-FTD. Molecular Therapy Nucleic Acids, 16, 172-185. (*Co-corresponding author)
  • Long, Y., Sou, W.H., Yung, K.W.Y., Liu, H., Wan, S.W.C., Li, Q., Zeng, C., Chan, G.H.C., Law, C.O.K., Lau, T.C.K., Ngo, J.C.K. (2018) Distinct mechanisms govern the phosphorylation of different SR splicing factors. Journal of Biological Chemistry, 294(4), 1312-1327.
  • Li, W., Tam, K.M.V., Chan, W.W.R., Koon, A.C., Ngo, J.C.K., Chan, H.Y.E., and Lau, K.F. (2018) Neuronal adaptor FE65 stimulates Rac1-mediated neurite outgrowth by recruiting and activating ELMO1. Journal of Biological Chemistry, 293, 7674-7688.
  • Hatcher, J.M., Wu, G., Zeng, C., Zhu, J., Meng, F., Patel, S., Wang, W., Ficarro, S.B., Leggett, A.L., Powell, C., Marto, J.A., Zhang, K., Ngo, J.C.K., Fu, X., Zhang, T., and Gray, N. (2018).  SRPKIN-1: A covalent SRPK1/2 inhibitor that potently covers VEGF from pro-angiogenic to anti-angiogenic form. Cell Chemical Biology. 25,460-470.
  • Zhang, Q., Chen, Z.S., An, Y., Liu, Hou, Y., Li, W., Lau, K.F., Koon, A., Ngo, J.C.K.*, and Chan, H.Y.E. (2018). A peptidylic inhibitor for neutralizing expanded CAG RNA-induced nucleolar stress in polyglutamine diseases. RNA. 24(4):486-498. (*Co-corresponding author)
  • Zhang, Q., Yang, M, Sorensen, K.K., Madsen, C.S., Boesen, J.T., An, Y., Peng, S.H., Wei, Y., Jensen, K.J., Zuo, Z.J., Chan, H.Y.E., and Ngo, J.C.K. (2017)  A brain-targeting lapidated peptide for neutralizing RNA-mediated toxicity in polyglutamine disease. Scientific Reports. 7:12077.
  • Lui, M., Lo, C.Y., Wang, G., Chow, H.F., Ngo, J.C.K., Wan, D.C.C., Poon, L.L.M., and Shaw, P.C. (2017). Identification of influenza polymerase inhibitors targeting polymerase PB2 cap-binding domain through virtual screening. Antiviral Research. 144, 186-195.
  • Kromann-Hansen, T., Oldenburg, E., Yung, K.W.Y., Ghassabeh, G.H., Muyldermans, S., Declerck, P.J., Huang, M.D., Andreasen, P.A., and Ngo, J.C.K. (2016). A camelid-derived antibody fragment targeting the active site of a serine protease balances between inhibitor and substrate behaviour. Journal of Biological Chemistry. 291, 15156-15168.
  • Zhang, Q., Tsoi, H., Peng, S., Li, P.P., Lau, K.F., Rudnicki, D.D., Ngo, J.C.K., Chan, H.Y. (2016) A peptidylic inhibitor-based therapeutic approach that simultaneously suppresses RNA- and protein-mediated toxicities in polyglutamine diseases. Dis. Model Mech., 9,321-334.
  • Chow, W.N., Ngo, J.C.K., Li, W., Chen, Y.W., Tam, K.M., Chan, H.Y., Miller, C.C., Lau, K.F. (2015) Phosphorylation of FE65 Ser610 by serum- and glucocorticoid-induced kinase 1 modulates Alzheimer's disease amyloid precursor protein processing. Biochemical Journal. 470, 303-17.
  • Liang, N., Zheng, C., Tao, K.P., Sou, W.H., Hsia, H.P., Qu, D., Lau, S.N., and Ngo, J.C.K. (2014). Primary structural features of SR-like protein AcinusS define the phosphorylation mechanism by SRPK2. Biochemical Journal, 459, 181-191. 
  • Zhao, B., Yuan, C., Li, R., Qu, D., Huang, M., and Ngo, J.C.K. (2013) Crystal structures of matriptase in complex with its inhibitor hepatocyte growth factor activator inhibitor-1. Journal of Biological Chemistry, 288(16); 11155-11164.
  • Yuan, C., Cheng, L., Meehan, E., Daly, N., Craik, D.J., Huang, M., Ngo, J.C.K. (2011) Structure of catalytic domain of Matriptase in complex with Sunflower trypsin inhibitor-1. BMC Structural Biology, 11:30. 
  • Ngo, J.C.K., Jiang, L., Lin, Z., Yuan, Cai., Chen, Z., Zhang, X., Yu, H., Wang, J., Lin, L., Huang, M. (2011). Structural basis for therapeutic intervention of uPA/uPAR system. Current Drug Targets,12(12), 1729-43.
  • Ngo, J.C.K., Huang, M.D., Roth, D.A., Furie, B.C. and Furie, B. (2008) Crystal structure of human factor VIII: Implications for the formation of the factor IXa:factor VIIIa complex. Structure, 16, 597-606.
  • Ngo, J.C.K., Giang, K., Chakrabarti, S.,  Ma, C.T., Huynh, N., Hagopian, J.C., Dorrestein, P.C., Fu, X.D., Adams, J..A. and Ghosh, G. (2008) A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1. Molecular Cell, 29, 563-576.
  • Ngo, J.C.K., Gullingsrud, J., Giang, K., Yeh, M. J., Fu, X.D.,  Adams, J.A., McCammon, J.A. and Ghosh, G. (2007) SR protein kinase 1 is resilient to inactivation. Structure, 15, 123-133.
  • Ngo, J.C.K., Chakrabarti, S., Ding J.H., Velazquez-Dones A., Nolen, B., Aubol, B.E., Adams, J.A., Fu, X.D. and Ghosh, G. (2005) Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2. Molecular Cell, 20, 77-89 (Cover). 

Research Grants

  • 2017-20 RGC General Research Fund; Investigation of the interaction and phosohorylation mechanisums of Hepatitis B virus core protein by SR protein kinase 2 and the roles of their interaction in HBV replication.
  • 2015-17 RGC General Research Fund; Investigation of the different phosphorylation mechanisms of SR proteins by SRPKs.
  • 2011-14 RGC General Research Fund; Regulation and phosphorylation of SR proteins by SRPK2.
  • 2011-13 Research Fund for the Control of Infectious Diseases; Search of inhibitors that target HIV pre-mRNA splicing to overcome drug resistance
  • 2010-12 RGC General Research Fund; Structural and functional studies of SR Protein Kinase 2: A key factor in the regulation of pre-mRNA splicing of cellular and viral proteins.