Dr. Kok Lian Ho

Dr. Kok Lian Ho

Associate Professor
Universiti Putra Malaysia, Malaysia


Highest Degree
Ph.D. in Structural Biochemistry and Molecular Biology from University of Edinburgh, UK

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Area of Interest:

Biomedical Sciences
100%
Biochemistry
62%
Structural Biology
90%
Molecular Biology
75%
Virology
55%

Selected Publications

  1. Thong, Q.X., R. Biabanikhankahdani, K.L. Ho, N.B. Alitheen and W.S. Tan, 2019. Thermally-responsive virus-like particle for targeted delivery of cancer drug. Scient. Rep., Vol. 9. 10.1038/s41598-019-40388-x.
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  2. Chong, L.C., H. Ganesan, C.Y. Yong, W.S. Tan and K.L. Ho, 2019. Expression, purification and characterization of the dimeric protruding domain of Macrobrachium rosenbergii nodavirus capsid protein expressed in Escherichia coli. PLoS ONE, Vol. 14. 10.1371/journal.pone.0211740.
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  3. Chew, S.Y., K.L. Ho, Y.K. Cheah, T.S. Ng, D. Sandai, A.J. Brown and L.T.L. Than, 2019. Glyoxylate cycle gene ICL1 is essential for the metabolic flexibility and virulence of Candida glabrata. Scient. Rep., Vol. 9. 10.1038/s41598-019-39117-1.
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  4. Thong, Q.X., C.L. Wong, M.K. Ooi, C.L. Kueh, K.L. Ho, N.B. Alitheen and W.S. Tan, 2018. Peptide inhibitors of Macrobrachium rosenbergii nodavirus. J. Gen. Virol., 99: 1227-1238.
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  5. Tan, C.S., M. Hassan, Z.A.M. Hussein, I. Ismail, K.L. Ho, C.L. Ng and Z. Zainal, 2018. Structural and kinetic studies of a novel nerol dehydrogenase from Persicaria minor, a nerol-specific enzyme for citral biosynthesis. Plant Physiol. Biochem., 123: 359-368.
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  6. Rahaman, S.N.A., J.M. Yusop, Z.A. Mohamed-Hussein, W.M. Aizat and K.L. Ho et al., 2018. Crystal structure and functional analysis of human C1ORF123. PeerJ, Vol. 6. 10.7717/peerj.5377.
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  7. Ho, K.L., M. Gabrielsen, P.L. Beh, C.L. Kueh and, Q.X. Thong et al., 2018. Structure of the Macrobrachium rosenbergii nodavirus: A new genus within the Nodaviridae? PLoS Biol., Vol. 16, No. 10. 10.1371/journal.pbio.3000038.
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  8. Gan, B.K., C.Y. Yong, K.L. Ho, A.R. Omar, N.B. Alitheen and W.S. Tan, 2018. Targeted delivery of cell penetrating peptide virus-like nanoparticles to skin cancer cells. Scient. Rep., Vol. 8. 10.1038/s41598-018-26749-y.
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  9. Biabanikhankahdani, R., K.L. Ho, N.B. Alitheen and W.S. Tan, 2018. A dual bioconjugated virus-like nanoparticle as a drug delivery system and comparison with a pH-responsive delivery system. Nanomaterials, Vol. 8, No. 4. 10.3390/nano8040236.
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  10. Ong, H.K., W.S. Tan and K.L. Ho, 2017. Virus like particles as a platform for cancer vaccine development. PeerJ, Vol. 5. 10.7717/peerj.4053.
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  11. Mohd-Sharif, N., S. Shaibullah, V. Givajothi, C.S. Tan and K.L. Ho et al., 2017. Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae. Acta Crystal. Sect. F: Struct. Biol. Commun., 73: 109-115.
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  12. Lim, S.L., C.W. Ooi, W.S. Tan, E.S. Chan, K.L. Ho and B.T. Tey, 2017. Biosensing of hepatitis B antigen with poly(acrylic acid) hydrogel immobilized with antigens and antibodies. Sens. Actuat. B: Chem., 252: 409-417.
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  13. Jinfeng, E.C., M.I.M. Rafi, K.C. Hoon, H.K. Lian and C.Y. Kqueen, 2017. Analysis of chemical constituents, antimicrobial and anticancer activities of dichloromethane extracts of Sordariomycetes sp. endophytic fungi isolated from Strobilanthes crispus. World J. Microbiol. Biotechnol., Vol. 33. 10.1007/s11274-016-2175-4.
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  14. Ho, K.L., C.L. Kueh, P.L. Beh, W.S. Tan and D. Bhella, 2017. Cryo-electron microscopy structure of the Macrobrachium rosenbergii nodavirus capsid at 7 Angstroms resolution. Scient. Rep., Vol. 7, No. 1. 10.1038/s41598-017-02292-0.
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  15. Biabanikhankahdani, R., S. Bayat, K.L. Ho, N.B.M. Alitheen and W.S. Tan, 2017. A simple add-and-display method for immobilisation of cancer drug on his-tagged virus-like nanoparticles for controlled drug delivery. Scient. Rep., Vol. 7. 10.1038/s41598-017-05525-4.
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  16. Rahaman, S.N.A., J.M. Yusop, Z.A. Mohamed-Hussein, K.L. Ho, A.H. Teh, J. Waterman and C.L. Ng, 2016. Cloning, expression, purification, crystallization and X-ray crystallographic analysis of recombinant human C1ORF123 protein. Acta Crystal. Sect. F: Struct. Biol. Commun., 72: 207-213.
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  17. Joseph, N.M., K.L. Ho, B.T. Tey, C.S. Tan, N. Shafee and W.S. Tan, 2016. Production of the virus-like particles of nipah virus matrix protein in Pichia pastoris as diagnostic reagents. Biotechnol. Progr., 32: 1038-1045.
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  18. Chia, J.Y., W.S. Tan, C.L. Ng, N.J. Hu, H.L. Foo and K.L. Ho, 2016. A/T run geometry of B-form DNA is independent of bound Methyl-CpG binding domain, cytosine methylation and flanking sequence. Scient. Rep., Vol. 6. 10.1038/srep31210.
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  19. Chai, K.P., N.F.B. Othman, A.H. Teh, K.L. Ho and K.G. Chan et al., 2016. Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass. Scient. Rep., Vol. 6. 10.1038/srep23126.
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  20. Biabanikhankahdani, R., N.B.M. Alitheen, K.L. Ho and W.S. Tan, 2016. pH-responsive virus-like nanoparticles with enhanced tumour-targeting ligands for cancer drug delivery. Scient. Rep., Vol. 6. 10.1038/srep37891.
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  21. Yong, C.Y., S.K. Yeap, Z.H. Goh, K.L. Ho, A.R. Omar and W.S. Tan, 2015. Induction of humoral and cell-mediated immune responses by hepatitis B virus epitope displayed on the virus-like particles of prawn nodavirus. Applied Environ. Microbiol., 81: 882-889.
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  22. Yong, C.Y., S.K. Yeap, K.L. Ho, A.R. Omar and W.S. Tan, 2015. Potential recombinant vaccine against influenza A virus based on M2e displayed on nodaviral capsid nanoparticles. Int. J. Nanomed., 10: 2751-2763.
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  23. Pang, S.L., K.L. Ho, J. Waterman, A.H. Teh, F.T. Chew and C.L. Ng, 2015. Cloning, expression, purification, characterization, crystallization and X-ray crystallographic analysis of recombinant Der f 21 (rDer f 21) from Dermatophagoides farinae. Acta Crystal. Sect. F: Struct. Biol. Commun., 71: 1396-1400.
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  24. Muhamad, A., K.L. Ho, M.B.A. Rahman, B.A. Tejo, D. Uhrín and W.S. Tan, 2015. Hepatitis B virus peptide inhibitors: Solution structures and interactions with the viral capsid. Org. Biomol. Chem., 13: 7780-7789.
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  25. Tan, W.S. and K.L. Ho, 2014. Phage display creates innovative applications to combat hepatitis B virus. World J. Gastroenterol., 20: 11650-11670.
    PubMed  |  
  26. Shaibullah, S., N. Mohd-Sharif, K.L. Ho, M. Firdaus-Raih, S. Nathan, R. Mohamed and C.L. Ng, 2014. Crystallization and preliminary crystallographic studies of the hypothetical protein BPSL1038 from Burkholderia pseudomallei. Acta Crystal. Sect. F: Struct. Biol. Commun., 70: 1697-1700.
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  27. Yoon, K.Y., W.S. Tan, B.T. Tey, K.W. Lee and K.L. Ho, 2013. Native agarose gel electrophoresis and electroelution: A fast and cost-effective method to separate the small and large hepatitis B capsids. Electrophoresis, 34: 244-253.
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  28. Salvamani, S., Z.H. Goh, K.L. Ho, B.T. Tey and W.S. Tan, 2013. Oligomerization state of the multimerization domain of Nipah virus phosphoprotein. Process Biochem., 48: 1476-1480.
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  29. Muhamad, A., K.L. Ho, M.B.A. Rahman, D. Uhrín and W.S. Tan, 2013. Solution structure and in silico binding of a cyclic peptide with hepatitis B surface antigen. Chem. Biol. Drug Des., 81: 784-794.
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  30. Lee, K.W., B.T. Tey, K.L. Ho, B.A. Tejo and W.S. Tan, 2012. Nanoglue: An alternative way to display cell-internalizing peptide at the spikes of hepatitis B virus core nanoparticles for cell-targeting delivery. Mol. Pharmaceut., 9: 2415-2423.
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  31. Lee, K.W., B.T. Tey, K.L. Ho and W.S. Tan, 2012. Delivery of chimeric hepatitis B core particles into liver cells. J. Applied Microbiol., 112: 119-131.
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  32. Ho, K.L., I.W. McNae, L. Schmiedeberg, R.J. Klose, A.P. Bird and M.D. Walkinshaw, 2008. MeCP2 binding to DNA depends upon hydration at methyl-CpG. Mol. Cell, 29: 525-531.
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  33. Tan, W.S., I.W. McNae, K.L. Ho and M.D. Walkinshaw, 2007. Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension. Acta Crystal. Sect. F: Struct. Biol. Crystal. Commun., 63: 642-647.
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  34. Ho, K.L., K. Yusoff, H.F. Seow and W.S. Tan, 2003. Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. J. Med. Virol., 69: 27-32.
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