Cheng-Ming Chiang Simmons Comprehensive Cancer Center, Department of Biochemistry, and Department of Pharmacology, University of Texas Southwestern Medical Center, USA
1 protocol

Hsien-Tsung Lai
  • Simmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, USA
  • 1 Author merit


Ph.D., Department of Biology, University of California, San Diego, San Diego State University, 2007

Current position

Postdoctoral Fellow, University of Texas Southwestern Medical Center, Simmons Comprehensive Cancer Center, Mentor: Dr. Cheng-Ming Chiang


  1. Wu, S. Y., Lee, A. Y., Lai, H. T., Zhang, H. and Chiang, C. M. (2013). Phospho switch triggers Brd4 chromatin binding and activator recruitment for gene-specific targeting. Mol Cell 49(5): 843-857.
  2. Kim, M. K., Kang, Y. S., Lai, H. T., Barakat, N. H., Magante, D. and Stumph, W. E. (2010). Identification of SNAPc subunit domains that interact with specific nucleotide positions in the U1 and U6 gene promoters. Mol Cell Biol 30(10): 2411-2423.
  3. Lai, H. T., Kang, Y. S. and Stumph, W. E. (2008). Subunit stoichiometry of the Drosophila melanogaster small nuclear RNA activating protein complex (SNAPc). FEBS Lett 582(27): 3734-3738.
  4. Lai, H. T., Chen, H., Li, C., McNamara-Schroeder, K. J. and Stumph, W. E. (2005). The PSEA promoter element of the Drosophila U1 snRNA gene is sufficient to bring DmSNAPc into contact with 20 base pairs of downstream DNA. Nucleic Acids Res 33(20): 6579-6586.
  5. Lynn, S., Gurr, J. R., Lai, H. T. and Jan, K. Y. (2000). NADH oxidase activation is involved in arsenite-induced oxidative DNA damage in human vascular smooth muscle cells. Circ Res 86(5): 514-519.
  6. Lynn, S., Lai, H. T., Gurr, J. R. and Jan, K. Y. (1997). Arsenite retards DNA break rejoining by inhibiting DNA ligation. Mutagenesis 12(5): 353-358.
  7. Lynn, S., Lai, H. T., Kao, S. M., Lai, J. and Jan, K. Y. (1997). Cadmium inhibits DNA strand break rejoining in methyl methanesulfonate-treated CHO-K1 cells. Toxicol Appl Pharmacol 144(1): 171-176.
1 Protocol published
Bimolecular Fluorescence Complementation (BiFC) Assay for Direct Visualization of Protein-Protein Interaction in vivo
Authors:  Hsien-Tsung Lai and Cheng-Ming Chiang, date: 10/20/2013, view: 7908, Q&A: 0
Bimolecular Fluorescence Complementation (BiFC) assay is a method used to directly visualize protein-protein interaction in vivo using live-cell imaging or fixed cells. This protocol described here is based on our recent paper describing ...