Joseph Jen-Tse Huang Ph.D.
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Assistant Research Fellow, Institute of Chemistry |
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| Years | Position | Affiliation |
| 2002-2004 | Ph.D. | Dept. of Chem., National Taiwan University, Taiwan |
| 2004-2005 | Institute of Chemistry, Academia Sinica | |
| 2005-2007 | Dept. of Chem., Univ. Wisconsin-Madison, USA | |
| 2007-now | Assistant Research Fellow | Institute of Chemistry, Academia Sinica |
Research interests
Study the aggregation and misfolding of Tar DNA binding protein TDP-43 (TDP43) in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FLD).
Develop fluorescence-based methodologies, such as Forster resonance energy transfer (FRET) or fluorescence anisotropy, to investigate the interactions between nascent peptides and chaperon proteins. Explore the specific interaction between chaperones and protein aggregates and develop potential treatment.
Studies of in vitro protein folding driven by various effect (turn formation, hydrophobic interaction, solvation and etc.) using various biophysical method (including fluorescence technique, CD, NMR, Mass etc.).
In an effort to clarify the physical properties of the C-terminal domain of TDP-43, we have synthesized peptide fragments and shown that only D1 within D1-4 can form twisted fibrils.
(A) PONDR analysis of the full-length TDP-43 (1-414).Calculations use VL3 version of PONDR. EM images of (B) D1, (C) 315T, and (D) G294A incubated in pH 7.0 phosphate buffer at 37℃ for 2 weeks. The scale bars represent 100 nm.
Selected publications
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Chen, K.-H., Lin, Y.-Y., Xie, Z.-J., Tu, P.-H., Chen, P.-Y., Liao, T.-Y., Huang, J.-T.* Induction of Amyloid Fibrils by the C-terminal Fragment of TDP-43 in Amyotrophic Lateral Sclerosis. J. Am. Chem. Soc. 2010, 132, 1186.
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Hwu, J. R. *, Huang, J. J. -T., Tsai, F.-Y., Tsay, S.-C., Hsu, M.-H., Hwamg, K. C., Horng, J.-C., Ho, J. A., Lin, C.-C. Photochemical activities of N-nitroso carboxamides and sulfoximides as well as their application to DNA cleavage. Chem. Eur. J. 2009, 15, 8742-8750.
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Huang, J. J.-T. *, Jhan, J.-W. Ultra-fast and Cotranslational Protein Folding. Natural Sciences Newsletter. 2008, 20, 50-53.
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Kirchdoerfer, R. N.; Huang, J. J.-T.; Isola, M. K.; Cavagnero, Silvia. * Fluorescence-Based Analysis of Aminoacyl- and Petidyl-tRNA by Low-pH SDS PAGE. Anal. Biochem. 2007, 364, 92-94.
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Kuo, N. N.-W., Huang, J. J.-T., Miksovska, J., Chen, P.-Y., Larsen, R., Chan, S.I. * Effects of turn stability on the kinetics of refolding of a hairpin in β-sheet. J. Am. Chem. Soc. 2005, 127, 48, 16945-16954.
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Chan, S. I. *; Huang, J. J.-T.; Larsen, R. W.; Rock, R. S.; Hansen, K. C. Early kinetic events in protein folding: The development and applications of caged peptides in Dynamic Studies in Biology; Goeldner, M. and Givens. R. (eds), Wiley-VCH GmbH & Co. Germany, 2005, pp479-494.
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Chen, R. P. Y., Huang, J. J.-T., Chen, H. L., Jan, H., Velusamy, M., Lee, C. T., Fann, W. S., Larsen, R. W., Chan, S. I. * Measuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale. Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 7305-7310.


