Biography

Dr. Tai-huang Huang

Institute of Biomedical Sciences

Academia Sinica, China, Taiwan

Distinguished Research Fellow


Email: [email protected], [email protected]


Qualifications

1979 Ph.D., Brandeis University,Physics

1969 M.Sc., M.I.T., Nat'l Magnet Lab


Publications (Selected)

  1. Mandar T. Naik , Nandita Naik, Camy C.-H. Kung, Tai-Huang Huang “NMR residual dipolar couplings investigation in the topology of house dust mite Group V allergens” J. Structural Biology V 216, Issue 4, Dec 2024, 108138 (https://doi.org/10.1016/j.jsb.2024.108138) 1
  2. Chiu, H. W., Chou, C. L., Lee, K. T., Shih, C. C., Huang, T. H., & Sung, L. C. (2024). Nattokinase attenuates endothelial inflammation through the activation of SRF and THBS1. International journal of biological macromolecules, 268(Pt 2), 131779. https://doi.org/10.1016/j.ijbiomac.2024.131779
  3. Mälarstig, A., Grassmann, F., Dahl, L., Dimitriou, M., McLeod, D., Gabrielson, M., Smith-Byrne, K., Thomas, C. E., Huang, T. H., Forsberg, S. K. G., Eriksson, P., Ulfstedt, M., Johansson, M., Sokolov, A. V., Schiöth, H. B., Hall, P., Schwenk, J. M., Czene, K., & Hedman, Å. K. (2023). Evaluation of circulating plasma proteins in breast cancer using Mendelian randomisation. Nature communications, 14(1), 7680. https://doi.org/10.1038/s41467-023-43485-8
  4. Suresh, S., Rabbie, R., Garg, M., Lumaquin, D., Huang, T. H., Montal, E., Ma, Y., Cruz, N. M., Tang, X., Nsengimana, J., Newton-Bishop, J., Hunter, M. V., Zhu, Y., Chen, K., de Stanchina, E., Adams, D. J., & White, R. M. (2023). Identifying the Transcriptional Drivers of Metastasis Embedded within Localized Melanoma. Cancer discovery, 13(1), 194–215. https://doi.org/10.1158/2159-8290.CD-22-0427
  5. Chen, T. S., Huang, T. H., Lai, M. C., & Huang, C. W. (2023). The Role of Glutamate Receptors in Epilepsy. Biomedicines, 11(3), 783. https://doi.org/10.3390/biomedicines11030783
  6. Chen, L., Zhang, Z., Han, Q., Maity, B. K., Rodrigues, L., Zboril, E., Adhikari, R., Ko, S. H., Li, X., Yoshida, S. R., Xue, P., Smith, E., Xu, K., Wang, Q., Huang, T. H., Chong, S., & Liu, Z. (2023). Hormone-induced enhancer assembly requires an optimal level of hormone receptor multivalent interactions. Molecular cell, 83(19), 3438–3456.e12. https://doi.org/10.1016/j.molcel.2023.08.027
  7. Li, G., Chen, H., Shen, F., Smithson, S. B., Shealy, G. L., Ping, Q., Liang, Z., Han, J., Adams, A. C., Li, Y., Feng, D., Gao, B., Morita, M., Han, X., Huang, T. H., Musi, N., & Zang, M. (2023). Targeting hepatic serine-arginine protein kinase 2 ameliorates alcohol-associated liver disease by alternative splicing control of lipogenesis. Hepatology (Baltimore, Md.), 78(5), 1506–1524. https://doi.org/10.1097/HEP.0000000000000433
  8. Katsumura, S., Siddiqui, N., Goldsmith, M. R., Cheah, J. H., Fujikawa, T., Minegishi, G., Yamagata, A., Yabuki, Y., Kobayashi, K., Shirouzu, M., Inagaki, T., Huang, T. H., Musi, N., Topisirovic, I., Larsson, O., & Morita, M. (2022). Deadenylase-dependent mRNA decay of GDF15 and FGF21 orchestrates food intake and energy expenditure. Cell metabolism, 34(4), 564–580.e8. https://doi.org/10.1016/j.cmet.2022.03.005
  9. Weiss, J. M., Hunter, M. V., Cruz, N. M., Baggiolini, A., Tagore, M., Ma, Y., Misale, S., Marasco, M., Simon-Vermot, T., Campbell, N. R., Newell, F., Wilmott, J. S., Johansson, P. A., Thompson, J. F., Long, G. V., Pearson, J. V., Mann, G. J., Scolyer, R. A., Waddell, N., Montal, E. D., … White, R. M. (2022). Anatomic position determines oncogenic specificity in melanoma. Nature, 604(7905), 354–361. https://doi.org/10.1038/s41586-022-04584-6
  10. Baggiolini, A., Callahan, S. J., Montal, E., Weiss, J. M., Trieu, T., Tagore, M. M., Tischfield, S. E., Walsh, R. M., Suresh, S., Fan, Y., Campbell, N. R., Perlee, S. C., Saurat, N., Hunter, M. V., Simon-Vermot, T., Huang, T. H., Ma, Y., Hollmann, T., Tickoo, S. K., Taylor, B. S., … White, R. M. (2021). Developmental chromatin programs determine oncogenic competence in melanoma. Science (New York, N.Y.), 373(6559), eabc1048. https://doi.org/10.1126/science.abc1048
  11. Xu, Y., Carrascosa, L. C., Yeung, Y. A., Chu, M. L., Yang, W., Djuretic, I., Pappas, D. C., Zeytounian, J., Ge, Z., de Ruiter, V., Starbeck-Miller, G. R., Patterson, J., Rigas, D., Chen, S. H., Kraynov, E., Boor, P. P., Noordam, L., Doukas, M., Tsao, D., Ijzermans, J. N., … Chaparro-Riggers, J. (2021). An Engineered IL15 Cytokine Mutein Fused to an Anti-PD1 Improves Intratumoral T-cell Function and Antitumor Immunity. Cancer immunology research, 9(10), 1141–1157. https://doi.org/10.1158/2326-6066.CIR-21-0058
  12. Huang, T. H., Wang, P. W., Yang, S. C., Chou, W. L., & Fang, J. Y. (2018). Cosmetic and Therapeutic Applications of Fish Oil's Fatty Acids on the Skin. Marine drugs, 16(8), 256. https://doi.org/10.3390/md16080256
  13. Sofia S. Mariasina, Olga A. Petrova, Ilya A. Osterman, Sergey V. Efimov, Vladimir V. Klochkov, Petr V. Sergiev, Olga A. Dontsova, Tai-huang Huang, Chi-Fon Chang, and Vladimir I. Polshakov (2018) “NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome" Biomolecular NMR assignments (May, 2018) doi: 10.1007/s12104-018-9827-2 2
  14. Li, C. W., Lim, S. O., Chung, E. M., Kim, Y. S., Park, A. H., Yao, J., Cha, J. H., Xia, W., Chan, L. C., Kim, T., Chang, S. S., Lee, H. H., Chou, C. K., Liu, Y. L., Yeh, H. C., Perillo, E. P., Dunn, A. K., Kuo, C. W., Khoo, K. H., Hsu, J. L., … Hung, M. C. (2018). Eradication of Triple-Negative Breast Cancer Cells by Targeting Glycosylated PD-L1. Cancer cell, 33(2), 187–201.e10. https://doi.org/10.1016/j.ccell.2018.01.009
  15. Huang, T. -H. (2017) Unraveling the packaging mechanism of coronavirus ribonucleocapsid “ J. Human VIrol. Ritrovirol. 5(2): 00148. DOI: 10.15406/jhvrv.2017.05.00148. 3
  16. Mandar T. Naik, Mooseok Kang, Chun-Chen Ho, Pei-Hsin Liao, Yung-Lin Hsie, Nandita M. Naik, Szu-Huan Wang, Iksoo Chang*, Hsiu-Ming Shih*, Tai-Huang Huang 1,*(2017) “Molecular mechanism of K65 acetylation-induced attenuation of Ubc9 and the NDSM interaction” Sci. Rep. 7:17391 | DOI:10.1038/s41598-017-17465’ Dec 12 (http://rdcu.be/A7N1) 4
  17. Ching-Yu Chou, Mouna Abdesselem, Cedric Bouzigues, Minglee Chu, Angelo Guiga, Tai-Huang Huang, Fabien Ferrage, Thierry Gacoin, Antigoni Alexandrou, Dimitris Sakellariou (2017) “Ultra-wide range field-dependent measurements of the relaxivity of Gd1-xEuxVO4 nanoparticle contrast agents using a mechanical sample-shuttling relaxometer” Sci. Rep. Mar 20;7:44770. doi: 10.1038/srep44770. 5
  18. Chou, C.Y., Chu, M• Chang, C.F., Yu4, T, Huang, T.H., Sakellariou, D. (2016) “High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe” J Biomol NMR 66:187–194 (DOI 10.1007/s10858-016-0066-5) 6
  19. Chang CK, Huang TH.* (2016) “Untangling the structure of the TDP-43 N-terminal domain.” FEBS J. 2016 Apr;283(7):1239-41. doi: 10.1111/febs.13676. Epub 2016 Feb 27. 7
  20. Huang, T.-h. (2015) “Probing the Molecular Basis of SUMO-Mediated Signaling Pathway by NMR” Chinese J. Magn. Resonance.  32 (2): 163-180. 8
  21. Huang, S.Y.,Chang, C.F.,Fang, P.J., Naik, M.T.,Güntert, P. Shih, H.M., and Huang, T.-h.*(2015)“NMR structure note: The RING domain of human promyelocytic leukemia protein (PML)” J. Biomol. NMR (2015)61 (2), 173-180.
  22. Huang, S.Y., Naik, M.T.,Chang, C.F.,Fang, P.J., Wang, Y.H., Shih, H.M., and Huang, T.-h.* “NMR structure note: The B-box 1 dimer of human promyelocytic leukemia protein” J. Biomol. NMR,, (2014) 60, 275-281.
  23. Chang, C.K., Hou, M. H., Chang, C.F., Hsiao, C.D. and Huang, T.-h.* (2014) “The SARS Coronavirus Nucleocapsid Protein – Forms and Functions” Antiviral Res.103:39-50.
  24. Kung, C.C.H., Nail, M.T., Wang, S.H. Shih, H.M. Chang, C.C., Lin, L.Y. Chen, Ma, C., Chang, C.-F. and Huang, .T.-h.* (2014) “Structural Analysis of Poly-SUMO Chain Recognition by RNF4-SIMs Domain” Biochem. J.462(1):53-65.
  25. Li, Y.-C., Chang, C.-K., Chang, C.F.,Cheng, Y.H., Fang, P.R., Yu, T., Chen, S.C.,Hsiao, C.D.* andHuang, T.-h.* (2014) “Structural dynamics of two-component response regulatorRstA fromKlebsiella pneumoniaein recognition of promoter DNA element”. Nucleic Acid Res. 42 (13), 8777-8788
  26. Hsueh, K.L. Yu, L.K., Chen, Y.H., Cheng, Y.H., Hsieh, Y.C., Ke, S.C., Hung, K.W., Chen, C.J. and Huang, T.-h.* (2013) “FeoC fromKlebsiella pneumoniaecontains a [4Fe-4S] cluster”J. Bacteriol. 195(20): 4726-4734.
  27. Lo, Y.S., Lin, S.Y., Wang, S.M., Wang, C.T., Chiu, Y.L., Huang, T.-h. and Hou, M.H.* (2013) “Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid” FEBS Lett. 587 (2), 120-127
  28. Hsieh, Y.L., Kuo, H.Y., Naik, M.T., Chang, C.C., Liao, P.H., Ho, C.C., Huang, T.C., Jeng, J.C., Hsu, P.H., Tsai, M.D., Huang, T.-h. and Shih, S.H.* (2013) “Ubc9 acetylation modulates distinct SUMO target modification and hypoxia response”. EMBO J. 32, 791-804.
  29. Chang, C.K., Chiang, M.H., Toh, E.K.-W., Chang, C.F. and Huang, T.-h.* (2013) “Molecular mechanism of oxidation-induced trans-activating response region DNA-binding protein of 43 kDa (TDP-43) aggregation and loss of function” FEBS Lett. 587 (6), 575-582
  30. Chen, I.J., Yuann, J.M., Chang, Y.M., Lin, S.Y., Zhao, Perlman, S., Shen, Y.Y., Huang, T.-h.; Hou, M.H.* (2013) “Crystal structure-based exploration of the important role of Arg106 in the RNA-binding domain” of human coronavirus OC43 nucleocapsid protein” Biochimica et Biophysica Acta – Proteins and Proteomics 1834(6): 1054-1062.
  31. Chang, C.K., Chen, C.M., Chiang, M.H.. Hsu, Y.L.,Chang, C.F. and Huang., T.-h.*  (2013) “Transient Oligomerization of the SARS-CoV N Protein – Implication for virus ribonucleoprotein packaging”, PLoS ONE 8 (5) e65045, doi:10.1371/journal.pone.0065045.
  32. Hung, K.W., Tsai, J.Y., Juan, T.H., Hsu, Y.L., Hsiao, C.D.* and Huang, T.H.* (2012) “Crystal structure ofKpNFeoB/KpFeoC complex and the roles of FeoC in the regulation ofFe2+transport by the bacterial Feo system”. J. Bacteriology, 194(23), 6518-26.
  33. Chou, C,-Y. Chu, M. Chang, C.-F. Huang, T.-h.* (2012)“A compact high-speed mechanical sample shuttle for field-dependent high-resolution solution NMR” J. Magn. Resonance 214(1), 302-308).
  34. Sekiyama, N., Jee, J., Isogai, S., Akagi, K.I., Huang, T.-h., Ariyoshi, M., Tochio, H. and Shirakawa, M.* (2012) “NMR analysis of Lys63-linked polyubiquitin recognition by the tandem ubiquitin-interacting motifs of Rap80.”J Biomol NMR. 52(4), 339-350.
  35. Hung, K.W., Juan, T.H., Hsu, Y.L. and Huang, T.-h.* (2012) “NMR structure note: The ferrous iron transport protein C (FeoC) fromKlebsiella pneumoniae” J. Biomol. NMR 53 (2) 161-165.
  36. Chang, C.K., Wu, T.H., Wu, C.Y., Chiang, M.H., Toh, E.K.W., Hsu, Y.C., Lin, K.F., Liao, Y.H., Huang, T.-h*., Huang, J.J.T.* (2012) “The effect of theN-terminus on the oligomerization process and DNA binding affinity of TDP-43” Biochem. Biophys. Res. Comm. 425 (2), 219-224.
  37. Wang, C.H., Davamani, F., Sue, S.C., Lee, S.C., Wu, P.L.., Tang, F.M., Shih, C., Huang, T.-h.* and Wu*, W.G. (2011) “Cell surface heparan sulfates mediate internalization of PWWP/HATH domain of HDGFviamacropinocytosis to fine-tune cell signaling process involved in fibroblast cell migration”,  Biochem. J.433(1), 127-138.
  38. Chang, C.C., Naik, M.T., Huang, Y.S., Jeng, J.C., Liao, P.H., Kuo, H.Y., Ho, C.C., Hsieh, Y.L., Lin, C.H., Huang, N.J., Naik, N.M., Kung, C.C.H., Lin, S.Y., Chen, R.H., Chang, K.S., Huang, T.-h.*, and Shih, H.M.* (April, 2011) “Structural and functional roles of Daxx SIM phosphorylation in SUMO paralogue-selective binding and apoptosis modulation” Mol. Cell, 42(1), 62-74.
  39. Brautigam*, C. A. Wynn, R. M., Chuang, J. L., Naik3, M.T., Young, B.B., Huang, T.-h. and Chuang, D.T.* (2011) “Structural and Thermodynamic Basis for Weak Interactions between Dihydrolipoamide Dehydrogenase and Subunit-binding Domain of the Branched-chain α-Ketoacid Dehydrogenase Complex”J. Biol. Chem. 286(26): 23476- 23488
  40. Jiang, I., Tsai, C.-K., Chen, S.C., Wang, S., Amiraslanov, I., Chang, C.F., Wu, W.J., Tai, J.H., Liaw, Y.C.* and Huang, T.-h*. (2011) “Molecular basis of the recognition of the ap65-1 gene transcription promoter elements by a Myb protein from the protozoan parasiteTrichomonasvaginalis”Nucleic Acid Res. 39(20), 8992-9008.
  41. Hung, K.W., Chang, Y.W., Eng, E.T., Chen, J.H., Chen, Y.C., Sun, Y.J., Hsiao, C.D.*, Dong, G., Spasov, K.A., Unger, V.M., & Huang, T.-h.* (Jun, 2010) “Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB” J. Struct. Biol. 170(3), 501-512
  42. Fang, H. J., Chen, Y. Z., Li, M. S.*,Wu, M. C.*,Chang, C. L., Chang, C. K., Hsu, Y. L., Huang, T. -h.*, Chen, H. M., Tsong, T. Y.*, Hu, C. K.* (2009) “Thermostability of the N-terminal RNA-binding domain of the SARS-CoV nucleocapsid protein: Experiments and numerical simulations” Biophys. J. 96(5):1892-901.
  43. Chang, C.K., Hsu, Y.L., Chang, Y.H., Chao, F.A., Wu, M.C., Huang, Y.S., Hu, C.K., Huang, T.-h.* (2009) “Multiple Nucleic Acid Binding Sites and Intrinsic Disorder of Severe Acute Respiratory Syndrom Coronavirus Nucleocapsid Protein: Implication for Ribonucleocapsid Protein Packaging”, J. Virol. 83: 2255-2264
  44. Naik, M.T., Chang, C.F., Kuo, I.C., Kung, C.C.H., Chua, K.Y.* and Huang, T.-h.*(2008) “Roles of structure and structural dynamics in the antibody recognitio04n of the allergen proteins: A NMR study onBlomia tropicalismajorallergen” Structure 16, 125-136.
  45. Takeda, M., Chang, C.K., Ikeya, T. Güntert, P., Chang, Y.S., Hsu, Y.L., Huang, T.-h.*, and Kainosho, M.* (2008) “Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method” J. Mol. Biol. 380, 608-622.


Personal Website:

http://www.ibms.sinica.edu.tw/pages/pi/index.php?id=33
https://www.researchgate.net/scientific-contributions/Tai-Huang-Huang-39036122

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