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Lin, Ta-Hsien
  • Education: PhD. Chemistry, University of California, San Diego
  • Office: B-15, Chi-Ten Building, Taipei Veterans General Hospital
  • Phone: 886-2-28712121 ext.2703
  • Personal Web Site:
  • Research
    • • Ubiquitination and deubiquitination play a critical role in protein homeostasis and have been linked to human diseases such as cancer. Deubiquitination is performed by deubiquitinating enzymes (DUBs), also known as deubiquitinases. Ubiquitin specific protease (USP) is family of deubiquitinases. It has been reported that UPS is a potential drug target. We are interested in structure-based rational design of USP inhibitors.
    • • Alzheimer’s disease is thought to be associated with aggregation of β-amyloid peptide (Aβ). The aggregation process of Aβ involves conformational changes, suggesting that the structural property and conformational stability play an important role in Aβ aggregation. It has been shown that genetically mutated Aβ, which cause early-onset familial Alzheimer’s disease (FAD), are more prone to aggregation than wild-type Aβ, suggesting that genetic mutation might alter the structural property and conformational stability of Aβ. Currently, we are investigating the effect of genetic mutation on Aβ structure and the mechanism of Aβ-lipid interaction. Study of the effect of Aβ structure on its aggregation behavior may help us gain more insight into Aβ aggregation mechanism from the structural point of view.
    • • Human apolipoprotein E (apoE) has been known to play a key role in the transport of plasma cholesterol and lipoprotein metabolism. It is also highly associated with late-onset familial and sporadic Alzheimer’s disease (AD). ApoE has three major isoforms, apoE2, apoE3, and apoE4. The three isoforms differ from one another only by one or two amino acids, but have markedly differences in their biological functions. The lipid- and receptor-binding abilities of apoE are isoform-specific, suggesting that structural characteristics of apoE isoforms might play important roles in their functions. We are interested in the structure-functional relationship of apoE isoforms.
    • • Protein phosphatase 1 (PP1) is one of the major serine/threonine eukaryotic protein phosphatases. It plays a critical role in the regulation of various cellular functions, including carbohydrate metabolism, protein synthesis, cell cycle, muscle contraction and neuronal signaling. The catalytic subunit of PP1 in cells is associated with different binding proteins to form a variety of holoenzymes. These binding proteins may target the enzyme to specific subcellular compartments in which PP1 regulates the functions of its substrates. The catalytic subunit of PP1 is specifically regulated by three protein inhibitors, inhibitor-1, DARPP-32 (dopamine and cAMP-regulated phosphoprotein of apparent Mr 32,000) and inhibitor-2. The inhibition of PP1 is regulated through phosphorylation of these protein inhibitors. Our goal is to understand the molecular mechanisms of PP1 regulation from the structural point of view.
    • Chu-Ting Liang, Yu-Shan Lin, Yi-Choang Huang, Hsien-Lu Huang, Jia-Qian Yang, Tsung-Hsien Wu, Chi-Fon Chang, Shing-Jong Huang, Hsien-Bin Huang* & Ta-Hsien Lin* Characterization of the interactions between inhibitor-1 and recombinant PP1 by NMR spectroscopy, 2018, Scientific reports, 8, Article number: 50.


    • Chun-Tien Kuo, Yi-Lin Chen, Wei-Tse Hsu, Su-Chun How, Yu-Hong Cheng, Shu-Shun Hsueh, Hwai-Shen Liu, Ta-Hsien Lin, Josephine W. Wu*, Steven S.-S. Wang* Investigating the effects of erythrosine B on amyloid fibril formationderived from lysozyme, 2017, International Journal of Biological Macromolecules, 98, 159–168.


    • Chu-Ting Liang, Hsien-Bin Huang, Chih-Ching Wang, Yi-Ru Chen, Chi- Fon Chang, Ming-Shi Shiao, Yi-Cheng Chen*, Ta-Hsien Lin* L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment, 2016, PLOS ONE, 11, e0154327.


    • Chi-Jen Lo, Chih-Ching Wang, Hsien-bin Huang, Chi-Fon Chang, Ming-Shi Shiao, Yi-Cheng Chen* and Ta-Hsien Lin* Arctic mutation accelerates Aβ aggregation in SDS through reducing the helical propensity of residues 15-25, 2015, Amyloid, 22, 8-18.


    • Yu-Jun Hu, Deli Irene, Chi-Jen Lo, Yong-Liang Cai, T.-C. Tzen, Ta-Hsien Lin and Chia-Lin Chyan*, Resonance assignments and secondary structure of a phytocystatin from Sesamum indicum, 2015, Biomol. NMR Assign., 9, 309-311.


    • Chi-Jen Lo, Chia-Lin Chyan, Yi-Chen Chen, Chi-Fon Chang, Hsien-bin Huang* and Ta-Hsien Lin*, Resonance assignments and secondary structure of apolipoprotein E C-terminal domain in DHPC micelles, 2015, Biomol. NMR Assign., 9, 187-190.


    • Chih-Kai Chang, Wei-An Chen, Chao-Yu Sie, Shen-Chieh Lin, Lilian Tsai-Wei Lin, Ta-Hsien Lin, Cheng-Che Hsu*, Steven S.-S. Wang* Investigating the effects of plasma pretreatment on the formation of ordered aggregates of lysozyme, 2015, Colloids and Surfaces B: Biointerfaces, 126, 154–161.


    • Deli Irene, Fu-Hsing Sung, Jian-Wen Huang, Ta-Hsien Lin, Yi-chen Chen and Chia-Lin Chyan* Resonance assignments and secondary structure of calmodulin in complex with its target sequence in rat olfactory cyclic nucleotide-gated ion channel, 2014, Biomol. NMR Assign., 8, 97-102.


    • Shu-Hsiang Huang, Shyue-Chu Ke, Ta-Hsien Lin, Hsin-Bin Huang, Yi-Cheng Chen* Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation, 2014, PLOS ONE, 9, e90385.


    • Yu-Shan Lin, Hsien-Lu Huang, Weiting Liu, Ta-Hsien Lin*, and Hsien-bin Huang* Identification of the high molecular weight isoform of phostensin, 2014, Int. J. Mol. Sci., 15, 1068-1079.


    • Chen-Yuan Kao, Jun-Kun Lai, Ta-Hsien Lin, Yu-Jiun Lin, Jeng-Shiung Jan∗, Steven S.-S. Wang∗ Examining the inhibitory actions of copolypeptides against amyloidfibrillogenesis of bovine insulin, 2013, Biochemical Engineering Journal, 78, 181-188.


    • Yi-Ru Chen, Hsien-bin Huang, Chi-Jen Lo, Chih-Ching Wang, Li-Kang Ho, Hsin-Tzu Liu, Ming-Shi Shiao, Ta-Hsien Lin*, Yi-Cheng Chen* Effect of Alanine Replacement of L17 and F19 on the Aggregation and Neurotoxicity of Arctic-Type Aβ40, 2013, PLOS ONE, 8, e61847.


    • Deli Irene, Jian-Wen Huang, Tse-Yu Chung, Feng-Yin Li, Jason T.-C. Tzen, Ta-Hsien Lin and Chia-Lin Chyan* Binding orientation and specificity of calmodulin to rat olfactory cyclic nucleotide-gated ion channel,2013, J. Biomol. Struct. Dyn., 34, 414-425.


    • Tzu-Fan Wang, Ning-Sheng Lai, Kuang-Yung Huang, Hsien-Lu Huang, Ming-Chi Lu, Yu-Shan Lin, Chun-Yu Chen, Su-Qin Liu, Ta-Hsien Lin* and Hsien-Bin Huang* Identification and Characterization of the Actin-Binding Motif of Phostensin, 2012, Int. J. Mol. Sci., 13, 15967-15982.


    • Chih-Ching Wang, Hsien-bin Huang, Huey-Jen Tsay, Ming-Shi Shiao, Wen-Jin Winston Wu, Yi-Chen Chen* and Ta-Hsien Lin* Characterization of Aβ aggregation mechanism probing by Congo red, 2012, J. Biomol. Struct. Dyn., 30, 160-169.



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