Chen-Chu Wang
Chen-Chu Wang has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
- Bo-Han Chen
Department of Biological Science and Technology, National Chiao Tung University, Hsinchu 300, Taiwan
1 shared publication - Kuo-Sheng Hung
Taipei Medical University
1 shared publication - Yi-Chih Mao
Department of Biological Science and Technology, National Chiao Tung University, 75 Po-Ai Street, Hsinchu 30068, Taiwan
1 shared publication - You-Hua Hou
Department of Biological Science and Technology, National Chiao Tung University, 75 Po-Ai Street, Hsinchu 30068, Taiwan
1 shared publication - Yuh-Shyong Yang
Institute of Biological Science and Technology, National Chiao Tung University, Hsinchu 300, Taiwan
1 shared publication
Latest Publications
- Open Access
Tyrosine Sulfation as a Protein Post-Translational Modification
Integration of inorganic sulfate into biological molecules plays an important role in biological systems and is directly involved in the instigation of diseases. Protein tyrosine sulfation (PTS) is a common post-translational modification that was first reported in the literature fifty years ago. However, the significance of PTS under physiological conditions and its link to diseases have just begun to be appreciated in recent years. PTS is catalyzed by tyrosylprotein sulfotransferase (TPST) through transfer of an activated sulfate from 3'-phosphoadenosine-5'-phosphosulfate to tyrosine in a variety of proteins and peptides. Currently, only a small fraction of sulfated proteins is known and the understanding of the biological sulfation mechanisms is still in progress. In this review, we give an introductory and selective brief review of PTS and then summarize the basic biochemical information including the activity and the preparation of TPST, methods for the determination of PTS, and kinetics and reaction mechanism of TPST. This information is fundamental for the further exploration of the function of PTS that induces protein-protein interactions and the subsequent biochemical and physiological reactions.
Open AccessTyrosine Sulfation as a Protein Post-Translational Modification
Integration of inorganic sulfate into biological molecules plays an important role in biological systems and is directly involved in the instigation of diseases. Protein tyrosine sulfation (PTS) is a common post-translational modification that was first reported in the literature fifty years ago. However, the significance of PTS under physiological conditions and its link to diseases have just begun to be appreciated in recent years. PTS is catalyzed by tyrosylprotein sulfotransferase (TPST) through transfer of an activated sulfate from 3'-phosphoadenosine-5'-phosphosulfate to tyrosine in a variety of proteins and peptides. Currently, only a small fraction of sulfated proteins is known and the understanding of the biological sulfation mechanisms is still in progress. In this review, we give an introductory and selective brief review of PTS and then summarize the basic biochemical information including the activity and the preparation of TPST, methods for the determination of PTS, and kinetics and reaction mechanism of TPST. This information is fundamental for the further exploration of the function of PTS that induces protein-protein interactions and the subsequent biochemical and physiological reactions.