Dr. Tinghai (Peter) Xu earned a B.S. in biotechnology from East China University of Science and Technology (ECUST) followed by a Ph.D. in pharmacology from Shanghai Institute of Materia Medica, Chinese Academy of Sciences. As a doctoral student in the labs of Dr. Eric Xu and Dr. Karsten Melcher, who hold appointments at Van Andel Research Institute and Shanghai Institute of Materia Medica, he explored the relationship between Ab and γ-secretase as well as the structure and function of DNA methyltransferase and nucleosome complexes. In 2014, while working on his thesis research, he joined Van Andel Research Institute as a guest student. He is now a postdoctoral fellow in the Xu and Jones laboratories.
Dr. Xu’s current work utilizes single particle electron cryo-electron microscopy to study the structure and function of DNMT-nucleosome complexes and the PRC2-nucleosome complex.
Ph.D. in molecular pharmacology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (SIMM) China (Adviser: Dr. Eric Xu and Dr. Karsten Melcher)
Thesis: Structural and functional studies of C99 and Ab
B.S. in biotechnology, East China University of Science and Technology (Adviser: Dr. Qiyao Wang)
Excellent graduation thesis, ECUST (2012)
Comprehensive course scholarship, ECUST (2011–2012)
Comprehensive course scholarship, ECUST (2010–2011)
Excellent volunteer, Shanghai World Expo 2010 (2010)
National Scholarship, Ministry of Education of the People’s Republic of China (2009–2010)
Vice President, Student Union of the Bioengineering College, ECUST (2009–2010)
National Encouragement Scholarship, Ministry of Education of the People’s Republic of China (2008–2009)
To view a list of selected publications click below. To view Dr. Xu’s Google Scholar page click here.
Yan Y*, Xu TH*, Melcher K, Xu HE. 2017. Defining the minimum substrate and charge recognition model of gamma-secretase. Acta Pharmacol Sin doi:10.1038/aps.2017.35.
Yan Y*, Xu TH*, Harikumar KG, Miller LJ, Melcher K, Xu HE. 2017. Dimerization of the transmembrane domain of amyloid precursor protein is determined by residues around the gamma-secretase cleavage sites. J Biol Chem doi:10.1074/jbc.M117.789669.
Chen GF, Xu TH, Yan Y, Zhou YR, Jiang Y, Melcher K, Xu HE. 2017. Amyloid beta: structure, biology and structure-based therapeutic development. Acta Pharmacol Sin doi:10.1038/aps.2017.28.
Ma H, Duan J, Ke J, He Y, Gu X, Xu TH, Yu H, Wang Y, Brunzelle JS, Jiang Y, Rothbart SB, Xu HE, Li J, Melcher K. 2017. A D53 repression motif induces oligomerization of TOPLESS corepressors and promotes assembly of a corepressor-nucleosome complex. Sci Adv 3(6):e1601217.
Xu TH, Yan Y, Kang Y, Jiang Y, Melcher K, Xu HE. 2016. Alzheimer’s disease-associated mutations increase amyloid precursor protein resistance to gamma-secretase cleavage and the Abeta42/Abeta40 ratio. Cell Discov 2:16026.
Zhao LH, Zhou XE, Wu ZS, Yi W, Xu Y, Li S, Xu TH, Liu Y, Chen RZ, Kovach A, Kang Y, Hou L, He Y, Xie C, Song W, Zhong D, Xu Y, Wang Y, Li J, Zhang C, Melcher K, Xu HE. 2013. Crystal structures of two phytohormone signal-transducing alpha/beta hydrolases: karrikin-signaling KAI2 and strigolactone-signaling DWARF14. Cell Res 23:436–439.