People (only the participants of GIBH are listed)
HE Jun
Title:Principle Investigator
Subject:
Email:he_jun@gibh.ac.cn
Address:Kaiyuan Dadao 190,510530,Guangzhou,China
Study/Work Experience

2018 – now

Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences/Principle Investigator

2016 – 2018

UCB Pharma/Senior Scientist

2013 – 2016

The Clare Hall Laboratories, the Francis Crick Institute/Post-doctoral Research Fellow

2012 – 2013

The Institute of Cancer Research/Post-doctoral Scientist

2008 – 2012

The Institute of Cancer Research/Ph.D

Research Areas

Dr. Jun He is an Ph.D. supervisor and a selected member of the Chinese Academy of Sciences' esteemed high-level talent program, serves as the board member of the Cryo-Electron Microscopy Branch of the China Biophysical Society and the Guangdong Branch of the Chinese Society of Electron Microscopy. His research endeavors leverage cutting-edge methodologies, notably cryo-electron microscopy reconstruction, to delve into the intricate realm of biomacromolecular machines. These machines, with their pivotal involvement in the epigenetic regulation of tumors, form the crux of Dr. He's investigative focus. Dr. He’s scientific contributions have found a notable place in the annals of research, with impactful papers gracing the pages of premier international journals such as Cell Research, Molecular Cell, Nature Microbiology, and Nature Communications. Dr. He's intellectual pursuit extends to a rich portfolio of research undertakings, encompassing prestigious initiatives such as the Key Research and Development Program under the Ministry of Science and Technology (2020YFC0845900, 2020YFE0202200), grants from the National Natural Science Foundation of China (NSFC) earmarked for pivotal projects (32170189), collaborative funding projects (U20A2013), and grants bestowed by the Guangdong Provincial Natural Science Foundation (2019A1515011907).

Academic Performance

2019: Huangpu Talent Program, Guangzhou City

2018: High-Level Talent Program, Chinese Academy of Sciences

2013: Chairman’s Prize for Best PhD, the Institute of Cancer Research

2012: Government Award for outstanding students abroad

Representative Papers

1.Li, W. #, Cao, P. #, Xu, P., Sun, F., Wang, C., Zhang, J., Dong, S., Wilson, J. R., Xu, D., Fan, H., Feng, Z., Zhang, X., Zhu, Q., Fan, Y., Brown, N., Justin, N., Gamblin, S. J., Li, H., Zhang, Y.*, He, J*. Rapid reconstitution of ubiquitinated nucleosome using a non-denatured histone octamer ubiquitylation approach. Cell & Bioscience, 14(1), 81. (2024)

2.Zhang, J. #, Zhao, H., Zou, B., Li, H., Dong, S., Guan, J., Wang, C., Li, W., Liu, Y., Chen, Y., Rasheed, N.*, He, J*. Cryo-EM structure and functional analysis of the chromatin remodeler RSF. Acta Crystallographica Section F: Structural Biology Communications, 80: 125-34. (2024)

3.Xue, L. #, Chang, T. #, Li, Z., Wang, C., Zhao, H., Li, M., Tang, P., Wen, X., Yu, M., Wu, J., Bao, X., Wang, X., Gong, P., He, J., Chen, X.*, Xiong, X*. Cryo-EM structures of Thogoto virus polymerase reveal unique RNA 2 transcription and replication mechanisms among orthomyxoviruses. Nature Communications 15.1 : 4620. (2024)

4.Wang, N. #, Sheng, Y. #, Liu, Y., Guo, Y., He, J., Liu, J*. Cryo-EM structures of Mycobacterium tuberculosis polynucleotide phosphorylase suggest a potential mechanism for its RNA substrate degradation. Archives of Biochemistry and Biophysics, 754, 109917. (2024)

5.Liu, B. #, Niu, X. #, Deng, Y. #, Zhang, Z. #, Wang, Y., Gao, X., Liang, H., Li, Z., Wang, Q., Cheng, Y., Chen, Q., Huang, S., Pan, Y., Su, M., Lin, X., Niu, C., Chen, Y., Yang, W., Zhang, Y., Yan, Q., He, J., Zhao, J.*, Chen, L.*, Xiong, X*. An unconventional VH1-2 antibody tolerates escape mutations and shows an antigenic hotspot on SARS-CoV-2 spike. Cell reports, 43(6), 114265. (2024)

6. Dong, S. #, Li, H. #, Wang, M. #, Rasheed, N. #, Zou, B., Gao, X., Guan, J., Li, W., Zhang, J., Wang, C., Zhou, N., Shi, X., Li, M., Zhou, M., Huang, J., Li, H., Zhang, Y., Wong, K.H., Zhang, X., Chao, W.C.H.*, and He, J*. Structural basis of nucleosome deacetylation and DNA linker tightening by Rpd3S histone deacetylase complex. Cell Research 33, 790-801. (2023)

7. Zhang, X. #, Li, Z. #, Zhang, Y. #, Liu, Y. #, Wang, J., Liu, B., Chen, Q., Wang, Q., Fu, L., Wang, P., Zhong, X., Jin, L., Yan, Q., Chen, L., He, J.*, Zhao, J. *, and Xiong, X*. Disulfide stabilization reveals conserved dynamic features between SARS-CoV-1 and SARS-CoV-2 spikes. Life Science Alliance6. (2023)

8. Yu, H. #, Liu, B. #, Zhang, Y. #, Gao, X. #, Wang, Q. #, Xiang, H. #, Peng, X. #, Xie, C. #, Wang, Y. #, Hu, P., Shi, J., Shi, Q., Zheng, P., Feng, C., Tang, G., Liu, X., Guo, L., Lin, X., Li, J., Liu, C., Huang, Y., Yang, N., Chen, Q., Li, Z., Su, M., Yan, Q., Pei, R., Chen, X., Liu, L., Hu, F., Liang, D., Ke, B., Ke, C. *, Li, F. *, He, J. *, Wang, M.*, Chen, L.*, Xiong, X.*, and Tang, X*. Somatically hypermutated antibodies isolated from SARS-CoV-2 Delta infected patients cross-neutralize heterologous variants. Nature Communications 14, 1058. (2023)

9.Zhang, X.#, Xin, J.#, Wang, Z.#, Wu, W., Liu, Y., Min, Z., Xin, Y., Liu, B., He, J., Zhang, X., and Xu, X*. Structural basis of a bi-functional malonyl-CoA reductase (MCR) from the photosynthetic green non-sulfur bacterium Roseiflexus castenholzii. Mbio14, e0323322. (2023)

10. Tang, L. #, Dong, S. #, Rasheed, N. #, Wu, H.W. #, Zhou, N. #, Li, H., Wang, M., Zheng, J.*, He, J.*, and Chao, W.C.H*. Vibrio parahaemolyticus prey targeting requires autoproteolysis-triggered dimerization of the type VI secretion system effector RhsP. Cell Reports 41, 111732. (2022)

11. He, P. #, Liu, B. #, Gao, X. #, Yan, Q. #, Pei, R. #, Sun, J., Chen, Q., Hou, R., Li, Z., Zhang, Y., Zhao, J., Sun, H., Feng, B., Wang, Q., Yi, H., Hu, P., Li, P., Zhang, Y., Chen, Z., Niu, X., Zhong, X., Jin, L., Liu, X., Qu, K., Ciazynska, K.A., Carter, A.P., Briggs, J.A.G., Chen, J., Liu, J., Chen, X.*, He, J.*, Chen, L.*, and Xiong, X*. SARS-CoV-2 Delta and Omicron variants evade population antibody response by mutations in a single spike epitope. Nature Microbiology 7, 1635-1649. (2022)

12. Chen, M. #, He, Y. #, Liu, D., Tian, L., Xu, P., Liu, X., Pan, Y., Dong, S., He, J. *, and Zhang, Y*. Structure Insights Into Photosystem I Octamer From Cyanobacteria. Frontiers in Microbiology 13, 876122. (2022)

13. Wang, X. et al. A potent human monoclonal antibody with pan-neutralizing activities directly dislocates S trimer of SARS-CoV-2 through binding both up and down forms of RBD. Signal Transduction and Targeted Therapy 7, 114. (2022)

14. Qu, K. #, Chen, Q., Ciazynska, K.A., Liu, B., Zhang, X., Wang, J., He, Y., Guan, J., He, J., Liu, T., Zhang, X., Carter, A.P., Xiong, X.*, and Briggs, J.A.G*. Engineered disulfide reveals structural dynamics of locked SARS-CoV-2 spike. PLoS Pathogens 18, e1010583. (2022)

15. Chen, M. #, Liu, X., He, Y., Li, N., He, J.*, and Zhang, Y*. Diversity Among Cyanobacterial Photosystem I Oligomers. Frontiers in Microbiology 12, 781826. (2021)

16. Zhang, C. #, Li, L., He, J., Chen, C., and Su, D*. Nonstructural protein 7 and 8 complexes of SARS-CoV-2. Protein Science 30, 873-881. (2021)

17. Zhang, C. #, Chen, Y., Li, L., Yang, Y., He, J., Chen, C. *, and Su, D*. Structural basis for the multimerization of nonstructural protein nsp9 from SARS-CoV-2. Molecular biomedicine 1, 5. (2020)

18. Frigola, J. #, He, J. #, Kinkelin, K., Pye, V.E., Renault, L., Douglas, M.E., Remus, D., Cherepanov, P. *, Costa, A. *, and Diffley, J.F.X*. Cdt1 stabilizes an open MCM ring for helicase loading. Nature communications 8, 15720. (2017)

19. He, J. #, Chao, W.C. #, Zhang, Z., Yang, J., Cronin, N., and Barford, D*. Insights into degron recognition by APC/C coactivators from the structure of an Acm1-Cdh1 complex. Molecular cell 50, 649-660. (2013)

20. He, J. #, Kulkarni, K., da Fonseca, P.C., Krutauz, D., Glickman, M.H., Barford, D.*, and Morris, E.P*. The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric alpha-helical rings. Structure 20, 513-521. (2012)

21. da Fonseca, P.C. #, He, J., and Morris, E.P*. Molecular model of the human 26S proteasome. Molecular cell 46, 54-66. (2012)