The laboratory conducts research on the structure and function of key proteins in response to stress in plants and crops. By combining methods such as biochemistry and molecular biology, the molecular mechanisms regulating the functions and activities of these proteins are elucidated, providing breeding clues for efficient stress resistance and variety improvement in plants.

       1. Gao, R., Jia, Y., Xu, X., Fu, P., Zhou, J., Yang, G*. (2024). Structural insights into the Oryza sativa cation transporters HKTs in salt tolerance. J Integr Plant Biol, 66(4), 700-708. (*Corresponding author)

2.  Gao, X., Xu, X., Sun, T., Lu, Y., Jia, Y., Zhou, J., …Yang, G*. (2024). Structural changes in the conversion of an Arabidopsis outward-rectifying K+ channel into an inward-rectifying channel. Plant Commun. (*Corresponding author)

3. Zhang, Y., Zhou, J., Ni, X., Wang, Q., Jia, Y., Xu, X., …Yang, G*. (2023). Structural basis for the activity regulation of Salt Overly Sensitive 1 in Arabidopsis salt toler  ance. Nature Plants. 9(11), 1915-1923 (*Corresponding author)

4. Jia, Y., Zhang, Y., Wang, W., Lei, J., Ying, Z., Yang, G*. (2024). Structural and functional insights of the human peroxisomal ABC transporter ALDP. Elife, 11, e75039. (*Corresponding author)

5.  Lu, Y., Yu, M., Jia, Y., Yang, F., Zhang, Y., Xu, X., …Yang, G*. (2022) Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis. Nat Commun, 13(1), 5682              (*Corresponding author）

6. Zhou, R., Yang, G*., & Shi, Y. (2020). Macromolecular complex in recognition and proteolysis of amyloid precursor protein in Alzheimer’s disease. Current Opinion in Structural Biology, 61, 1-8. (*Corresponding author)

7. Zhou, R., Yang, G*., Guo, X., Zhou, Q., Lei, J., & Shi, Y. (2019). Recognition of the amyloid precursor protein by human γ-secretase. Science, 363(6428), eaaw0930. (*Co-first author)

8. Yang, G., Zhou, R., Zhou, Q., Guo, X., Yan, C., Ke, M., ... & Shi, Y. (2019). Structural basis of Notch recognition by human γ-secretase. Nature, 565(7738), 192.

9. Zhou, R., Yang, G*., & Shi, Y. (2017). Dominant negative effect of the loss-of-function γ-secretase mutants on the wild-type enzyme through heterooligomerization. Proceedings of the National Academy of Sciences, 114(48), 12731-12736. (*Co-first author)

10. Yang, G., Zhou, R., & Shi, Y. (2017). Cryo-EM structures of human γ-secretase. Current opinion in structural biology, 46, 55-64.

11. Yu, X., Yang, G*., Yan, C., Baylon, J. L., Jiang, J., Fan, H., ... & Yan, N. (2017). Dimeric structure of the uracil: proton symporter UraA provides mechanistic insights into the SLC4/23/26 transporters. Cell research, 27(8), 1020. (*Co-first author and corresponding author)

12. Sun, L., Zhou, R., Yang, G., & Shi, Y. (2017). Analysis of 138 pathogenic mutations in presenilin-1 on the in vitro production of Aβ42 and Aβ40 peptides by γ-secretase. Proceedings of the National Academy of Sciences, 114(4), E476-E485.

13. Bai, X. C., Rajendra, E., Yang, G., Shi, Y., & Scheres, S. H. (2015). Sampling the conformational space of the catalytic subunit of human γ-secretase. Elife, 4, e11182.

14. Bai, X. C., Yan, C., Yang, G*., Lu, P., Ma, D., Sun, L., ... & Shi, Y. (2015). An atomic structure of human γ-secretase. Nature, 525(7568), 212. (*Co-first author)

15. Sun, L., Zhao, L., Yang, G*., Yan, C., Zhou, R., Zhou, X., ... & Shi, Y. (2015). Structural basis of human γ-secretase assembly. Proceedings of the National Academy of Sciences, 112(19), 6003-6008. (*Co-first author)

16. Xie, T., Yan, C., Zhou, R., Zhao, Y., Sun, L., Yang, G., ... & Shi, Y. (2014). Crystal structure of the γ-secretase component nicastrin. Proceedings of the National Academy of Sciences, 111(37), 13349-13354.

17. Lu, P., Bai, X.C., Ma, D., Xie, T., Yan, C., Sun, L., Yang, G., Zhao, Y., Zhou, R., Scheres, S.H. and Shi, Y. (2014). Three-dimensional structure of human γ secretase. Nature, 512(7513), 166.