DHH&TXD Laboratory

1. Yang, Lili#; Chen, Yujiao#; Chang, Shenghai#; Wang, Xin; Zhang, Changbin; Zhang, Zhibo; Ding, Bi-sen; Su, Zhaoming*; Dong, Haohao*; Tang, Xiaodi* ; Structural insights into the activation of the divisome complex FtsWIQLB, Cell Discovery, 2024, 10(2)

https://www.nature.com/articles/s41421-023-00629-w

2. Shen, Chongrong#; Chang, Shenghai#; Luo, Qinghua#; Chan, Kevin Chun#; Zhang, Zhibo; Luo, Bingnan; Xie, Teng; Lu, Guangwen; Zhu, Xiaofeng; Wei, Xiawei; Dong, Changjiang; Zhou, Ruhong*; Zhang, Xing*; Tang, Xiaodi*; Dong, Haohao* ; Structural basis of BAM-mediated outer membrane β- barrel protein assembly, Nature, 2023, 617(7959): 185-193

https://www.nature.com/articles/s41586-023-05988-8

3. Xia, Anjie#; Yong, Xihao#; Zhang, Changbin#; Lin, Guifeng#; Jia, Guowen#; Zhao, Chang#; Wang, Xin#; Hao, Yize#; Wang, Yifei; Zhou, Pei; Yang, Xin; Deng, Yue; Wu, Chao; Chen, Yujiao; Zhu, Jiawei; Tang, Xiaodi; Liu, Jingming; Zhang, Shiyu; Zhang, Jiahao; Xu, Zheng; Hu, Qian; Zhao, Jinlong; Yue, Yuting; Yan, Wei; Su, Zhaoming; Wei, Yuquan; Zhou, Rongbin*; Dong, Haohao*; Shao, Zhenhua*; Yang, Shengyong* ; Cryo-EM structures of human GPR34 enable the identification of selective antagonists, Proceedings of the National Academy of Sciences, 2023, 120(39): 1- 11

https://www.pnas.org/doi/abs/10.1073/pnas.2308435120

4. Tang, Xiaodi#; Chang, Shenghai#; Zhang, Ke#; Luo, Qinghua#; Zhang, Zhengyu; Wang, Ting; Qiao, Wen; Wang, Chen; Shen, Chongrong; Zhang, Zhibo; Zhu, Xiaofeng; Wei, Xiawei; Dong, Changjiang*; Zhang, Xing*; Dong, Haohao* ; Structural basis for bacterial lipoprotein relocation by the transporter LolCDE, Nature Structural & Molecular Biology, 2021, 28(4): 347-355

https://www.nature.com/articles/s41594-021-00573-x

5. Tang, Xiaodi#; Chang, Shenghai#; Qiao, Wen#; Luo, Qinghua; Chen, Yuejia; Jia, Zhiying; Coleman, James; Zhang, Ke; Wang, Ting; Zhang, Zhibo; Zhang, Changbin; Zhu, Xiaofeng; Wei, Xiawei; Dong, Changjiang*; Zhang, Xing*; Dong, Haohao* ; Structural insights into outer membrane asymmetry maintenance in Gram-negative bacteria by MlaFEDB, Nature Structural & Molecular Biology, 2020, 28: 81-91

https://www.nature.com/articles/s41594-020-00532-y

6. Tang, Xiaodi#; Chang, Shenghai#; Luo, Qinghua#; Zhang, Zhengyu#; Qiao, Wen; Xu, Caihuang; Zhang, Changbin; Niu, Yang; Yang, Wenxian; Wang, Ting; Zhang, Zhibo; Zhu, Xiaofeng; Wei, Xiawei; Dong, Changjiang*; Zhang, Xing*; Dong, Haohao* ; Cryo-EM structures of lipopolysaccharide transporter LptB(2)FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism, Nature Communications, 2019, 10: 0-4175

https://www.nature.com/articles/s41467-019-11977-1

7. Dong, Haohao#; Zhang, Zhengyu#; Tang, Xiaodi#; Paterson, Neil G.*; Dong, Changjiang* ; Structural and functional insights into the lipopolysaccharide ABC transporter LptB(2)FG, Nature Communications, 2017, 8

https://www.nature.com/articles/s41467-017-00273-5

8. Gu, Yinghong#; Li, Huanyu#; Dong, Haohao#; Zeng, Yi#; Zhang, Zhengyu#; Paterson, Neil G.#; Stansfeld, Phillip J.#; Wang, Zhongshan; Zhang, Yizheng; Wang, Wenjian*; Dong, Changjiang* ;Structural basis of outer membrane protein insertion by the BAM complex, Nature, 2016, 531(7592):64-69

https://www.nature.com/articles/nature17199

9. Dong, Haohao; Xiang, Quanju; Gu, Yinghong; Wang, Zhongshan; Paterson, Neil G.; Stansfeld, Phillip J.; He, Chuan; Zhang, Yizheng; Wang, Wenjian*; Dong, Changjiang* ; Structural basis for outer membrane lipopolysaccharide insertion, Nature, 2014, 511(7507): 52-56

https://www.nature.com/articles/nature13464