Author

H. E. Xu

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 16 Biochemistry· 4 Cell Biology· 2 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 22 Research Focus:protein structure prediction· 17 Organism:human· 15 Assay:structural biology· 11 Assay:cryo-EM· 9 Research Focus:drug response / drug discovery· 5 Research Focus:host-pathogen & immune response· 4 Research Focus:protein folding & dynamics· 4

Frequent Co-Authors

Y. Jiang· 18 shared W. Yin· 14 shared X. He· 9 shared D. Yang· 7 shared M.-W. Wang· 7 shared P. Xu· 6 shared Q. Yuan· 6 shared X. Wang· 6 shared

Activity by Year

2019-2023 · peak 9/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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18 shared papersBiophysics

Y. Jiang

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23 papers

Recent·Most cited

Structure basis for recognition of 26RFa by the pyroglutamylated RFamide peptide receptor

S. Jin, X. Li, Y. Xu, S. Guo, C. Wu, B. Pan, W. Xin, H. Zhang, W. Hu, Y. Yin, T. Zhang, K. Wu, Q. Yuan, H. E. Xu, X. Xie, Y. Jiang

This study determines the cryo-EM structure of QRFPR bound to 26RFa, revealing the recognition mechanism and aiding drug design for obesity and diabetes.

bioRxiv · Dec 9, 2023 · PreprintBiophysics

A conserved and druggable pocket in class B G protein coupled receptors for orally active small molecule agonists

H. E. Xu, L. Zhao, Q. He, Q. Yuan, Y. Gu, X. He, H. Shan, J. Li, K. Wang, Y. Li, W. Hu, K. Wu, J. Shen

This study identifies a conserved binding pocket in class B GPCRs that enables small molecule agonists like PCO371 to activate G proteins without triggering arrestin signaling.

bioRxiv · Jun 8, 2023 · PreprintBiochemistry

Structure of a G protein-coupled receptor with GRK2 and a biased ligand

J. Duan, H. Liu, Y. Ji, Q. Yuan, X. Li, K. Wu, T. Gao, S. Zhu, Y. Jiang, W. Yin, H. E. Xu

The paper reports the structure of NTSR1 bound to GRK2, Gq, and a biased ligand, revealing how the ligand enhances GRK2 binding and enables arrestin-biased signaling.

bioRxiv · Oct 19, 2022 · PreprintCell Biology

Molecular Recognition of Itching Neuropeptides by Bombesin Receptors.

C. Li, Y. Xu, H. Liu, H. Cai, Y. Jiang, H. E. Xu, W. Yin

The paper presents cryo-EM structures of bombesin receptors bound to their neuropeptide ligands, revealing the mechanism of ligand selectivity and receptor activation for itch treatment.

bioRxiv · Oct 10, 2022 · PreprintBiophysics

Molecular recognition of two endogenous hormones by the human parathyroid hormone receptor-1

L.-h. Zhao, Q. Yuan, A. Dai, C.-W. Chen, X. He, C. Zhang, Y. Xu, Y. Zhou, M.-W. Wang, D. Yang, H. E. Xu

The paper reports cryo-EM structures of PTH1R bound to PTH and PTHrP, revealing molecular mechanisms of hormone recognition and selectivity.

bioRxiv · Oct 9, 2022 · PreprintBiochemistry

Structural Genomics of the Human Dopamine Receptor System

P. Xu, S. Huang, B. E. Krumm, Y. Zhuang, C. Mao, Y. Zhang, Y. Wang, X.-P. Huang, Y.-F. Liu, X. He, H. Li, W. Yin, Y. Jiang, Y. Zhang, B. L. Roth, H. E. Xu

This study reports cryo-EM structures of all human dopamine receptor subtypes bound to Rotigotine, revealing binding modes, activation mechanisms, and G-protein coupling specificity for drug design.

bioRxiv · Oct 9, 2022Biochemistry

Universal mechanism of hormone and allosteric agonist mediated activation of glycoprotein hormone receptors as revealed by structures of follicle stimulating hormone receptor

H. E. Xu, Y. Zhang, S. Zhang, J. Duan, P. Xu, H. Zhang, X. Luan, J. Yang, Y. Ji, X. He, H. Jiang, X. Cheng, Y. Jiang, C. Mao, D. Shen

The paper reports cryo-EM structures of FSHR in inactive and active states, revealing a conserved activation mechanism and the role of H6157.42 in agonist selectivity.

bioRxiv · Aug 1, 2022 · PreprintCell Biology

Structural and biochemical mechanism for increased infectivity and immune evasion of Omicron BA.1 and BA.2 variants and their mouse origins

Y. Xu, C. Wu, X. Cao, C. Gu, H. Liu, M. Jiang, X. Wang, Q. Yuan, K. Wu, J. Liu, X. He, D. Wang, X. Wang, S.-J. Deng, H. E. Xu, W. Yin

This study investigates the structural and biochemical features of Omicron BA.1 and BA.2 variants, showing increased infectivity and mouse ACE2 binding compared to wildtype, suggesting a potential human-cat-mouse-human transmission cycle.

bioRxiv · Apr 12, 2022 · PreprintBiophysics

Structural insights into the peptide selectivity and activation of human neuromedin U receptors

C. You, Y. Zhang, P. Xu, S. Huang, W. Yin, H. E. Xu, Y. Jiang

This study reports cryo-EM structures of NMUR1 and NMUR2 bound to NMU and NMS, revealing peptide selectivity mechanisms and activation principles for drug design.

bioRxiv · Feb 21, 2022Biophysics

Structures of the Omicron spike trimer with ACE2 and an anti-Omicron antibody: mechanisms for the high infectivity, immune evasion and antibody drug discovery

W. Yin, Y. Xu, P. Xu, X. Cao, C. Wu, C. Gu, X. He, X. Wang, S. Huang, Q. Yuan, K. Wu, W. Hu, Z. Huang, J. Liu, Z. Wang, , H. E. Xu

bioRxiv · Dec 27, 2021 · PreprintBiophysics

Structural mechanism of calcium-mediated hormone recognition and Gβ interaction by the human melanocortin-1 receptor

S. Ma, Y. Chen, A. Dai, W. Yin, J. Guo, D. Yang, F. Zhou, Y. Jiang, M.-W. Wang, H. E. Xu

The paper presents cryo-EM structures of MC1R-Gs complexes with ligands, revealing calcium's role in hormone recognition and Gβ interactions, and a conserved activation mechanism.

bioRxiv · Jun 20, 2021Biophysics

Molecular recognition of an acyl-peptide hormone and activation of ghrelin receptor

Y. Wang, S. Guo, Y. Zhuang, Y. Yun, P. Xu, X. He, J. Guo, W. Yin, H. E. Xu, X. Xie, Y. Jiang

The paper presents cryo-EM structures of the ghrelin receptor bound to ghrelin and GHRP-6, revealing the binding pocket for the octanoyl group and providing insights for drug design.

bioRxiv · Jun 9, 2021Biophysics

Molecular insights into differentiated ligand recognition of the human parathyroid hormone receptor 2

X. Wang, X. Cheng, L. Zhao, Y. Wang, C. Ye, X. Zou, A. Dai, Z. Cong, J. Chen, Q. Zhou, T. Xia, H. Jiang, H. E. Xu, D. Yang, M.-W. Wang

This study reports the cryo-EM structure of PTH2R bound to TIP39 and a Gs protein, revealing ligand specificity and disease-associated mutation effects.

bioRxiv · Jun 9, 2021Biochemistry

Structural basis for recognition of anti-migraine drug lasmiditan by the serotonin receptor 5-HT1F-G protein complex

S. Huang, p. Xu, Y. Tan, C. You, Y. Zhang, Y. Jiang, H. E. Xu

This study determines the cryo-EM structure of the 5-HT1F receptor complex with lasmiditan and a G protein, revealing the mechanism of selective activation and informing drug design.

bioRxiv · May 29, 2021Biophysics

Molecular basis for kinin selectivity and activation of the human bradykinin receptors

Y.-L. Yin, C. Ye, F. Zhou, J. Wang, D. Yang, W. Yin, M.-W. Wang, H. E. Xu, Y. Jiang

The paper reports structures of bradykinin receptors bound to their ligands and reveals mechanisms of selectivity and activation, providing insights for drug design.

bioRxiv · May 27, 2021Biophysics

Structures of the human cholecystokinin receptors in complex with agonists and antagonists

X. Zhang, C. He, M. Wang, Q. zhou, D. Yang, Y. Zhu, W. Feng, H. Zhang, A. Dai, X. Chu, J. Wang, Z. Yang, Y. Jiang, U. Sensfuss, Q. Tan, , Q. Zhao

The paper reports crystal and cryo-EM structures of human CCKAR and CCKBR with ligands, revealing ligand recognition and activation mechanisms.

bioRxiv · May 19, 2021 · PreprintBiophysics

Structural basis for ligand recognition and G protein-coupling promiscuity of the cholecystokinin A receptor

Q. Liu, D. Yang, Y. Zhuang, T. I. Croll, X. Cai, A. Dai, X. He, J. Duan, W. Yin, C. Ye, F. Zhou, B. Wu, Q. Zhao, H. E. Xu, M.-W. Wang, Y. Jiang

The paper presents cryo-EM structures of CCKAR with different G proteins to elucidate its G protein coupling promiscuity and ligand recognition mechanism.

bioRxiv · May 9, 2021 · PreprintBiophysics

Molecular basis of ligand recognition and activation of human V2 vasopressin receptor

Y. Jiang, F. Zhou, C. Ye, X. Ma, W. Yin, Q. Zhou, X. He, X. Zhang, T. I. Croll, D. Yang, P. Wang, H. E. Xu, M.-W. Wang

The paper determines the structure of the V2 vasopressin receptor bound to AVP and Gs, revealing how AVP activates the receptor and providing insights for drug design.

Cell Research · Mar 19, 2021Peer-reviewedBiophysics

Structural basis for repurpose and design of nucleoside drugs for treating COVID-19

W. Yin, X. Luan, Z. Li, Y. Xie, Z. Zhou, J. Liu, M. Gao, X. Wang, F. Zhou, Q. Wang, Q. Wang, D. Shen, Y. Zhang, G. Tian, H. A. Aisa, , H. E. Xu

The paper reports cryo-EM structures of SARS-CoV-2 RdRp with nucleoside inhibitors, revealing their mechanism and guiding the design of more potent derivatives.

bioRxiv · Nov 1, 2020 · PreprintBiophysics

Structure Basis for Inhibition of SARS-CoV-2 by the Feline Drug GC376

X. Luan, W. Shang, Y. Wang, W. Yin, Y. Jiang, S. Feng, Y. Wang, M. Liu, R. Zhou, Z. Zhang, F. Wang, C. Wang, M. Gao, H. Wang, W. Wu, , S. Zhang

The paper determines the structure of SARS-CoV-2 Mpro and shows how GC376 inhibits its catalytic site, supporting its use as an antiviral drug.

bioRxiv · Jun 7, 2020Biophysics

Molecular mechanisms of fentanyl mediated β-arrestin biased signaling

P. W. de Waal, J. Shi, E. You, X. Wang, K. Melcher, Y. Jiang, H. E. Xu, B. Dickson

This paper investigates how fentanyl activates the mu-opioid receptor through beta-arrestin biased signaling using molecular dynamics simulations and validates findings with synthesized compounds.

PLOS Computational Biology · Apr 10, 2020Peer-reviewedBiophysics

Enzalutamide-induced PTH1R-mediated TGFBR2 decrease in osteoblasts contributes to resistance in prostate cancer bone metastases

S. Su, J. Cao, X. Meng, R. Liu, A. Vander Ark, E. Woodford, R. Zhang, I. Stiver, X. Zhang, Z. B. Madaj, M. J. Bowman, Y. Wu, H. E. Xu, B. Chen, H. Yu, X. Li

bioRxiv · Nov 25, 2019 · PreprintCancer Biology

A complex structure of arrestin-2 bound to a G protein-coupled receptor

W. Yin, Z. Li, M. Jin, Y. Yin, P. W. de Waal, K. Pal, Y. Yin, X. Gao, Y. He, J. Gao, X. Wang, Y. Zhang, H. Zhou, K. Melcher, Y. Jiang, , H. E. Xu

The paper reports the structure of arrestin-2 bound to neurotensin receptor 1, revealing a novel orientation that enables coupling to GPCRs lacking a C-terminal tail.

bioRxiv · Oct 29, 2019Biophysics