Author

R. D. Ye

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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Immunology· 3 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 4 Approach:experimental assay· 4 Research Focus:protein structure prediction· 4 Organism:human· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

A. Liu· 4 shared Y. Liu· 4 shared L. Zhu· 2 shared Q. Liao· 2 shared W. Zhang· 2 shared C. Llinas del Torrent Masachs· 1 shared F. Wang· 1 shared F. Ye· 1 shared

Activity by Year

2023-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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4 shared papersImmunology

A. Liu

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structural basis for constitutive activation and CXCL1 recognition of human herpesvirus 8-encoded G protein-coupled receptor KSHV-GPCR

A. Liu, Y. Liu, C. Llinas del Torrent Masachs, W. Zhang, L. Pardo, R. D. Ye

This study determines the cryo-EM structures of KSHV-GPCR in complex with Gi and CXCL1, revealing structural mechanisms of constitutive activation and ligand binding.

bioRxiv · Dec 27, 2023 · PreprintImmunology

Cryo-EM structure of monomeric CXCL12-bound CXCR4 in active state

Y. Liu, A. Liu, X. Li, Q. Liao, W. Zhang, L. Zhu, R. D. Ye

This paper presents a cryo-EM structure of CXCL12-bound CXCR4 in an active state, revealing key interactions that stabilize the ligand-receptor complex.

bioRxiv · Dec 21, 2023Immunology

Structural basis for EROS binding to human phagocyte NADPH oxidase NOX2

S. Liang, A. Liu, Y. Liu, F. Wang, Y. Zhou, T. Wang, Z. Liu, R. Ren, R. D. Ye

This study determines the cryo-EM structure of the EROS-NOX2-p22phox complex, revealing how EROS binds to NOX2 and regulates its activation.

bioRxiv · Sep 11, 2023 · PreprintImmunology

Cryo-EM structures of the human G-protein coupled receptor 1 (GPR1) - Gi protein complexes bound to the full-length chemerin and to its C-terminal nonapeptide

A. Liu, Y. Liu, G. Chen, W. Lyu, J. Wang, Q. Liao, F. Ye, L. Zhu, Y. Du, R. D. Ye

The paper reports cryo-EM structures of GPR1-Gi complexes bound to full-length chemerin and its C-terminal nonapeptide, revealing a 'two-site' interaction model and structural similarities to CMKLR1-Gi complexes.

bioRxiv · Jun 3, 2023 · PreprintPharmacology & Toxicology