Author

X. Cong

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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Biochemistry· 5 Biophysics· 1 Cell Biology· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 5 Approach:biophysical modeling· 2 Research Focus:cell signaling & trafficking· 2 Assay:cryo-EM· 2 Research Focus:drug response / drug discovery· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2

Frequent Co-Authors

S. Granier· 6 shared C. Leyrat· 4 shared C. BECHARA· 3 shared A. Fouillen· 2 shared B. Mouillac· 2 shared E. Del Nero· 2 shared H. Orcel· 2 shared J. Saint-Paul· 2 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 28 mutual co-author links

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6 shared papersBiochemistry

S. Granier

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Conformational dynamics underlying Atypical Chemokine Receptor 3 activation

O. Otun, C. Aljamous, E. Del Nero, M. Arimont-Segura, R. Bosma, B. Zarzycka, T. Girbau, C. Leyrat, C. de Graaf, R. Leurs, T. Durroux, S. Granier, X. Cong, C. BECHARA

This study investigates the conformational dynamics of ACKR3 activation using HDX-MS and molecular dynamics simulations, revealing key structural changes and ligand binding mechanisms.

bioRxiv · Jul 17, 2023 · PreprintBiochemistry

Biased activation of the vasopressin V2 receptor probed by NMR, paramagnetic ligands, and molecular dynamics simulations

G. Gaibelet, A. Fouillen, R. Stephanie, H. Orcel, C. Mendre, A. Kanso, R. Lanotte, J. Nguyen, J. Dimon, S. Urbach, R. Sounier, S. Granier, D. Bonnet, X. Cong, B. Mouillac, H. Demene

The paper uses NMR, molecular dynamics, and pharmacology to study conformational changes in the V2R receptor bound to different ligands, revealing a mechanism for Gs-biased agonism involving TM7 and TM3 interactions.

bioRxiv · Jun 6, 2023 · PreprintBiophysics

Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex

J. Bous, A. Fouillen, H. Orcel, S. Trapani, X. Cong, S. Fontanel, J. Saint-Paul, J. LAI KEE HIM, S. Urbach, N. Sibille, R. SOUNIER, S. Granier, B. Mouillac, P. Bron

The paper reports the cryo-EM structure of the V2 receptor-{beta}-arrestin1 complex, revealing structural variability in GPCR-arrestin interactions.

bioRxiv · Feb 11, 2022Biochemistry

The relaxin receptor RXFP1 signals through a mechanism of autoinhibition

S. C. Erlandson, S. Rawson, J. Osei-Owusu, K. P. Brock, X. Liu, J. A. Paulo, J. Mintseris, S. P. Gygi, D. S. Marks, X. Cong, A. C. Kruse

This study determines the cryo-EM structure of active-state RXFP1 bound to relaxin-2 and Gs protein, revealing an autoinhibition mechanism.

bioRxiv · Jan 22, 2022 · PreprintPharmacology & Toxicology

Structural insights into recognition of chemokine receptors by Staphylococcus aureus leukotoxins

C. Leyrat, S. Granier, T. Durroux, C. Bechara, S. Jeannot, F. Peysson, C. M. Grison, P. Verdie, L. Brunel, F. Hoh, X. Cong, O. Otun, P. Lambey

This study investigates how Staphylococcus aureus leukotoxins recognize chemokine receptors, identifying sulfotyrosine binding sites and proposing structural models for receptor-toxin interactions.

bioRxiv · Aug 5, 2021Biochemistry

Discovery and mechanism of action of small molecule inhibitors of ceramidases

S. Granier, R. D. Healey, E. Saied, X. Cong, G. Karsai, L. Gabellier, J. Saint-Paul, E. Del Nero, S. Jeannot, M. Drapeau, S. Fontanel, D. Maurel, S. Basu, C. LEYRAT, G. Bossis, , C. Arenz

The paper discovers small molecule inhibitors of alkaline ceramidase 3 using fluorescent substrates and characterizes their mechanism of action.

bioRxiv · Jun 15, 2021Biochemistry

An automated platform for structural analysis of membrane proteins through serial crystallography

R. D. Healey, S. Basu, A.-S. Humm, C. Leyrat, X. Cong, J. Golebiowski, F. Dupeux, A. Pica, S. Granier, J. A. Marquez

This paper introduces an automated platform for structural analysis of membrane proteins using serial crystallography, enabling high-throughput ligand discovery and structural determination.

bioRxiv · Jun 3, 2021Biochemistry

Phosphoproteomics Reveals AMPK Substrate Network in Response to DNA Damage and Histone Acetylation

Y. Jiang, X. Cong, S. Jiang, Y. Dong, L. Zhao, Y. Zang, M. Tan, J. Li

The paper identifies AMPK substrates and their roles in DNA damage response and histone acetylation through phosphoproteomics and histone modification analysis.

bioRxiv · Jul 2, 2020Cell Biology