Author

C. G. Tate

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Assay:fluorescence / live-cell microscopy· 1 Organism:human· 1 Research Focus:spatial domain detection· 1

Frequent Co-Authors

T. Warne· 2 shared A. Breuer· 1 shared A. Dore· 1 shared A. G. W. Leslie· 1 shared A. Gupta· 1 shared A. Tonnesen· 1 shared B. Carpenter· 1 shared C. G. Shuttle· 1 shared

Activity by Year

2018-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersBiophysics

T. Warne

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Author profile →

3 papers

Recent·Most cited

Multimodal intrinsic activation of GPCRs in ultrastable plasma membrane nanodomains

G. Kockelkoren, J. Carstensen, L. Lauritsen, E. Kazepidou, A. Tonnesen, C. G. Shuttle, P. S. Kaas, A. Gupta, A. Breuer, S. G. F. Rasmussen, L. Duffet, T. Warne, T. Patriarchi, C. G. Tate, M. Uline, D. Stamou

This paper quantifies GPCR intrinsic activation at the plasma membrane, revealing spatial multimodality with most receptors showing negligible spontaneous activation.

bioRxiv · Feb 28, 2024 · PreprintBiophysics

Molecular basis for high affinity agonist binding in GPCRs

T. Warne, P. Edwards, A. Dore, A. G. W. Leslie, C. G. Tate

The paper determines active-state structures of β1AR bound to agonists and identifies structural changes that increase agonist affinity.

bioRxiv · Oct 5, 2018Biochemistry

Cryo-EM structure of the adenosine A2A receptor coupled to an engineered heterotrimeric G protein

C. G. Tate, J. Garcia-Nafria, Y. Lee, X. Bai, B. Carpenter

The paper determines the cryo-EM structure of the adenosine A2A receptor bound to NECA and coupled to an engineered G protein, revealing structural similarities and flexibility compared to a crystal structure.

bioRxiv · Feb 19, 2018Biophysics