Author

P. McCormick

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· 1 Biophysics· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein structure prediction· 2 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Organism:human· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Brenlla-Lopez· 1 shared A. G. Beck-Sickinger· 1 shared A. Morton· 1 shared A. Rainish· 1 shared C. Lin· 1 shared D. Matzov· 1 shared D. R. Huxley· 1 shared D. Weikert· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperPharmacology & Toxicology

A. Brenlla-Lopez

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Author profile →

3 papers

Recent·Most cited

Intracellular binding pocket revealed in the human bitter taste receptor TAS2R14

L. Peri, D. Matzov, D. R. Huxley, A. Rainish, F. Fierro, L. Sapir, T. Pfeiffer, L. Waterloo, H. Huebner, D. Weikert, Y. Peleg, P. Gmeiner, P. Mccormick, M. Y. Niv, M. Shalev-Benami

The paper reveals the cryo-EM structure of hTAS2R14 bound to FFA and gustducin, showing dual binding pockets and supporting a dual binding mode for FFA.

bioRxiv · Apr 10, 2024Biochemistry

MRAP2 modifies signaling and oligomerization state of the melanocortin-4 receptor

I. Sohail, S.-A. Laurin, G. Kleinau, V. Chunilal, A. Morton, A. Brenlla-Lopez, Z. C. U. Kagiali, J. A. Tello, M.-J. Blouin, A. G. Beck-Sickinger, M. J. Lohse, P. Scheerer, M. Bouvier, P. McCormick, P. Annibale, H. Biebermann

This study shows that MRAP2 modifies MC4R signaling and oligomerization, enhancing G protein signaling while reducing beta-arrestin2 recruitment and receptor internalization.

bioRxiv · Apr 9, 2024Pharmacology & Toxicology

Structural basis of main proteases of coronavirus bound to drug candidate PF-07321332

J. Li, C. Lin, X. Zhou, F. Zhong, P. Zeng, H. Jiang, Y. Yang, P. McCormick, Y. Fu, J. Zhang

This study reports crystal structures of SARS-CoV-2, SARS-CoV, and MERS-CoV main proteases bound to PF-07321332, revealing conserved ligand-binding sites and insights into inhibitor mechanism.

bioRxiv · Nov 5, 2021Biophysics