Author

B. Kobilka

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:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Assay:protein structure· 1

Frequent Co-Authors

P. Gmeiner· 2 shared A. El Daibani· 1 shared C. Chen· 1 shared C. Jin· 1 shared C. Sar· 1 shared E. O'Brien· 1 shared F. Hetzer· 1 shared G. Skiniotis· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersPharmacology & Toxicology

P. Gmeiner

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Conformational dynamics of the μ-opioid receptor determine ligand intrinsic efficacy

J. Zhao, M. Elgeti, E. O'Brien, C. Sar, A. El Daibani, J. Heng, X. Sun, T. Che, W. L. Hubbell, B. Kobilka, C. Chen

The paper uses biophysical techniques to show how ligand-induced conformational changes in the μ-opioid receptor affect its signaling efficacy.

bioRxiv · Apr 28, 2023 · PreprintBiochemistry

Structure-based Evolution of G protein-biased μ-opioid Receptor Agonists

H. Wang, F. Hetzer, W. Huang, Q. Qu, J. Meyerowitz, J. Kaindl, H. Huebner, G. Skiniotis, B. Kobilka, P. Gmeiner

The paper reports cryoEM structures of the μ-opioid receptor bound to biased agonists PZM21 and FH210, revealing structural basis for reduced β-arrestin recruitment and guiding development of safer analgesics.

bioRxiv · Mar 22, 2022Pharmacology & Toxicology

An allosteric ligand stabilizes distinct conformations in the M2 muscarinic acetylcholine receptor

J. Xu, H. Hubner, Y. Hu, X. Niu, P. Gmeiner, C. Jin, B. Kobilka

This study uses NMR to show that the PAM LY2119620 changes the structure and dynamics of M2R in both extracellular and G-protein coupling domains, stabilizing distinct conformations not seen with orthosteric agonists.

bioRxiv · Feb 14, 2021 · PreprintBiophysics