Author

R. D. Cone

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

L. E. Gimenez· 2 shared A. E. Bruno· 1 shared A. Peisley· 1 shared C. B. Jeppesen· 1 shared C. Q. Hernandez· 1 shared G. L. Millhauser· 1 shared K. W. Conde-Frieboes· 1 shared L. L. Britt· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersPharmacology & Toxicology

L. E. Gimenez

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Demonstration of a common DPhe7 to DNal(2')7 peptide ligand antagonist switch for the melanocortin-3 and melanocortin-4 receptors identifies systematic mischaracterization of the pharmacological properties of melanocortin peptides

L. E. Gimenez, T. A. Noblin, S. Y. Williams, S. Mullick Bagchi, R.-L. Ji, Y.-X. Tao, C. B. Jeppesen, K. W. Conde-Frieboes, T. K. Sawyer, P. Grieco, R. D. Cone

The paper identifies a systematic mischaracterization of melanocortin peptide pharmacology by showing DNal(2)7 residues act as antagonists, not agonists, for MC3R and MC4R.

bioRxiv · Jan 3, 2022Pharmacology & Toxicology

Membrane Orientation and Oligomerization of the Melanocortin Receptor Accessory Protein 2

V. Chen, A. E. Bruno, L. L. Britt, C. Q. Hernandez, L. E. Gimenez, A. Peisley, R. D. Cone, G. L. Millhauser

This study investigates the membrane orientation and dimerization of MRAP2, showing that its dimerization occurs through the transmembrane domain and forms higher-order oligomers.

bioRxiv · Aug 3, 2020Biochemistry