M
Margaret L. Warner
Researcher at University of Oklahoma Health Sciences Center
Publications - 8
Citations - 225
Margaret L. Warner is an academic researcher from University of Oklahoma Health Sciences Center. The author has contributed to research in topics: Calcitonin gene-related peptide & Receptor. The author has an hindex of 5, co-authored 8 publications receiving 164 citations.
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Journal ArticleDOI
Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor.
Jason M. Booe,Christopher S. Walker,James Barwell,Gabriel Kuteyi,John Simms,Muhammad A. Jamaluddin,Margaret L. Warner,Roslyn M. Bill,Paul W. R. Harris,Margaret A. Brimble,David R. Poyner,Debbie L. Hay,Augen A. Pioszak +12 more
TL;DR: The structures and accompanying pharmacology data reveal how a class of accessory membrane proteins modulate ligand binding of a GPCR and may inform drug development targeting CLR:RAMP complexes.
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Probing the Mechanism of Receptor Activity-Modifying Protein Modulation of GPCR Ligand Selectivity through Rational Design of Potent Adrenomedullin and Calcitonin Gene-Related Peptide Antagonists.
TL;DR: These potent peptide antagonists with altered selectivity inform the development of AM/CGRP-based pharmacological tools and support the hypothesis that RAMPs alter CLR ligand selectivity through allosteric effects and direct peptide contacts.
Journal ArticleDOI
Calcitonin receptor N-glycosylation enhances peptide hormone affinity by controlling receptor dynamics.
Sang Min Lee,Yejin Jeong,John Simms,Margaret L. Warner,David R. Poyner,Ka Young Chung,Augen A. Pioszak +6 more
TL;DR: The results reveal that N-glycosylation can modulate GPCR function by altering receptor dynamics and extended to RAMP-CTR amylin receptor complexes and was also conserved in the related CGRP receptor.
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Engineering High-Potency R-spondin Adult Stem Cell Growth Factors
TL;DR: The results reveal the molecular basis for RSPOs1–4 activity differences and suggest that signaling potency is determined by ternary complex formation ability, whereas efficacy depends on ZNRF3 recruitment.
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Structure–function analyses reveal a triple β-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design
TL;DR: Differences in how the three peptides engage the receptors are revealed, inform development of AM2/IMD-based pharmacological tools and therapeutics, and provide insights into RAMP modulation of receptor pharmacology are provided.