Janosch Ehrenmann

ORCID: 0000-0003-4447-9298
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About
Contact & Profiles
Research Areas
  • Receptor Mechanisms and Signaling
  • Neuropeptides and Animal Physiology
  • Chemical Synthesis and Analysis
  • Neuroendocrine regulation and behavior
  • Monoclonal and Polyclonal Antibodies Research
  • Protein Kinase Regulation and GTPase Signaling
  • Mass Spectrometry Techniques and Applications
  • Circadian rhythm and melatonin
  • Metabolism, Diabetes, and Cancer
  • Spectroscopy and Quantum Chemical Studies
  • Protein Structure and Dynamics
  • Bone health and treatments
  • Viral Infectious Diseases and Gene Expression in Insects
  • Diabetes Treatment and Management
  • Hypothalamic control of reproductive hormones
  • Enzyme Structure and Function

University of Zurich
2016-2022

Neurokinins (or tachykinins) are peptides that modulate a wide variety of human physiology through the neurokinin G protein-coupled receptor family, implicated in diverse array pathological processes. Here we report high-resolution crystal structures NK1 (NK1R) bound to two small-molecule antagonist therapeutics - aprepitant and netupitant progenitor CP-99,994. The reveal detailed interactions between clinically approved antagonists NK1R, which induce distinct conformation resulting an...

10.1038/s41467-018-07939-8 article EN cc-by Nature Communications 2018-12-28

Human oxytocin receptor structure reveals the basis for ligand recognition and allosteric modulation by lipids ions.

10.1126/sciadv.abb5419 article EN cc-by-nc Science Advances 2020-07-15

Abstract Despite recent successes, many G protein-coupled receptors (GPCRs) remained refractory to detailed molecular studies due insufficient production yields, even in the most sophisticated eukaryotic expression systems. Here we introduce a robust method employing directed evolution of GPCRs yeast that allows fast and efficient generation receptor variants which show strongly increased functional levels hosts. Shown by evolving three different this study, is widely applicable, for are...

10.1038/srep21508 article EN cc-by Scientific Reports 2016-02-25

Neuropeptide-bound NK 1 R:G protein complex structures explain mechanisms ranging from insurmountable antagonism to activation.

10.1126/sciadv.abk2872 article EN cc-by-nc Science Advances 2021-12-08

The small cyclic neuropeptide hormone oxytocin (OT) and its cognate receptor play a central role in the regulation of social behaviour sexual reproduction. Here we report single-particle cryo-electron microscopy structure active (OTR) complex with ligand oxytocin. Our provides high-resolution insights into OT binding mode, OTR activation mechanism as well subtype specificity within oxytocin/vasopressin family.

10.1038/s41467-022-31325-0 article EN cc-by Nature Communications 2022-07-18

Abstract Structural and biophysical studies as well drug screening approaches on G protein-coupled receptors (GPCRs) have been largely hampered by the poor properties low expression yields of this largest class integral membrane proteins. Thermostabilisation GPCRs introduction stabilising mutations has a key factor to overcome these limitations. However, labelled ligands with sufficient affinity, which are required for selective binding correctly folded receptor, often not available. Here we...

10.1038/srep21294 article EN cc-by Scientific Reports 2016-02-18

Abstract The peptide hormone oxytocin modulates socioemotional behaviour and sexual reproduction via the centrally expressed receptor (OTR) across several species. Here, we report crystal structure of human OTR in complex with retosiban, a non-peptide antagonist developed as an oral drug for prevention preterm labour. Our reveals insights into detailed interactions between G-protein coupled (GPCR) OTR-selective antagonist. observation extrahelical cholesterol molecule, binding unexpected...

10.1101/2020.02.21.958090 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-02-21

Abstract The small cyclic neuropeptide hormone oxytocin (OT) and its cognate receptor play a central role in the regulation of social behaviour sexual reproduction. Here we report single-particle cryo-electron microscopy structure active (OTR) complex with ligand oxytocin. Our provides high-resolution insights into OT binding mode, OTR activation mechanism as well subtype specificity within oxytocin/vasopressin family.

10.1101/2022.02.21.481286 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2022-02-22
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