A5029581589- Receptor Mechanisms and Signaling
- Neuropeptides and Animal Physiology
- Lipid Membrane Structure and Behavior
- Monoclonal and Polyclonal Antibodies Research
- Mass Spectrometry Techniques and Applications
- RNA and protein synthesis mechanisms
- Neuroscience and Neuropharmacology Research
- Protein Kinase Regulation and GTPase Signaling
- Cellular transport and secretion
- Advanced Electron Microscopy Techniques and Applications
- RNA modifications and cancer
- Protein Structure and Dynamics
- RNA Research and Splicing
- Chemical Synthesis and Analysis
- Cancer-related gene regulation
- Chemical synthesis and alkaloids
- Epigenetics and DNA Methylation
- Pharmacological Receptor Mechanisms and Effects
- Glycosylation and Glycoproteins Research
- Microbial Natural Products and Biosynthesis
- Photoreceptor and optogenetics research
- Microtubule and mitosis dynamics
- Supramolecular Self-Assembly in Materials
- Psychedelics and Drug Studies
- Retinal Development and Disorders
Stanford University
2017-2025
Abbott (Sweden)
2025
University of Michigan
2010-2023
SLAC National Accelerator Laboratory
2019-2023
Stanford Medicine
2017-2018
University of Alberta
2017
Washtenaw Community College
2012-2015
Michigan United
2012-2015
Analysis Group (United States)
2013
Ann Arbor Center for Independent Living
2013
Flaviviruses, the human pathogens responsible for dengue fever, West Nile tick-borne encephalitis, and yellow are endemic in tropical temperate parts of world. The flavivirus nonstructural protein 1 (NS1) functions genome replication as an intracellular dimer immune system evasion a secreted hexamer. We report crystal structures full-length, glycosylated NS1 from viruses. hexamer is similar to solution visualized by single-particle electron microscopy. Recombinant binds lipid bilayers...
β-Arrestins (βarrs) interact with G protein-coupled receptors (GPCRs) to desensitize protein signaling, initiate signaling on their own, and mediate receptor endocytosis. Prior structural studies have revealed two unique conformations of GPCR-βarr complexes: the "tail" conformation, βarr primarily coupled phosphorylated GPCR C-terminal tail, "core" where, in addition is further engaged transmembrane core. However, relationship these distinct various functions βarrs unknown. Here, we created...
Choosing a partner G protein–coupled receptors (GPCRs) bind ligands outside the cell and trigger events inside by selectively binding activating specific proteins. The selectivity occurs even among highly related GPCRs. For example, five subtypes of muscarinic acetylcholine (M1R to M5R) play different roles in nervous system Maeda et al. determined cryo–electron microscopy structures M1R M2R bound their respective A side-by-side comparison provided molecular understanding protein–coupling...
The active-state complex between an agonist-bound receptor and a guanine nucleotide-free G protein represents the fundamental signaling assembly for majority of hormone neurotransmitter signaling. We applied single-particle electron microscopy (EM) analysis to examine architecture agonist-occupied β 2 -adrenoceptor (β AR) in with heterotrimeric Gs (Gαsβγ). EM 2D averages 3D reconstructions detergent-solubilized reveal overall that is very good agreement crystal structure ternary complex....
Abstract Single-particle cryo-electron microscopy (cryo-EM) has recently enabled high-resolution structure determination of numerous biological macromolecular complexes. Despite this progress, the application cryo-EM to G protein coupled receptors (GPCRs) in complex with heterotrimeric proteins remains challenging, owning both relative small size and limited stability these assemblies. Here we describe development antibody fragments that bind stabilize GPCR-G complexes for cryo-EM. One...