Cornelius Gati

Figure 1. Cryo-EM of abundant protein complexes in native membranes.

Figure 2. Cryo-EM of membrane proteins in vesicles.

Figure 3. 3D reconstruction of V-ATPase in native synaptic vesicle membranes.

Figure 4. Generation of membrane vesicles for structure determination of proteins in their native lipid bilayer.

I've written a review on what I think is an extremely exciting direction in cryo-EM:

Cryo-EM of endogenous membrane proteins in their native lipid bilayer

Open access in Quarterly Reviews of Biophysics:
doi.org/10.1017/S003...

I am incredibly excited to share that I will start my independent lab at the @unidue-zmb.bsky.social at the @unidue.bsky.social as Junior Professor of Cellular Biochemistry. Research in my lab has the goal to decipher the ubiquitin code!
There are multiple open positions!
(1/3)

CLCC1 promotes hepatic neutral lipid flux and nuclear pore complex assembly - Nature CRISPR–Cas9 screening identifies CLCC1 as a factor that increases neutral lipid flux to prevent hepatic steatosis and promotes nuclear pore complex assembly by promoting membrane bending and fusi...

Sooo happy to share our new paper in @nature.com “CLCC1 promotes hepatic neutral lipid flux and nuclear pore complex assembly.” A terrific collaboration with @arrudalab.bsky.social, led by co–first authors Alyssa Mathiowetz and Emily Maymand.
www.nature.com/articles/s41...

I am so grateful to the Blavatnik Family Foundation and the New York Academy of Sciences for this honor. Can’t wait to be back to the lab and celebrate with lab members on this special recognition of their hard work.

ChimeraX screenshot showing CubeNTube plugin.

The new ChimeraX CubeNTube plugin allows erasing parts of maps using cube, cylinder, and custom shapes and has undo. Created by Tamino Cairoli. Available from ChimeraX menu Tools / More Tools....

Deep-learning methods for contrast enhancement and artifact reduction in cryo-electron tomography: a systematic analysis of the state of the art and proposed improvements pubmed.ncbi.nlm.nih.gov/41711797/ #cryoEM

Our study of the CAT1 amino acid transporter and viral receptor is now online in @natcomms.nature.com!

Spearheaded by the incredibly talented @mingda-ye.bsky.social with colleagues from @cmd.ox.ac.uk, Strubi, CAMS Oxford Institute, @ndm.ox.ac.uk, and supported by the IM2PACT consortium.

New paper from my group in @science.org : "A small polymerase ribozyme that can synthesise itself and its complementary strand" www.science.org/doi/10.1126/...
Outstanding work by @edogia.bsky.social

Looking forward to #BPS2026 in San Francisco?

Come by the NIH sponsored Transformative High-Resolution Cryo-Electron Microscopy National Centers for #CryoEM at booth 410.

Our mission is to broaden access to high-resolution cryo-electron microscopy and tomography technologies - cryoemcenters.org

Fantastic news: our very own Aaliyah Tyson has been awarded a prestigious R36 NIDA Substance Use/Substance Use Disorder Dissertation Research Award.
Many congratulations to this very well deserved recognition!

Are you a cell biologist who secretly thinks cellular cryo-electron tomography is just George Palade-era EM, but fancier?

Join this webinar to see how modern #teamtomo has shifted from pretty pictures to quantitative, local membrane biology, and how that changes the questions we can ask.

Kicking off the new year with a completely refreshed look for the Filizola Lab website. Happy 2026, everyone! www.filizolalab.org

I’m excited to share that I’ve joined the Editorial Board of the Journal of Biological Chemistry. I look forward to serving this incredible community journal and engaging with exciting science! @asbmb.bsky.social 🧪

They grow up so fast! Huge congratulations to the newly minted Dr. Saif Khan, the first graduate of our lab. 🎓 He delivered a spectacular defense on our recent work in opioid receptor pharmacology. We’ll miss you greatly and wish you every success in your next chapter!

Structure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum AMPA receptors (AMPARs) are multimodal transducers of glutamatergic signals throughout the brain. Their diversity is exemplified in the cerebellum; at afferent synapses, AMPARs mediate high-frequency ...

Structure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum | Science www.science.org/doi/10.1126/...

Excited to share our latest @nature.com: How does naloxone (Narcan) stop an opioid overdose? We determined the first GDP-bound μ-opioid receptor–G protein structures and found naloxone traps a novel "latent” state, preventing GDP release and G protein activation.💊🧪 🧵👇 www.nature.com/articles/s41...

Come join our team! The deadline is December 7, but the application is quick. Only a cover letter, CV, and a short Research Highlight are needed #chemsky #chemjob #chembio

Bidirectional communication between nucleotide and substrate binding sites in a type IV multidrug ABC transporter Nature Communications - The communication hinge, found in type IV ABC transporters, forms a bidirectional communication between ATP- and substrate-binding sites. This is an unexplored allosteric...

🧪How does an ABC transporter 'know' nucleotides & substrates bound to far apart binding sites? Using 1H15N, 19F NMR, HDX-MS, PET-FCS & activity assays with Neuweiler, Marcoux, Orelle & Jault labs, we found a communication hinge! 😍🥳

@microverse.bsky.social @lifeprofile.bsky.social

rdcu.be/ePm4C

Structural snapshots capture nucleotide release at the μ-opioid receptor pubmed.ncbi.nlm.nih.gov/41193810/ #cryoEM

Structural snapshots capture nucleotide release at the μ-opioid receptor

Great structure work about MOR binding states from the Cornelius Gati lab! Congrats to all the authors, particularly Saif Khan. Looking forward!

Remember, remember the 5th of November. Today marks the tenth anniversary of my PhD defense. I'm officially old now. (fin)

Huge thanks to our amazing team — and especially to my first graduate student Saif Khan (second from right), who spearheaded this project with incredible drive and creativity. Credit also goes to him for the stunning movie in the first post. (8/n)

Supported by extensive molecular dynamics simulations, we assembled the first half of the G protein activation pathway — a major step toward understanding how GPCRs translate drug binding into cellular signaling. (7/n)

The mind-blowing part: a “latent” state — where the receptor and G protein both appear inactive, yet remain bound to each other. Naloxone traps this state, stalling activation. This likely explains its ability to block opioid signaling so effectively. (6/n)

To explore this further, we determined a series of four novel GDP-bound MOR–G protein structures — the first of their kind for any GPCR. Remarkably, the distribution of these states correlated with the efficacy of the respective ligand. (5/n)

We developed a simple BRET-based assay — “nuc-BRET” — to approximate the nucleotide affinity (EC₅₀) of MOR–G protein complexes. We found a clear inverse correlation: Antagonists stabilize GDP binding, while agonists promote its release for GTP exchange. (4/n)

Recent smFRET and DEER studies from the Kobilka lab (Zhang et al. 2024 Nature; Deutsch et al. 2025 bioRxiv, etc.) revealed clear links between MOR conformations and ligand efficacy. These findings inspired our next step. (3/n)

A big research theme in our lab: how do different drugs acting on the same receptor cause different levels of activity? This concept — called efficacy — lies at the heart of receptor pharmacology and drug discovery efforts. (2/n)

μ-opioid receptors (MOR) mainly signal by activating G proteins. This happens when the G protein swaps its bound GDP molecule for GTP — triggering subunit dissociation and downstream signaling. A classic textbook cartoon, from Alberts et al. - Molecular Biology of the Cell: (1/n)