Michael Grabe

This paper identifies two strategies to modulate the Orf9b-Tom70 interaction by screening for small molecules that either stabilize Orf9b dimer or block its binding to Tom70, with potential to restore interferon signaling against SARS-CoV-2.

This paper uses molecular dynamics simulations to show that hydrophobic mismatch between transmembrane proteins and lipid membranes leads to lipid sorting based on tail unsaturation.

The paper identifies aliphatic-to-threonine substitutions as a conserved adaptation in mitochondrial membrane proteins that balances hydrophilicity and hydrophobicity requirements.

The paper uses molecular dynamics simulations and electrophysiology to study conformational changes in TMEM16A upon inhibitor removal, revealing conductive and non-conductive states and mechanisms of Ca2+-dependent gating.

This study identifies CLCC1 as a regulator of hepatic neutral lipid flux and nuclear pore complex assembly through CRISPR screens and functional analyses.

This paper compares multislice projections of MD simulations with cryoEM to identify structural prediction errors in coarse-grained and all-atom MD simulations of membranes.

The paper investigates how PI(3,5)P2 regulates lysosomal pH by inhibiting ClC-7, showing structural changes in ClC-7 upon PI(3,5)P2 binding and linking this to disease mutations.

This study develops a biophysical model to show how lipid binding and mutations affect Orf9b's conformational equilibrium and its interaction with Tom70, influencing interferon suppression.

The paper investigates how cytosolic ion concentrations affect TGN/EE luminal pH and shows that this process is crucial for plant salt tolerance.

The paper develops a cooperative binding model for ligands to protein fibrils, relating measured EC50 and IC50 values to intrinsic affinity and cooperativity.

The paper develops a cell-based phospholipid scrambling assay to show that TMEM16F preferentially scrambles phosphatidylserine and phosphatidylcholine over phosphatidylethanolamine.

This paper designs dynamic proteins with switch-like behavior using deep learning, validated by structure solving and simulations showing controllable conformational changes.

This paper presents cryo-EM structures of human K2P13.1 (THIK-1) revealing a novel hydrophilic pore restriction and lipid cofactor site, with implications for modulator development.

This study uses simulations to show that TMEM16 proteins primarily scramble lipids in an open groove when Ca2+ is bound, but also do so at the dimer interface when Ca2+ is absent.