Marcel P Goldschen-Ohm

This study shows introducing a proline at site 2 in the α1 M2-M3 linker of GABAARs enhances GABA-sensitivity and spontaneous activity, suggesting it relieves a molecular brake on channel activation.

The paper uses nanophotonic methods to observe sequential ligand binding to a cyclic nucleotide-gated ion channel at single-molecule resolution, revealing cooperative binding and intermediate states.

The paper identifies a conserved atomic interaction in inhibitory neurotransmitter receptors that stabilizes channel gating and explains disease-linked mutations.

This study stabilizes an open-state conformation of the α1β3γ2 GABAAR using mutations and simulations, revealing how allosteric modulators and antagonists affect receptor gating.

The paper investigates the effect of the GABAA receptor α4 subunit variant Ile114Asn on membrane expression when combined with β3 and δ subunits, finding reduced maximal GABA-elicited currents.

The paper identifies a single main-chain hydrogen bond in the β2 subunit M2-M3 linker that inhibits GABAA receptor pore opening and is required to keep the unliganded channel closed.

The paper introduces smBEVO, a computer vision method for efficiently correcting baseline drift in single-molecule time series.

The paper develops an unsupervised method to select the optimal objective criterion for the DISC algorithm, improving performance on single-molecule fluorescence time series with varying signal-to-noise and time window lengths.

The paper identifies a critical residue in the α1M2-M3 linker that regulates GABAA receptor pore gating by diazepam, showing how it enhances the drug's effect on channel opening.