M. Hotta

Cysteine Substitutions Define Etomidate Binding and Gating Linkages in the α-M1 Domain of γ-Aminobutyric Acid Type A (GABAA) Receptors*

R. Olsen, D. C. Chiara, S. Forman, 2013, The Journal of Biological Chemistry.

Mutations at Beta N265 in γ-Aminobutyric Acid Type A Receptors Alter Both Binding Affinity and Efficacy of Potent Anesthetics

S. Forman, David W. Pierce, Deirdre S. Stewart, 2014, PloS one.

Tryptophan and Cysteine Mutations in M1 Helices of &agr;1&bgr;3&ggr;2L &ggr;-Aminobutyric Acid Type A Receptors Indicate Distinct Intersubunit Sites for Four Intravenous Anesthetics and One Orphan Site

S. Forman, Anahita Nourmahnad, A. M. Ziemba, 2016, Anesthesiology.

State-Dependent Etomidate Occupancy of Its Allosteric Agonist Sites Measured in a Cysteine-Substituted GABAA Receptor

S. Forman, Rooma Desai, Deirdre S. Stewart, 2013, Molecular Pharmacology.