Bruce A. Bamber

Pharmacological characterization of the homomeric and heteromeric UNC-49 GABA receptors in C. elegans.

The composition of the GABA receptor at the Caenorhabditis elegans neuromuscular junction.

Presynaptic terminals independently regulate synaptic clustering and autophagy of GABAA receptors in Caenorhabditis elegans.

Residues in the first transmembrane domain of the Caenorhabditis elegans GABA(A) receptor confer sensitivity to the neurosteroid pregnenolone sulfate.

Shaping cellular form and function by autophagy.

The neurosteroids dehydroepiandrosterone sulfate and pregnenolone sulfate inhibit the UNC-49 GABA receptor through a common set of residues.

Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes.

Multiple roles for the first transmembrane domain of GABAA receptor subunits in neurosteroid modulation and spontaneous channel activity.

Regulated lysosomal trafficking as a mechanism for regulating GABAA receptor abundance at synapses in Caenorhabditis elegans.