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gamma-Aminobutyric acid (GABA)ergic neurons are thought to play a key role both in visual processing and in the complex sensory-motor transformations that take place in the mammalian superior colliculus. To understand the organization of GABAergic neurons in the ferret superior colliculus, we applied antisera to several markers of GABAergic function, including GABA, two isoforms of its synthetic enzyme glutamic acid decarboxylase (GAD-65 and GAD-67), and the GABA transporter, GAT-1. We also applied antisera to several calcium binding proteins (calbindin [CB], calretinin [CR], and parvalbumin [PV]) and neuronal nitric oxide synthase (NOS), chemical markers that colocalize with GABA in some areas of the central nervous system. The distribution of GABAergic neurons in the ferret is similar to that of other mammalian species. GABAergic neurons in the ferret superior colliculus were small, morphologically diverse, and widely distributed throughout all layers of the colliculus. As has been shown in other mammalian species, neurons expressing PV, CB, CR, and NOS were differentially distributed in layers and patches throughout the ferret colliculus. None of these markers, however, showed a distribution that mirrored that of GABAergic neurons. Furthermore, few GABAergic neurons colocalized these neurochemical markers. Only 14% of GABAergic neurons in the superficial layers and 18% of neurons in the deeper layers colocalized PV, 14% of GABAergic neurons in the superficial layers and 10% in the deeper layers colocalized CB, and only 1% of GABAergic neurons in both the superficial and deep layers colocalized nitric oxide synthase. Thus, the arrangement of GABAergic neurons in the ferret superior colliculus is broadly distributed and is distinct from other recognized organizational patterns in the superior colliculus.

Two series of efavirenz analogues have been developed: one in which the cyclopropane ring has been replaced by small heterocycles and another in which the entire acetylenic side chain has been replaced by alkyloxy groups. Several members of both series show equivalent potency to efavirenz against both wild-type virus and the key K103N mutant.