Alpha-band (8-14 Hz) oscillatory EEG activity was examined with high-density scalp electrical recording during the cue-stimulus interval of an endogenous spatial cueing paradigm. In different blocks, cued spatial locations (left or right) were in either the upper or lower visual field, and attended stimuli were either oriented Ts or moving dots. Distractor stimuli were equally likely in the uncued hemifield. Sustained focal increases of alpha-band activity were seen over occipital cortex contralateral to the direction of the to-be-ignored location (ipsilateral to the cued direction of attention) before onset of the to-be-attended stimulus. The focus of alpha-band activity also moved depending on whether cued locations were in the upper or lower field. Results are consistent with active gating of uncued spatial locations.

Comparing retention rates of new AEDs can provide useful insight into their tolerability and efficacy. This study showed highest retention rate with LTG, which was significantly different from ZNS (p=0.0025), LEV (p<0.0001), OXC (p=0.0024), and TPM (p<0.0001). Beside ineffectiveness, other leading causes of discontinuation were adverse behavioral effects with LEV, rash with LTG and OXC, and sedation for TPM and ZNS.

Single-chain Fvs (scFvs) are commonly used building blocks for creating engineered diagnostic and therapeutic antibody molecules. Bispecific antibodies (BsAbs) hold particular interest due to their ability to simultaneously bind and engage two distinct targets. We describe a technology for producing stable, scalable IgG-like bispecific and multivalent antibodies based on methods for rapidly engineering thermally stable scFvs. Focused libraries of mutant scFvs were designed using a combination of sequence-based statistical analyses and structure-, and knowledge-based methods. Libraries encoding these designs were expressed in E. coli and culture supernatants-containing soluble scFvs screened in a high-throughput assay incorporating a thermal challenge prior to an antigen-binding assay. Thermally stable scFvs were identified that retain full antigen-binding affinity. Single mutations were found that increased the measured T(m) of either the V(H) or V(L) domain by as much as 14 degrees C relative to the wild-type scFv. Combinations of mutations further increased the T(m) by as much as an additional 12 degrees C. Introduction of a stability-engineered scFv as part of an IgG-like BsAb enabled scalable production and purification of BsAb with favorable biophysical properties.