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Background The arcuate foramen is an anatomic variant that is thought to arise from ossification of the posterior atlanto-occipital membrane. Owing to potential entrapment of the vertebral artery segment that traverses the foramen, vertebrobasilar ischemia may occur, and the person may experience vertigo, headache, or neck pain. Methods We reviewed the literature regarding anatomy (both human and comparative), embryology, nomenclature, pathology, and surgery of the arcuate foramen. Results Surgically, the presence of an arcuate foramen is important when placing screws into lateral masses of the atlas. In these cases, the screws can damage the V3 segment of the vertebral artery and/or the suboccipital nerve. Conclusions It is important to review the current literature on the arcuate foramen to further understand its morphology and clinical relevance.

Aptamer-immobilized gold nanoparticles (AuNP)/single-walled carbon nanotube (SWNT) field effect transistor (FET) sensors are fabricated for the detection of the ErbB2 protein. The 5′-thiol-modified 40-mer naphthyl DNA aptamers are immobilized on the AuNPs using well-established thiol chemistry. Carbodiimidazole-activated tween 20 (CDI-tween 20) layers are also introduced to the surface of the SWNT via hydrophobic interactions for blocking the attachment of nonspecific substances. Quantitative experiments reveal the specific binding effect of ErbB2 on the electrical measurements by comparing the electrical responses from a non-specific binding and control aptamer experiments. Under the optimized experimental conditions, the ErbB2 protein is clearly detectable at concentrations as low as 10 pM. The self-gating effect of the present device with a concentric electrode is able to provide a reliable electrical measurement scheme by circumventing the limits related to the isoelectric point of the target protein. Furthermore, the sensor fabrication, treatment and detection method have the potential to meet the following requirements: simplicity, portability, low cost and no need for bulky optical instruments.

Brain accumulation of soluble oligomers of the amyloid-β peptide (AβOs) is increasingly considered a key early event in the pathogenesis of Alzheimer's disease (AD). A variety of AβO species have been identified, both in vitro and in vivo, ranging from dimers to 24mers and higher order oligomers. However, there is no consensus in the literature regarding which AβO species are most germane to AD pathogenesis. Antibodies capable of specifically recognizing defined subpopulations of AβOs would be a valuable asset in the identification, isolation, and characterization of AD-relevant AβO species. Here, we report the characterization of a human single chain antibody fragment (scFv) denoted NUsc1, one of a number of scFvs we have identified that stringently distinguish AβOs from both monomeric and fibrillar Aβ. NUsc1 readily detected AβOs previously bound to dendrites in cultured hippocampal neurons. In addition, NUsc1 blocked AβO binding and reduced AβO-induced neuronal oxidative stress and tau hyperphosphorylation in cultured neurons. NUsc1 further distinguished brain extracts from AD-transgenic mice from wild type (WT) mice, and detected endogenous AβOs in fixed AD brain tissue and AD brain extracts. Biochemical analyses indicated that NUsc1 targets a subpopulation of AβOs with apparent molecular mass greater than 50 kDa. Results indicate that NUsc1 targets a particular AβO species relevant to AD pathogenesis, and suggest that NUsc1 may constitute an effective tool for AD diagnostics and therapeutics.