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Despite the overwhelming body of research suggesting that students with intellectual disability benefit from access to general education placements, students with intellectual disability continue to be educated primarily in segregated settings. Furthermore, the percentage of students with intellectual disability included in general education classrooms varies greatly among and within states across the United States. In an effort to explore such variability in New York State, we examined trends in general education placement rates of students with intellectual disability across districts and possible predictors of placement in regular classes. Results suggest that although descriptive patterns of placement exist, a more definitive explanation of variability requires a deeper analysis of policy and procedure at the district level. Keywords: intellectual disability, special education, least restrictive environment, inclusive education, A continued focus on access to placement in regular classes for students with disabilities is apparent in many countries (Ainscow & Cesar, 2006; Drudy & Kinsella, 2009). In fact, UNESCO [...]

Morphine suppresses respiration for longer periods of time when it is injected into the spinal column than when it is given intravenously. This indicates that morphine and other opioids can directly affect the central nervous system.

GABA is effective in the mammalian central nervous system through ionotropic (GABAA/C) receptors, producing fast synaptic inhibition and metabotropic (GABAB) receptors. The encoding gene of GABAB receptor GABABR1 was cloned. It is retained as an immature glycoprotein on intracellular membranes when expressed in mammalian cells. The complementary DNA encoding of a new GABAB subtype, GABABR2, has been cloned. It is found to form heterodimers with GABABR1 via interactions at the intracellular carboxy-terminal tails.

The E1B 19k protein is part of a DNA virus and aids the virus' apoptosis-inhibiting characteristics. This inhibiting mechanism appears to involve binding a new member of the bcl-2 family called bak for bcl-2 homologous antagonist/killer. Enhanced apoptosis occurs when bak is overexpressed, indicating that E1B 19k inhibits apoptosis by binding one of the genes producing proteins responsible for apoptosis. E1B 19k appears to be a homologue of Bcl-xL which is the cellular protein equivalent in that it also binds bcl-2 proteins.

The basic module of signal transduction that involves G-protein-coupled receptors is usually portrayed as comprising a receptor, a heterotrimeric G protein and an effector. It is now well established that regulated interactions between receptors and arrestins, and between G proteins and regulators of G-protein signalling alter the effectiveness and kinetics of information transfer. However, more recent studies have begun to identify a host of other proteins that interact selectively with individual receptors at both the intracellular and extracellular face of the membrane. Although the functional relevance of many of these interactions is only beginning to be understood, current information indicates that these interactions might determine receptor properties, such as cellular compartmentalization or signal selection, and can promote protein scaffolding into complexes that integrate function.

The molecular nature of the metabotropic [GABA.sub.B] receptor was for some time a mystery, however it was recently discovered that two related G-protein-coupled receptors have to heterodimerize to form the functional [GABA.sub.B] receptor at the cell surface. This review discusses the most recent findings in the rapidly expanding field of [GABA.sub.B] receptor research, and includes a summary of all splice variants of both receptor subunits identified to date. It also evaluates emerging evidence that certain splice variants might play a role in determining pharmacologically distinguishable receptors, and reviews receptor localization at the sub-cellular level and involvement in neuronal development.

[Gamma]-Aminobutyric acid type B ([GABA.sub.B]) receptors mediate the metabotropic actions of the inhibitory neurotransmitter GABA. These seven-transmembrane receptors are known to signal primarily through activation of G proteins to modulate the action of ion channels or second messengers. The functional [GABA.sub.B] receptor is made up of a heterodimer consisting of two subunits, [GABA.sub.B]-R1 and [GABA.sub.B]-R2, which interact via coiled-coil domains in their C-terminal tails. By using a yeast two-hybrid approach, we have identified direct interactions between the C-terminal tails of [GABA.sub.B]-R1 and [GABA.sub.B]-R2 with two related transcription factors, CREB2 (ATF4) and ATFx. In primary neuronal cultures as well in recombinant Chinese hamster ovary cells expressing [GABA.sub.B] receptors, CREB2 is localized within the cytoplasm as well as the nucleus. Activation of the [GABA.sub.B] receptor by the specific agonist baclofen leads to a marked translocation and accumulation of CREB2 from the cytoplasm into the nucleus. We demonstrate that receptor stimulation results in activation of transcription from a CREB2 responsive reporter gene. Such a signaling mechanism is unique among Family C G protein-coupled receptors and, in the case of the [GABA.sub.B] receptor and CREB2, may play a role in long-term changes in the nervous system.

Research was conducted to prove that the wild-type tube and pelle death domains in Drosophila bind together using the yeast two-hybrid system. Proteins corresponding to the death domains of tube and pelle were purified. It was observed that the proteins form corresponding heterodimeric complexes in vitro. Results demonstrate that specific interaction between the core death domains in tube and pelle found in vivo is recapitulated by the purified proteins in vitro.