We report the fabrication and characterization of ZnO nanowire memory devices using a ferroelectric Pb(Zr(0.3)Ti(0.7))O(3) (PZT) film as the gate dielectric and the charge storage medium. With a comparison to nanowire transistors based on SiO(2) gate oxide, the devices were evaluated in terms of their electric transport, retention, and endurance performance. Memory effects are observed as characterized by an eminent counterclockwise loop in I-V(g) curves, which is attributed to the switchable remnant polarization of PZT. The single-nanowire device exhibits a high (up to 10(3)) on/off ratio at zero gate voltage. Our results give a proof-of-principle demonstration of the memory application based on a combination of nanowires (as channels) and ferroelectric films (as gate oxide).

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The human ABCB1 protein, (P-glycoprotein or MDR1) is a membrane-bound glycoprotein that harnesses the energy of ATP hydrolysis to drive the unidirectional transport of substrates from the cytoplasm to the extracellular space. As a large range of therapeutic agents are known substrates of ABCB1 protein, its role in the onset of multidrug resistance has been the focus of much research. This role has been of particular interest in the field of pharmacogenomics where genetic variation within the ABCB1 gene, particularly in the form of single nucleotide polymorphisms (SNPs), is believed to contribute to inter-individual variation in ABCB1 function and drug response. In this review we provide an update on the influence of coding region SNPs within the ABCB1 gene on drug pharmacokinetics. By utilizing the crystal structure of the mouse ABCB1 homolog (Abcb1a), which is 87% homologous to the human sequence, we accompany this discussion with a graphical representation of residue location for amino acids corresponding to human ABCB1 coding region SNPs. Also, an assessment of residue conservation, which is calculated following multiple sequence alignment of 11 confirmed sequences of ABCB1 homologs, is presented and discussed. Superimposing a 'heat map' of residue homology to the Abcb1a crystal structure has permitted additional insights into both the conservation of individual residues and the conservation of their immediate surroundings. Such graphical representation of residue location and conservation supplements this update of ABCB1 pharmacogenetics to help clarify the often confounding reports on the influence of ABCB1 polymorphisms on drug pharmacokinetics and response.

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