Ordered ferromagnetic−nonmagnetic alloy (Co−Cu, Co−Ag and Fe−Ag) nanowire arrays embedded in the nanochannels of anodic aluminum membranes (AAM) have been fabricated by electrodeposition. Scanning electron microscopy and transmission electron microscopy observations reveal that these alloy nanowires are uniform in diameter and ordered. Magnetic measurements show that the perpendicular coercivity (H C ⊥) of these ordered nanowire arrays increases dramatically, reaches their maximum, and then decreases sharply during the annealing process. However, there is not much change of the parallel coercivity (H C ∥) for these alloy nanowire arrays in the same annealing conditions. This phenomenon should be contributed to the special structure of the nanowires/AAM.

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UGTs play crucial roles in the metabolism and detoxification of both endogenous and xenobiotic compounds. The key roles of UGTs in human health have garnered great interest in the design and development of specific probes for human UGTs. However, in contrast to other human enzymes, the probe substrates for human UGTs are rarely reported, owing to the highly overlapping substrate specificities of UGTs and the lack of the integrated crystal structures of UGTs. Over the past decades, many efforts are made to develop specific probe substrates for UGTs and use them in both basic research and drug discovery. This review focuses on recent progress in the development of probe substrates for UGTs and their biomedical applications. A long list of chemical probes for UGTs, including non-fluorescent and fluorescent probes along with their structural information and kinetic parameters, are prepared and analyzed. Additionally, challenges and future directions in this field are highlighted in the final section. All information and knowledge presented in this review provide practical tools/methods for measuring UGT activities in complex biological samples, which will be very helpful for rapid screening and characterization of UGT modulators, and for exploring the relevance of UGT enzymes to human diseases.