94 GHz dual-reflector antenna with reflectarray subreflector

The design, construction and measured performance is described of an offset parabolic reflector antenna which employs a reflectarray subreflector to tilt the focused beam from the boresight direction at 94 GHz. An analysis technique based on the method of moments (MoM) is used to design the dual-reflector antenna. Numerical simulations were employed to demonstrate that the high gain pattern of the antenna can be tilted to a predetermined angle by introducing a progressive phase shift across the aperture of the reflectarray. Experimental validation of the approach was made by constructing a 28 × 28 element patch reflectarray which was designed to deflect the beam 5° from the boresight direction in the azimuth plane. The array was printed on a 115 µm thick metal backed quartz wafer and the radiation patterns of the dual reflector antenna were measured from 92.6-95.5 GHz. The experimental results are used to validate the analysis technique by comparing the radiation patterns and the reduction in the peak gain due to beam deflection from the boresight direction. Moreover the results demonstrate that this design concept can be developed further to create an electronically scanned dual reflector antenna by using a tunable reflectarray subreflector.

Ran GTPase in Nuclear Envelope Formation and Cancer Metastasis

Ran is a small ras-related GTPase that controls the nucleocytoplasmic exchange of macromolecules across the nuclear envelope. It binds to chromatin early during nuclear formation and has important roles during the eukaryotic cell cycle, where it regulates mitotic spindle assembly, nuclear envelope formation and cell cycle checkpoint control. Like other GTPases, Ran relies on the cycling between GTP-bound and GDP-bound conformations to interact with effector proteins and regulate these processes. In nucleocytoplasmic transport, Ran shuttles across the nuclear envelope through nuclear pores. It is concentrated in the nucleus by an active import mechanism where it generates a high concentration of RanGTP by nucleotide exchange. It controls the assembly and disassembly of a range of complexes that are formed between Ran-binding proteins and cellular cargo to maintain rapid nuclear transport. Ran also has been identified as an essential protein in nuclear envelope formation in eukaryotes. This mechanism is dependent on importin-β, which regulates the assembly of further complexes important in this process, such as Nup107–Nup160. A strong body of evidence is emerging implicating Ran as a key protein in the metastatic progression of cancer. Ran is overexpressed in a range of tumors, such as breast and renal, and these perturbed levels are associated with local invasion, metastasis and reduced patient survival. Furthermore, tumors with oncogenic KRAS or PIK3CA mutations are addicted to Ran expression, which yields exciting future therapeutic opportunities