Structure, magnetic properties, and thermal stability of Sm(1-x)Tm_xCo_5compounds

Structure, magnetic properties, and thermal stability of ternary Sm1-xTmxCo5 compounds were studied via X-ray diffraction（XRD）, thermal magnetic analysis（TMA）, and magnetic measurements. XRD results show that all the compounds have a main phase of hexagonal CaCu5-type crystal structure with small amount of impurity phases; increasing Tm content is associated with contraction of the hexagonal unit cell in the direction of the c axis and expansion of the a and b parameters. TMA results indicate that the Curie temperature（TC） of Sm1-xTmxCo5 compounds gets higher with the increase in Tm content.Magnetic measurements show that both the magnetic anisotropy field（HA） and the magnetization at an applied field of 7 T（M7 T） decrease with the increase of Tm content. However, the thermal stability of both the HAand M7 Tof all the Tm doped compounds is remarkably improved compared with that of the pure SmCo5 compound, leading to the result that both the M7 Tand HAof Sm0.8Tm0.2Co5 .2are higher than those of SmCo5 compound at 473 K, which indicates the good potential of Tm doped compound in the practical applications at elevated temperature.

A sting in the tail： the N-terminal domain of the androgen receptor as a drug target

The role of androgen receptor （AR） in the initiation and progression of prostate cancer （PCa） is well established. Competitive inhibition of the AR ligand-binding domain （LBD） has been the staple of antiandrogen therapies employed to combat the disease in recent years. However, their efficacy has often been limited by the emergence of resistance, mediated through point mutations, and receptor truncations. As a result, the prognosis for patients with malignant castrate resistant disease remains poor. The amino-terminal domain （NTD） of the AR has been shown to be critical for AR function. Its modular activation function （AF-1） is important for both gene regulation and participation in protein-protein interactions. However, due to the intrinsically disordered structure of the domain, its potential as a candidate for therapeutic intervention has been dismissed in the past. The recent emergence of the small molecule EPI-O01 has provided evidence that AR-NTD can be targeted therapeutically, independent of the LBD. Targeting of AR-NTD has the potential to disrupt multiple intermolecular interactions between AR and its coregulatory binding partners, in addition to intramolecular cross-talk between the domains of the AR. Therapeutics targeting these protein-protein interactions or NTD directly should also have efficacy against emerging AR splice variants which may play a role in PCa progression. This review will discuss the role of intrinsic disorder in AR function and illustrate how emerging therapies might target NTD in PCa.