Establishment of a Numerical Model for Sulfate Attacked Concrete Considering Multi-factors

Sulfate attack is one of the major durability problems of concrete structures, which is manifested by expansive cracks and deterioration of cement paste. In this study, a numerical model is proposed to predict the process of ionic diffusion into concrete under external sulfate attack. The chemical reaction and diffusion processes are considered in this model. Furthermore, the influence of calcium leaching, chemical activity of multi-ions, temperature and changes in porosity are also taken into account. The initial porosity and tortuosity are assumed to be homogeneous in concrete, and the chemical potential gradient is regarded as the driving force for ions migrating in pore solution. The modified Davies equation is employed to quantize interaction effect among different ions in solution. A temperature dependent parameter is introduced in the diffusion process of sulfate ion. The dissolution of solid calcium is divided into two stages referring to solid-liquid equilibrium curve of calcium ion. One is the dissolution of the calcium hydroxide, and the other is the decalcification of the calcium silicate hydrate. The influence of calcium leaching on porosity is further considered in diffusion coefficient. Moreover, changes in porosity due to formation of expansive ettringite are also reflected in the diffusion coefficient. Finally, a new numerical model is established and a comparison of the model prediction with the experimental results has been conducted. It is demonstrated that the established diffusion-reaction model can provide a better deterioration assessment of concrete structures exposed to sulfate attack

Angle-resolved broadband ferromagnetic resonance apparatus enabled through a spring-loaded sample mounting manipulator

Broadband ferromagnetic resonance is a useful technique to determine the magnetic anisotropy and study the magnetization dynamics of magnetic thin films. We report a spring-loaded sample loading manipulator for reliable sample mounting and rotation. The manipulator enables maximum signal, enhances system stability and is particularly useful for fully automated in-plane-field angle-resolved measurements. This angle-resolved broadband ferromagnetic resonance apparatus provides a viable method to study anisotropic damping and weak magnetic anisotropies, both vital for fundamental research and applications.Comment: 11pages,4 figure

PHF8-GLUL axis in lipid deposition and tumor growth of clear cell renal cell carcinoma.

For clear cell renal cell carcinoma (ccRCC), lipid deposition plays important roles in the development, metastasis, and drug resistance. However, the molecular mechanisms underlying lipid deposition in ccRCC remain largely unknown. By conducting an unbiased CRISPR-Cas9 screening, we identified the epigenetic regulator plant homeodomain finger protein 8 (PHF8) as an important regulator in ccRCC lipid deposition. Moreover, PHF8 is regulated by von Hippel-Lindau (VHL)/hypoxia-inducible factor (HIF) axis and essential for VHL deficiency-induced lipid deposition. PHF8 transcriptionally up-regulates glutamate-ammonia ligase (GLUL), which promotes the lipid deposition and ccRCC progression. Mechanistically, by forming a complex with c-MYC, PHF8 up-regulates TEA domain transcription factor 1 (TEAD1) in a histone demethylation-dependent manner. Subsequently, TEAD1 up-regulates GLUL transcriptionally. Pharmacological inhibition of GLUL by l-methionine sulfoximine not only repressed ccRCC lipid deposition and tumor growth but also enhanced the anticancer effects of everolimus. Thus, the PHF8-GLUL axis represents a potential therapeutic target for ccRCC treatment

Modeling a New Water Channel That Allows SET9 to Dimethylate p53

SET9, a protein lysine methyltransferase, has been thought to be capable of transferring only one methyl group to target lysine residues. However, some reports have pointed out that SET9 can dimethylate Lys372 of p53 (p53-K372) and Lys4 of histone H3 (H3-K4). In order to understand how p53 can be dimethylated by SET9, we measured the radius of the channel that surrounds p53-K372, first on the basis of the crystal structure of SET9, and we show that the channel is not suitable for water movement. Second, molecular dynamic (MD) simulations were carried out for 204 ns on the crystal structure of SET9. The results show that water leaves the active site of SET9 through a new channel, which is made of G292, A295, Y305 and Y335. In addition, the results of molecular docking and MD simulations indicate that the new water channel continues to remain open when S-adenosyl-L-methionine (AdoMet) or S-adenosyl-L-homocysteine (AdoHcy) is bound to SET9. The changes in the radii of these two channels were measured in the equilibrium phase at the constant temperature of 300 K. The results indicate that the first channel still does not allow water to get into or out of the active site, but the new channel is large enough to allow this water to circulate. Our results indicate that water can be removed from the active site, an essential process for allowing the dimethylation reaction to occur