Large Distance Modification of Newtonian Potential and Structure Formation in Universe

In this paper, we study the effects of super-light brane world perturbative modes on structure formation in our universe. As these modes modify the large distance behavior of Newtonian potential, they effect the clustering of a system of galaxies. So, we explicitly calculate the clustering of galaxies interacting through such a modified Newtonian potential. We use a suitable approximation for analyzing this system of galaxies, and discuss the validity of such approximations. We observe that such corrections also modify the virial theorem for such a system of galaxies.Comment: 13 pages, 3 captioned figure

Impact of Shape and Pore Size of Mesoporous Silica Nanoparticles on Serum Protein Adsorption and RBCs Hemolysis

With the rapid development of nanotechnology, mesoporous silica nanoparticles (MSNs) with numerous forms and structures have been synthesized and extensively applied in biomedicine in the past decades. However, our knowledge about the biocompatibility of the developed MSNs has not matched their development. Therefore, in this work, we have synthesized sphere-shaped MSNs with different pore scales (<i>s</i>-SPs and <i>l</i>-SPs) and rod-shape (RPs-3) MSNs to evaluate the influence of the morphology and pore size on their interaction with serum proteins and red blood cells (RBCs). The adsorption of human albumin (HSA), globulin (HGG), and fibrinogen (HSF) onto different kinds of MSNs has been analyzed by pseudo second-order kinetic model, and the conformational changes of the adsorbed proteins have been studied by FTIR spectroscopy. We find that the conformation of absorbed HSA and HSF, while not HGG, will be affected by the pore size and morphology of the MSNs. The conformational changes of the adsorbed proteins will further affect their saturated adsorption capacity. However, the initial adsorption rate is only determined by the property of MSNs and proteins. Additional hemolysis assay shows that the pore size and morphology of the MSNs will also affect their hemolytic activity in RBCs which will be extremely depressed by the formation of protein corona. These systematic studies will provide an overall understanding in the blood compatibility of MSNs as well as useful guidelines for fabrication of blood-compatible nanomaterials

Additional file 4: of Tricho-rhino-phalangeal syndrome 1 protein functions as a scaffold required for ubiquitin-specific protease 4-directed histone deacetylase 2 de-ubiquitination and tumor growth

Figure S2. (A and B) USP4 protein and mRNA levels were unaffected upon silencing of TRPS1 in T47D cell line. (JPG 1408 kb

Additional file 6: of Tricho-rhino-phalangeal syndrome 1 protein functions as a scaffold required for ubiquitin-specific protease 4-directed histone deacetylase 2 de-ubiquitination and tumor growth

Table S3. A, B Differential expressed genes upon silencing of TRPS1 or HDAC2 in MCF7 by RNA-sequencing. (XLSX 2609 kb