S matrix of collective field theory

By applying the Lehmann-Symanzik-Zimmermann (LSZ) reduction formalism, we study the S matrix of collective field theory in which fermi energy is larger than the height of potential. We consider the spatially symmetric and antisymmetric boundary conditions. The difference is that S matrices are proportional to momenta of external particles in antisymmetric boundary condition, while they are proportional to energies in symmetric boundary condition. To the order of $g_{st}^2$, we find simple formulas for the S matrix of general potential. As an application, we calculate the S matrix of a case which has been conjectured to describe a "naked singularity".Comment: 19 page, LaTe

Visualization of a mammalian mitochondrion by coherent x-ray diffractive imaging

We report a three dimensional (3D) quantitative visualization of a mammalian mitochondrion by coherent x-ray diffractive imaging (CXDI) using synchrotron radiation. The internal structures of a mitochondrion from a mouse embryonic fibroblast cell line (NIH3T3) were visualized by tomographic imaging at approximately 60 nm resolution without the need for sectioning or staining. The overall structure consisted of a high electron density region, composed of the outer and inner membranes and the cristae cluster, which enclosed the lower density mitochondrial matrix. The average mass density of the mitochondrion was about 1.36 g/cm3. Sectioned images of the cristae reveal that they have neither a baffle nor septa shape but were instead irregular. In addition, a high resolution, about 14 nm, 2D projection image was captured of a similar mitochondrion with the aid of strongly scattering Au reference objects. Obtaining 3D images at this improved resolution will allow CXDI to be an effective and nondestructive method for investigating the innate structure of mitochondria and other important life supporting organelles. ? 2017 The Author(s).11Ysciescopu

Novel D-hordein-like HMW glutenin sequences isolated from Psathyrostachys juncea by thermal asymmetric interlaced PCR

New high-molecular-weight glutenin (HMW glutenin) sequences isolated from six Psathyrostachys juncea accessions by thermal asymmetric interlaced PCR differ from previous sequences from this species. They showed novel modifications in all of the structural domains, with unique C-terminal residues, and their N-terminal lengths were the longest among the HMW glutenins reported to date. In their repetitive domains, there were three repeatable motif units: 13-residue [GYWH(/I/Y)YT(/Q)S(/T)VTSPQQ], hexapeptide (PGQGQQ), and tetrapeptide (ITVS). The 13-residue repeats were restricted to the current sequences, while the tetrapeptides were only shared by D-hordein and the current sequences. However, these sequences were not expressed as normal HMW glutenin proteins because an in-frame stop codon located in the C-termini interrupted the intact open reading frames. A phylogenetic analysis supported different origins of the P. juncea HMW glutenin sequences than that revealed by a previous study. The current sequences showed a close relationship with D-hordein but appeared to be more primitive

Wnt signalling and cancer stem cells

[Abstract] Intracellular signalling mediated by secreted Wnt proteins is essential for the establishment of cell fates and proper tissue patterning during embryo development and for the regulation of tissue homeostasis and stem cell function in adult tissues. Aberrant activation of Wnt signalling pathways has been directly linked to the genesis of different tumours. Here, the components and molecular mechanisms implicated in the transduction of Wnt signal, along with important results supporting a central role for this signalling pathway in stem cell function regulation and carcinogenesis will be briefly reviewed.Ministerio de Ciencia e Innovación; SAF2008-0060

Characterization of a novel 4.0-kb y-type HMW-GS from Eremopyrum distans

A novel 4.0-kb Fy was sequenced and bacterially expressed. This gene, the largest y-type HMW-GS currently reported, is 4,032-bp long and encodes a mature protein with 1,321 amino acid (AA) residues. The 4.0-kb Fy shows novel modifications in all domains. In the N-terminal, it contains only 67 AA residues, as three short peptides are absent. In the repetitive domain, the undecapeptide RYYPSVTSPQQ is completely lost and the dodecapeptide GSYYPGQTSPQQ is partially absent. A novel motif unit, PGQQ, is present in addition to the two standard motif units PGQGQQ and GYYPTSPQQ. Besides, an extra cysteine residue also occurs in the middle of this domain. The large molecular mass of the 4.0-kb Fy is mainly due to the presence of an extra-long repetitive domain with 1,279 AA residues. The novel 4.0-kb Fy gene is of interest in HMW-GS gene evolution as well as to wheat quality improvement with regard to its longest repetitive domain length and extra cysteines residues

A Study of J/psi-->gamma gamma V(rho,phi) Decays with the BESII Detector

Using a sample of $58\times 10^6$ $J/\psi$ events collected with the BESII detector, radiative decays $J/\psi\to\gamma\gamma V$, where $V=\rho$ or $\phi$, are studied. A resonance around 1420 MeV/c$^2$ (X(1424)) is observed in the $\gamma\rho$ mass spectrum. Its mass and width are measured to be $1424\pm 10(stat)\pm 11(sys)$ MeV/c$^2$ and $101.0\pm 8.8 \pm 8.8$ MeV/c$^2$, respectively, and its branching ratio $B(J/\psi\to \gamma X(1424)\to \gamma \gamma \rho)$ is determined to be $(1.07\pm0.17 \pm 0.11)\times 10^{-4}$. A search for $X(1424)\to \gamma\phi$ yields a 95% C.L. upper limit $B(J/\psi\to \gamma X(1424)\to \gamma\gamma \phi) < 0.82 \times 10^{-4}$.Comment: 10 pages, 5 figures, submitted to PL