Photoneutron reaction cross section measurements on 94Mo and 90Zr relevant to the p-process nucleosynthesis

The photodisintegration cross sections for the 94Mo({\gamma},n) and 90Zr({\gamma},n) reactions have been experimentally investigated with quasi-monochromatic photon beams at the High Intensity {\gamma}-ray Source (HI{\gamma}S) facility of the Triangle Universities Nuclear Laboratory (TUNL). The energy dependence of the photoneutron reaction cross sections was measured with high precision from the respective neutron emission thresholds up to 13.5 MeV. These measurements contribute to a broader investigation of nuclear reactions relevant to the understanding of the p-process nucleosynthesis. The results are compared with the predictions of Hauser-Feshbach statistical model calculations using two different models for the dipole {\gamma}-ray strength function. The resulting 94Mo({\gamma},n) and 90Zr({\gamma},n) photoneutron stellar reaction rates as a function of temperature in the typical range of interest for the p-process nucleosynthesis show how sensitive the photoneutron stellar reaction rate can be to the experimental data in the vicinity of the neutron threshold

Genes encoding α-amylase inhibitors are located in the short arms of chromosomes 3B, 3D and 6D of wheat (Triticum aestivum L.)

Three -amylase inhibitors, designated Inh. I, II and III have been purified from the 70% ethanol extract of hexaploid wheat (Triticum aestivum L.) and characterized by amino acid analysis, N-terminal amino acid sequencing and enzyme inhibition tests. Inhibitors I and III have identical N-terminal sequences and inhibitory properties to those of the previously described 0.19/0.53 group of dimeric inhibitors. Inhibitor II has an N-terminal sequence which is identical to that of the previously described 0.28 monomeric inhibitor, but differs from it in that in addition to being active against -amylase from Tenebrio molitor, it is also active against mammalian salivary and pancreatic -amylases. Compensating nulli-tetrasomic and ditelosomic lines of wheat cv. Chinese Spring have been analysed by two-dimensional electrophoresis, under conditions in which there is no overlap of the inhibitors with other proteins, and the chromosomal locations of the genes encoding these inhibitors have been established: genes for Inh. I and Inh. III are in the short arms of chromosomes 3B and 3D, respectively, and that for Inh. II in the short arm of chromosome 6D

Psalms for Organ, Volume 11: Ulster

Pages 23-27 in Psalms for Organ, Volume 11

Compton Scattering from \u3csup\u3e4\u3c/sup\u3eHe at 61 MeV

The Compton scattering cross section from 4He has been measured with high statistical accuracy over a scattering angle range of 40∘−159∘ using a quasimonoenergetic 61-MeV photon beam at the High Intensity Gamma-Ray Source. The data are interpreted using a phenomenological model sensitive to the dipole isoscalar electromagnetic polarizabilities (αs and βs) of the nucleon. These data can be fit with the model using values of αs and βs that are consistent with the currently accepted values. These data will serve as benchmarks of future calculations from effective field theories and lattice quantum chromodynamics

Gut microbiota trajectory in early life may predict development of celiac disease.

BACKGROUND: To investigate whether alterations in the developing intestinal microbiota and immune markers precede celiac disease (CD) onset in infants at familial risk of developing the disease. METHODS: A nested case-control study was carried out as part of a larger prospective cohort study, which included healthy full-term newborns (> 200) with at least one first relative with biopsy-verified CD. The present study includes cases of CD (n = 10) and the best-matched controls (n = 10) who did not develop the disease after 5-year follow-up. Fecal microbiota, assessed by high-throughput 16S rRNA gene amplicon sequencing, and immune parameters were profiled at 4 and 6 months of age and related to CD onset. RESULTS: The microbiota of infants who remained healthy showed an increase in bacterial diversity over time, characterized by increases in Firmicutes families, but not those who developed CD. Infants who subsequently developed CD showed a significant reduction in sIgA levels over time, while those who remained healthy showed increases in TNF-α correlated to Bifidobacterium spp. An increased relative abundance of Bifidobacterium longum was associated with control children while increased proportions of Bifidobacterium breve and Enterococcus spp. were associated with CD development. CONCLUSION: The findings suggest that alterations in the early trajectory of gut microbiota in infants at CD risk could influence the immune maturation process and predispose to CD, although larger population studies are warranted to confirm this hypothesis

Delayed diagnosis of coeliac disease increases cancer risk

This is an Open Access article distributed under the terms of the Creative Commons Attribution Licens

Involvement of cell surface TG2 in the aggregation of K562 cells triggered by gluten

Gluten-induced aggregation of K562 cells represents an in vitro model reproducing the early steps occurring in the small bowel of celiac patients exposed to gliadin. Despite the clear involvement of TG2 in the activation of the antigen-presenting cells, it is not yet clear in which compartment it occurs. Herein we study the calcium-dependent aggregation of these cells, using either cell-permeable or cell-impermeable TG2 inhibitors. Gluten induces efficient aggregation when calcium is absent in the extracellular environment, while TG2 inhibitors do not restore the full aggregating potential of gluten in the presence of calcium. These findings suggest that TG2 activity is not essential in the cellular aggregation mechanism. We demonstrate that gluten contacts the cells and provokes their aggregation through a mechanism involving the A-gliadin peptide 31-43. This peptide also activates the cell surface associated extracellular TG2 in the absence of calcium. Using a bioinformatics approach, we identify the possible docking sites of this peptide on the open and closed TG2 structures. Peptide docks with the closed TG2 structure near to the GTP/GDP site, by establishing molecular interactions with the same amino acids involved in stabilization of GTP binding. We suggest that it may occur through the displacement of GTP, switching the TG2 structure from the closed to the active open conformation. Furthermore, docking analysis shows peptide binding with the β-sandwich domain of the closed TG2 structure, suggesting that this region could be responsible for the different aggregating effects of gluten shown in the presence or absence of calcium. We deduce from these data a possible mechanism of action by which gluten makes contact with the cell surface, which could have possible implications in the celiac disease onset