In-situ gamma-ray measurement to estimate depth distribution of Cs in farmland in Fukushima Prefecture.

Radioactive cesium released into the atmosphere caused by the Fukushima Dai-ichi Nuclear Power Plant accident in March 2011 has contaminated the surrounding area. We confirmed the applicability of in-situ methods to evaluate the depth distribution of Cs by employing the ratio of Compton-scattering and photo-peak components (r) obtained from measured gamma-ray spectra. In the present study, we applied the in-situ method to farmlands in Fukushima Prefecture whose sites were disturbed by decontamination and plowing operations.

Glucocorticoid sparing effect on Adalimumab for refractory Pyoderma gangrenosum in patients with Rheumatoid Arthritis: A Case series.

Pyoderma gangrenosum (PG) is a rare chronic skin disease characterized by painful skin ulcers. There are no treatment guidelines for PG; however, systemic treatment is often administered. Recently, adalimumab (ADA), a fully human monoclonal antibody against tumor necrosis factor, was approved for the treatment of refractory PG in Japan.

Integration of shoot-derived polypeptide signals by root TGA transcription factors is essential for survival under fluctuating nitrogen environments.

Unlike plants in the field, which experience significant temporal fluctuations in environmental conditions, plants in the laboratory are typically grown in controlled, stable environments. Therefore, signaling pathways evolved for survival in fluctuating environments often remain functionally latent in laboratory settings. Here, we show that TGA1 and TGA4 act as hub transcription factors through which the expression of genes involved in high-affinity nitrate uptake are regulated in response to shoot-derived phloem mobile polypeptides, CEP DOWNSTREAM 1 (CEPD1), CEPD2 and CEPD-like 2 (CEPDL2) as nitrogen (N) deficiency signals, and Glutaredoxin S1 (GrxS1) to GrxS8 as N sufficiency signals.

Elucidating the complex membrane binding of a protein with multiple anchoring domains using extHMMM.

Membrane binding is a crucial mechanism for many proteins, but understanding the specific interactions between proteins and membranes remains a challenging endeavor. Coagulation factor Va (FVa) is a large protein whose membrane interactions are complicated due to the presence of multiple anchoring domains that individually can bind to lipid membranes. Using molecular dynamics simulations, we investigate the membrane binding of FVa and identify the key mechanisms that govern its interaction with membranes.