Morpholine-Substituted Rhodamine Analogue with Multi-Configurational Switches for Optical Sensing of pH Gradient under Extreme Acidic Environments.

Superior pH-responsive molecules are required for the development of functional materials applicable to advanced molecular technologies. Despite having been widely developed, many rhodamine-based pH-responsive molecules exhibit a single configurational switch for "turn-on". Herein, we report a new type of rhodamine-based pH-responsive molecule with multi-configurational switches displaying stable two-step structural and color conversion in response to pH.

Promotion of cellular senescence by THG-1/TSC22D4 knockout through activation of JUNB.

Induction of cellular senescence in cancerous cells is an important strategy which is used in the treatment of cancer. However, cancer cells are capable of exhibiting resistance to cellular senescence through inactivation of tumor suppressors. Because of this, establishment of a route to cellular senescence induction in cancer cells is a crucial direction for developing future cancer therapies.

Association between duplicated maltase genes and the transcriptional regulation for the carbohydrate changes in Drosophila melanogaster.

Gene duplication could promote phenotypic and genetic adaptation to various environments. To understand the effects of gene duplication on transcriptional regulation associated with environmental changes, we focused on the starch hydrolysis pathway, in which amylase enzymes together with maltase enzymes hydrolyze starch into glucose. Drosophila genomes involve ten duplicated Maltase genes.

Cellular localization of prolactin-releasing peptide receptors in the human pituitary.

The recently identified prolactin (PRL)-releasing peptide (PrRP) is the first hypothalamic peptide hormone found to operate as a ligand of an orphan receptor that specifically stimulates PRL production from the pituitary gland. However, its other biological functions remain unknown. Using immunohistochemistry, we examined the distribution of the PrRP receptor in various human tissues, as well as the precise localization of the PrRP receptor in the human normal pituitary.