Rational Design of an Orthogonal Pair of Bimolecular RNase P Ribozymes through Heterologous Assembly of Their Modular Domains.

The modular structural domains of multidomain RNA enzymes can often be dissected into separate domain RNAs and their noncovalent assembly can often reconstitute active enzymes. These properties are important to understand their basic characteristics and are useful for their application to RNA-based nanostructures. Bimolecular forms of bacterial RNase P ribozymes consisting of S-domain and C-domain RNAs are attractive as platforms for catalytic RNA nanostructures, but their S-domain/C-domain assembly was not optimized for this purpose.

Modular Architecture of Bacterial RNase P Ribozymes as a Structural Platform for RNA Nanostructure Design.

Ribonuclease P (RNase P) is a class of enzymes involved in the processing of precursor tRNAs to remove their 5'-leader sequences. Ribonuclease P enzymes are classified into two completely distinct classes, an RNA-based enzyme and a protein-only enzyme. The RNA-based enzyme functions as a ribozyme in which the catalytic machinery is supported by its RNA component consisting of a single RNA molecule.

Measuring body composition using the bioelectrical impedance method can predict the outcomes of gemcitabine-based chemotherapy in patients with pancreatobiliary tract cancer.

In order to examine the effect on body composition of anticancer drug treatments, the body composition rate in patients being treated with gemcitabine (GEM)-based chemotherapy was measured over time on an outpatient basis with a simple body composition monitor using the bioelectrical impedance (BI) method. The results revealed a significant reduction in the body fat rate (P=0.01) over the course of treatment in patients with pancreatobiliary tract cancer who became unable to continue GEM-based chemotherapy due to progressive disease or a decreased performance status.