A thermally polarized, dissolved-phase Xe phantom for quality-control and multisite comparisons of gas-exchange imaging.

Harmonizing and validating Xe gas exchange imaging across multiple sites is hampered by a lack of a quantitative standard that 1) displays the unique spectral properties of Xe observed from human subjects in vivo and 2) has short enough T times to enable practical imaging. This work describes and demonstrates the development of two dissolved-phase, thermally polarized phantoms that mimic the in-vivo, red blood cell and membrane resonances of Xe dissolved in human lungs. Following optimization, combinations of two common organic solvents, acetone and dimethyl sulfoxide, resulted in two in-vivo-like dissolved-phase Xe phantoms yielding chemical shifts of 212.

Experiences of Māori and Pacific women recruited into a pregnancy clinical trial in Aotearoa, New Zealand: a Kaupapa Māori qualitative study.

Objectives: To explore the perspectives of Māori and Pacific women who participated in the Fish Oil study to ascertain what barriers and facilitators may exist for successfully recruiting Māori and Pacific women into clinical trials.

Design: A Kaupapa Māori qualitative study.

Setting: Auckland, New Zealand.

A multiplex method for rapidly identifying viral protease inhibitors.

With current treatments addressing only a fraction of pathogens and new viral threats constantly evolving, there is a critical need to expand our existing therapeutic arsenal. To speed the rate of discovery and better prepare against future threats, we establish a high-throughput platform capable of screening compounds against 40 diverse viral proteases simultaneously. This multiplex approach is enabled by using cellular biosensors of viral protease activity combined with DNA-barcoding technology, as well as several design innovations that increase assay sensitivity and correct for plate-to-plate variation.

Remodelling of Rea1 linker domain drives the removal of assembly factors from pre-ribosomal particles.

The ribosome maturation factor Rea1 (or Midasin) catalyses the removal of assembly factors from large ribosomal subunit precursors and promotes their export from the nucleus to the cytosol. Rea1 consists of nearly 5000 amino-acid residues and belongs to the AAA+ protein family. It consists of a ring of six AAA+ domains from which the ≈1700 amino-acid residue linker emerges that is subdivided into stem, middle and top domains.