Qualitative interviews to understand methods and systems used to collect ethnicity information in health administrative data sources in England.

 This article is one of a series aiming to inform analytical methods to improve comparability of estimates of ethnic health disparities based on different sources. This article explores the quality of ethnicity data and identifies potential sources of bias when ethnicity information is collected in three key NHS data sources. Future research can build on these findings to explore analytical methods to mitigate biases.

Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens.

The worldwide incidence of neisserial infections, particularly gonococcal infections, is increasingly associated with antibiotic-resistant strains. In particular, extensively drug-resistant strains that are resistant to third-generation cephalosporins are a major public health concern. There is a pressing clinical need to identify new targets for the development of antibiotics effective against -specific processes.

Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.

The membrane protein DsbD is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence. DsbD is a multi-domain protein consisting of a transmembrane domain (t-DsbD) flanked by two periplasmic domains (n-DsbD and c-DsbD). Previous studies have shown that DsbD is required for the survival of the obligate human pathogen Neisseria meningitidis.

H, N, C and C assignments of the two periplasmic domains of Neisseria meningitidis DsbD.

DsbD is a disulfide bond reductase present in the inner membrane of many Gamma-Proteobacteria. In the human pathogen Neisseria meningitidis, DsbD is required for viability and represents a potential target for the development of antibiotics. Here we report the chemical shift assignments (H, N, C and C) for the reduced and oxidized forms of the two periplasmic domains of N.

Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents.

Recent years have witnessed a dramatic increase in bacterial antimicrobial resistance and a decline in the development of novel antibiotics. New therapeutic strategies are urgently needed to combat the growing threat posed by multidrug resistant bacterial infections. The Dsb disulfide bond forming pathways are potential targets for the development of antimicrobial agents because they play a central role in bacterial pathogenesis.

Repair renal tubular cells: a potential false-positive diagnosis in urine cytology.

To study the cytopathology of repair renal tubular cells (RRTCs), the Papanicolaou-stained urine sediments of 371 patients with mild and moderate renal tubular injuries were reviewed. In 46 cases, the urine sediments showed, in addition to a mild or moderate increase in number of RTCs, a few isolated and clustered RRTCs that displayed well- or ill-defined, variably abundant, granular or vacuolated cytoplasm; slightly pleomorphic nuclei; and conspicuous or prominent nucleoli. A spectrum of nuclear changes ranging from mild to moderate atypias and/or severe atypia were present in many cases.