Purpose of Review We review the current understanding of the burden of dermatological disease through the lens of the Global Burden of Disease project, evaluate the impact of skin disease on quality of life in a global context, explore socioeconomic implications, and finally summarize interventions towards improving quality of dermatologic care in resource-poor settings. Recent Findings The Global Burden of Disease project has shown that skin diseases continue to be the 4th leading cause of nonfatal disease burden world-wide. However, research efforts and funding do not match with the relative disability of skin diseases. International and national efforts, such as the WHO List of Essential Medicines, are critical towards reducing the socioeconomic burden of skin diseases and increasing access to care. Recent innovations such as teledermatology, point-of-care diagnostic tools, and task-shifting help to provide dermatological care to underserved regions in a cost-effective manner. Summary Skin diseases cause significant non-fatal disability worldwide, especially in resource-poor regions. Greater impetus to study the burden of skin disease in low resource settings and policy efforts towards delivering high quality care are essential in improving the burden of skin diseases.

Cell signaling is a complex and highly regulated process. Post-translational modifications of proteins serve to sense and transduce cellular signals in a precisely coordinated manner. It is increasingly recognized that protein S-nitrosylation, the addition of a nitric oxide group to cysteine thiols, serves an important role in a wide range of signaling pathways. In spite of the large number of SNO-proteins now identified (~1000), the observed specificity of S-nitrosylation in terms of target proteins and specific cysteines within modified proteins is incompletely understood. Here we review the progress made in S-nitrosylation detection methods that have facilitated the study of the SNO-proteome under physiological and pathophysiological conditions, and some factors important in determining the SNO-proteome. Classification schemes for emergent denitrosylases and prospective 'protein S-nitrosylases' are provided.

Endogenous S-nitrosylation of proteins, a principal mechanism of cellular signaling in eukaryotes, has not been observed in microbes. We report that protein S-nitrosylation is an obligate concomitant of anaerobic respiration on nitrate in Escherichia coli. Endogenous S-nitrosylation during anaerobic respiration is controlled by the transcription factor OxyR, previously thought to operate only under aerobic conditions. Deletion of OxyR resulted in large increases in protein S-nitrosylation, and S-nitrosylation of OxyR induced transcription from a regulon that is distinct from the regulon induced by OxyR oxidation. Furthermore, products unique to the anaerobic regulon protected against S-nitrosothiols, and anaerobic growth of E. coli lacking OxyR was impaired on nitrate. Thus, OxyR serves as a master regulator of S-nitrosylation, and alternative posttranslational modifications of OxyR control distinct transcriptional responses.