A Harm Reduction Framework for Integrated Treatment of Co-Occurring Opioid Use Disorder and Trauma-Related Disorders.

The opioid epidemic has exposed a gulf in mental health research, treatment, and policy: Most patients with comorbid trauma-related disorder (TRD) and opioid use disorder (OUD) (TRD + OUD) remain undiagnosed or unsuccessfully treated for the combination of TRD symptoms and opioid use. TRD treatments tend to be psychotherapies that are not accessible or practical for many individuals with TRD + OUD, due to TRD treatment models not systematically incorporating principles of harm reduction (HR). HR practices prioritize flexibility and unequivocally improve outcomes and save lives in the treatment of OUD.

Practical Considerations for Treating Comorbid Posttraumatic Stress Disorder in the Addictions Clinic: Approaches to Clinical Care, Leadership, and Alleviating Shame.

A practical, common-sense framework for recognizing and addressing comorbid posttraumatic stress disorder (PTSD) in the substance use disorder (SUD) clinic is outlined. The article focuses on strategies that can help establish trauma-informed care or augment an existing approach. Interventions are organized around the task of ameliorating shame (or shame sensitivity), which represents a transdiagnostic mediator of psychopathology and, potentially, capacity for change.

Disulfide bond generation in mammalian blood serum: detection and purification of quiescin-sulfhydryl oxidase.

A sensitive new plate-reader assay has been developed showing that adult mammalian blood serum contains circulating soluble sulfhydryl oxidase activity that can introduce disulfide bonds into reduced proteins with the reduction of oxygen to hydrogen peroxide. The activity was purified 5000-fold to >90% homogeneity from bovine serum and found by mass spectrometry to be consistent with the short isoform of quiescin-sulfhydryl oxidase 1 (QSOX1). This FAD-dependent enzyme is present at comparable activity levels in fetal and adult commercial bovine sera.

Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidase.

The quiescin sulfhydryl oxidase (QSOX) family of enzymes generates disulfide bonds in peptides and proteins with the reduction of oxygen to hydrogen peroxide. Determination of the potentials of the redox centers in Trypanosoma brucei QSOX provides a context for understanding catalysis by this facile oxidant of protein thiols. The CXXC motif of the thioredoxin domain is comparatively oxidizing (E'0 of -144 mV), consistent with an ability to transfer disulfide bonds to a broad range of thiol substrates.

Short-term stability of sleep and heart rate variability in good sleepers and patients with insomnia: for some measures, one night is enough.

Study Objectives: Quantify the short-term stability of multiple indices of sleep and nocturnal physiology in good sleeper controls and primary insomnia patients.

Design: Intra-class correlation coefficients (ICC) were used to quantify the short-term stability of study outcomes.

Setting: Sleep laboratory.

Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family.

This work explores the substrate specificity of the quiescin sulfhydryl oxidase (QSOX) family of disulfide-generating flavoenzymes to provide enzymological context for investigation of the physiological roles of these facile catalysts of oxidative protein folding. QSOX enzymes are generally unable to form disulfide bonds within well-structured proteins. Use of a temperature-sensitive mutant of ubiquitin-conjugating enzyme 4 (Ubc4') as a model substrate shows that QSOX activity correlates with the unfolding of Ubc4' monitored by circular dichroism.