Publications by authors named "M J SEGHERS"

Background: Due to the COVID-19 pandemic, some pediatric radiologists have shifted to working from home; the long-term ramifications for pediatric radiologists and departments have not yet been defined.

Objective: To characterize experiences of working from home associated with the COVID-19 pandemic and guide expectations after the pandemic is controlled, via separate surveys of Society for Pediatric Radiology (SPR) and Society of Chiefs of Radiology at Children's Hospitals (SCORCH) members.

Materials And Methods: Two separate surveys were conducted.

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Background: Scrotal pain is a common complaint in the clinical practice, with many underlying causes. Infectious causes, like epididymitis, are frequently encountered in the work-up of scrotal pain. The presentation of epididymitis is mostly mild, yet major complications can occur.

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Introduction: Strategies for pain alleviation have relied heavily on opioids in the recent decades. One consequence is a crisis of opioid misuse, overdose, and overdose related death. This study sought patient and clinician incentives and barriers to the use of opioids in musculoskeletal illness.

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Introduction: Renal papillary necrosis is not commonly seen in daily practice, but can have severe consequences when it is not diagnosed in time. It is known to be associated with sickle cell hemoglobinopathies; however a wide range of etiologies are possible, and it is therefore not the first diagnosis clinicians consider in patients with sickle cell disease who present with hematuria.

Methods: A literature search was performed to summarize the current knowledge about renal papillary necrosis associated with sickle cell disease.

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γ-secretase is responsible for the proteolysis of amyloid precursor protein (APP) into short, aggregation-prone amyloid-beta (Aβ) peptides, which are centrally implicated in the pathogenesis of Alzheimer's disease (AD). Despite considerable interest in developing γ-secretase targeting therapeutics for the treatment of AD, the precise mechanism by which γ-secretase produces Aβ has remained elusive. Herein, we demonstrate that γ-secretase catalysis is driven by the stabilization of an enzyme-substrate scission complex via three distinct amino-acid-binding pockets in the enzyme's active site, providing the mechanism by which γ-secretase preferentially cleaves APP in three amino acid increments.

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