Neurological and Neuroradiological Manifestations in Neonates Born to Mothers With Coronavirus Disease 2019.

Background: To investigate the complications that occurred in neonates born to mothers with coronavirus disease 2019 (COVID-19), focusing on neurological and neuroradiological findings, and to compare differences associated with the presence of maternal symptoms.

Methods: Ninety neonates from 88 mothers diagnosed with coronavirus disease 2019 (COVID-19) during pregnancy were retrospectively reviewed. Neonates were divided into two groups: symptomatic (Sym-M-N, n = 34) and asymptomatic mothers (Asym-M-N, n = 56).

Optimizing hand-function patient outcome measures for inclusion body myositis.

Inclusion body myositis is the most commonly acquired myopathy after the age of 45. The slowly progressive and heterogeneous disorder is a challenge for measuring clinical trial efficacy. One current method for measuring progression utilizes the Inclusion Body Myositis-Functional Rating Scale.

A cross-sectional study of hand function in inclusion body myositis: Implications for functional rating scale.

Inclusion body myositis (IBM) is a slowly progressive and heterogeneous disorder that is a challenge for measuring clinical trial efficacy. The current methods of measuring progression of the disease utilizes the Inclusion Body Myositis Functional Rating Scale, grip strength by dynamometer, and finger flexor strength. One of the hallmarks of the disease is selective deep finger flexor weakness.

Impacts of dystrophin and utrophin domains on actin structural dynamics: implications for therapeutic design.

We have used time-resolved phosphorescence anisotropy (TPA) of actin to evaluate domains of dystrophin and utrophin, with implications for gene therapy in muscular dystrophy. Dystrophin and its homolog utrophin bind to cytoskeletal actin to form mechanical linkages that prevent muscular damage. Because these proteins are too large for most gene therapy vectors, much effort is currently devoted to smaller constructs.

The carboxy-terminal third of dystrophin enhances actin binding activity.

Dystrophin is an actin binding protein that is thought to stabilize the cardiac and skeletal muscle cell membranes during contraction. Here, we investigated the contributions of each dystrophin domain to actin binding function. Cosedimentation assays and pyrene-actin fluorescence experiments confirmed that a fragment spanning two-thirds of the dystrophin molecule [from N-terminal actin binding domain (ABD) 1 through ABD2] bound actin filaments with high affinity and protected filaments from forced depolymerization, but was less effective in both assays than full-length dystrophin.

Effects of physiological environments on the hydration behavior of mineral trioxide aggregate.

Utilizing scanning electron microscope, X-ray diffraction (XRD) and microhardness tests, we evaluated how various physiological environments affect the hydration behavior and physical properties of mineral trioxide aggregate (MTA). We found that the microstructure of hydrated MTA consists of cubic and needle-like crystals. The former comprised the principal structure of MTA, whereas the later were less prominent and formed in the inter-grain spaces between the cubic crystals.