Publications by authors named "V N Schulz"

Integrating time-of-flight (ToF) measurements in radiography and computed tomography (CT) enables an approach for scatter rejection in imaging systems that eliminates the need for anti-scatter grids, potentially increasing system sensitivity and image quality. However, present hardware dedicated to the time-correlated measurement of X-rays is limited to a small scale and low density. A switch to highly integrated electronics and detectors is needed to progress towards a medium-scale system capable of acquiring images, while offering a timing resolution below 300 ps FWHM to achieve scatter rejection comparable to current grids.

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Mammalian red blood cells are generated via a terminal erythroid differentiation pathway culminating in cell polarization and enucleation. Actin filament polymerization is critical for enucleation, but the molecular regulatory mechanisms remain poorly understood. We utilized publicly available RNA-seq and proteomics datasets to mine for actin-binding proteins and actin-nucleation factors differentially expressed during human erythroid differentiation and discovered that a focal adhesion protein-Tensin-1-dramatically increases in expression late in differentiation.

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Time resolution is crucial in positron emission tomography (PET) to enhance the signal-to-noise ratio and image quality. Moreover, high sensitivity requires long scintillators, which can cause distortions in the reconstructed images due to parallax effects. This study evaluates the performance of a time-of-flight (TOF)-PET module that makes use of a single-side readout of a4×43.

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To achieve precise control over the properties and performance of nanoparticles (NPs) in a microfluidic setting, a profound understanding of the influential parameters governing the NP size is crucial. This study specifically delves into poly(lactic--glycolic acid) (PLGA)-based NPs synthesized through microfluidics that have been extensively explored as drug delivery systems (DDS). A comprehensive database, containing more than 11 hundred data points, is curated through an extensive literature review, identifying potential effective features.

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Iron-sulfur (FeS) protein biogenesis in eukaryotes begins with the de novo assembly of [2Fe-2S] clusters by the mitochondrial core iron-sulfur cluster assembly (ISC) complex. This complex comprises the scaffold protein ISCU2, the cysteine desulfurase subcomplex NFS1-ISD11-ACP1, the allosteric activator frataxin (FXN) and the electron donor ferredoxin-2 (FDX2). The structural interaction of FDX2 with the complex remains unclear.

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