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Schulz, J. B.

Publications and source records attributed to Schulz, J. B..

3 recordsLinked to original sources

Characterization and Calibration of the iQID Digital Autoradiography System for Direct Quantitative Imaging of Beta-Emitters in Tissue Samples

Autoradiography provides microscale mapping of radionuclide distributions, a promising approach to complement nuclear medicine imaging for small-scale radiopharmaceutical therapy (RPT) research. However, quantitative protocols for {beta}-emitters remain under-established compared to those for -emitters. In this work, the ionizing-radiation quantum imaging detector (iQID) digital autoradiography system was characterized and calibrated specifically for the theranostic {beta}-emitter 177Lu. Spatial resolution, detection efficiency, background and minimum detectable activity, and depth dependence were characterized and compared to Geant4 Monte Carlo simulations. A methodology for converting count rates to activity was established, yielding a high linear response (range from 0 to 300 Bq). To validate the system for realistic measurement scenarios, cross-modality benchmarking was performed using a custom stacked multi-layer virtual water phantom to compare iQID performance with preclinical {micro}SPECT/CT. The iQID system demonstrated an effective spatial resolution of [~]43 {micro}m for 177Lu and achieved total activity estimates of (0.194 {+/-} 0.022) MBq, agreeing within 2% with the dispensed reference (0.197 {+/-} 0.015) MBq. Crucially, iQID exhibited superior quantitative accuracy for small-scale features (0.8 mm to 2.5 mm diameters), resolving activity concentrations in regions where {micro}SPECT/CT performance was severely limited by partial volume effects. This study establishes a validated framework for quantitative 177Lu digital autoradiography, laying the groundwork for accurate activity estimation in ex vivo tissue samples.

cancer biology↗

Impact of Phosphorylation on alpha-Synuclein Structural Determinants

Serine 129 can be phosphorylated in pathological inclusions formed by the intrinsically disordered protein human -synuclein (AS), a key player in Parkinsons disease and other synucleinopathies. Here, molecular simulations provide insight into the structural ensemble of phosphorylated AS. The simulations suggest that phosphorylation does not impact the structural content of the physiological AS conformational ensemble in aqueous solution, as the phosphate group is mostly solvated. The hydrophobic region of AS contains {beta}-hairpin structures, which may increase the propensity of the protein to undergo amyloid formation, as seen in the non-physiological (non-acetylated) form of the protein in a recent molecular simulation study. Our findings are consistent with existing experimental data, with the caveat of the observed limitations of the force field for the phosphorylated moiety. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=111 SRC="FIGDIR/small/531864v4_ufig1.gif" ALT="Figure 1"> View larger version (24K): org.highwire.dtl.DTLVardef@108c32dorg.highwire.dtl.DTLVardef@45e5d7org.highwire.dtl.DTLVardef@f49cf6org.highwire.dtl.DTLVardef@16ceb61_HPS_FORMAT_FIGEXP M_FIG C_FIG

biophysics↗

Small-molecule modulators of TRMT2A decrease PolyQ aggregation and PolyQ-induced cell death

Polyglutamine (polyQ) diseases are characterized by an expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats encoding for an uninterrupted prolonged polyQ tract. We previously identified TRMT2A as a strong modifier of polyQ-induced toxicity in an unbiased large-scale screen in Drosophila melanogaster. This work aimed at identifying and validating pharmacological TRMT2A inhibitors as treatment opportunities for polyQ diseases in humans. Computer-aided drug discovery was implemented to identify human TRMT2A inhibitors. Additionally, the crystal structure of one protein domain, the RNA recognition motif (RRM), was determined, and Biacore experiments with the RRM were performed. The identified molecules were validated for their potency to reduce polyQ aggregation and polyQ-induced cell death in human HEK293T cells and patient derived fibroblasts. Our work provides a first step towards pharmacological inhibition of this enzyme and indicates TRMT2A as a viable drug target for polyQ diseases.

molecular biology↗