Correction: BatCount: A software program to count moving animals.

[This corrects the article DOI: 10.1371/journal.pone.0278012.].

BatCount: A software program to count moving animals.

One of the biggest challenges with species conservation is collecting accurate and efficient information on population sizes, especially from species that are difficult to count. Bats worldwide are declining due to disease, habitat destruction, and climate change, and many species lack reliable population information to guide management decisions. Current approaches for estimating population sizes of bats in densely occupied colonies are time-intensive, may negatively impact the population due to disturbance, and/or have low accuracy. Research-based video tracking options are rarely used by conservation or management agencies for animal counting due to the perceived training and elevated operating costs. In this paper, we present BatCount, a free software program created in direct consultation with end-users designed to automatically count bats emerging from cave roosts (historical populations 20,000-250,000) with a streamlined and user-friendly interface. We report on the software package and provide performance metrics for different recording habitat conditions. Our analysis demonstrates that BatCount is an efficient and reliable option for counting bats in flight, with performance hundreds of times faster than manual counting, and has important implications for range- and species-wide population monitoring. Furthermore, this software can be extended to count any organisms moving across a camera including birds, mammals, fish or insects.

Three-Dimensionally Printed On-Skin Radiation Shields Using High-Density Filament.

PURPOSE: Custom-fabricated lead shields are often used for superficial radiation treatments to reduce radiation doses to adjacent healthy tissue. However, the process for fabricating these lead shields is time consuming, labor intensive, and uncomfortable for patients. Alternatively, patient-specific shields can be 3-dimensionally (3D) printed from a high-density bronze-based filament to address these concerns. This study was performed to assess the shielding characteristics of 3D-printed bronze (3DPB) shields, demonstrate their clinical viability, and report the first ever published case of a patient treated with a 3DPB shield. METHODS AND MATERIALS: The transmission of 6 and 9 MeV electron beams through varying thicknesses of 3DPB was first measured. Percent depth doses and beam profiles were measured with flat 3DPB shields and equivalent lead shields to determine surface dose enhancement, output factors, and field widths. Two 3DPB shields were designed and fabricated for an anthropomorphic phantom, and phantom measurements were performed using optically stimulated luminescence dosimeters and film. Finally, 3DPB shields were used during the treatment of 7 patients' skin lesions. RESULTS: Ten and 15 mm of 3DPB were sufficient to shield 6 and 9 MeV electrons, respectively, by 95%. The 3DPB and lead shields had nearly identical beam widths (within 1%). Output factors were on average within 0.8% for bronze shields and 1.2% for lead shields relative to an unshielded field. The skin enhancement for bronze was higher than for lead by an average of 6.3%. Phantom measurements using 3DPB shields generally showed less than 3% transmission of the primary beam under the 3DPB shield. The patients' shields fit as designed and were all deemed clinically acceptable by their physicians. CONCLUSIONS: The 3DPB shields fit better than lead shields, are easier to design and manufacture, and have similar dosimetric properties. 3DPB shields are a viable clinical option for patient-specific superficial shielding.

A novel, in-solution separation of endogenous cardiac sarcomeric proteins and identification of distinct charged variants of regulatory light chain.

The molecular conformation of the cardiac myosin motor is modulated by intermolecular interactions among the heavy chain, the light chains, myosin binding protein-C, and titin and is governed by post-translational modifications (PTMs). In-gel digestion followed by LC/MS/MS has classically been applied to identify cardiac sarcomeric PTMs; however, this approach is limited by protein size, pI, and difficulties in peptide extraction. We report a solution-based work flow for global separation of endogenous cardiac sarcomeric proteins with a focus on the regulatory light chain (RLC) in which specific sites of phosphorylation have been unclear. Subcellular fractionation followed by OFFGEL electrophoresis resulted in isolation of endogenous charge variants of sarcomeric proteins, including regulatory and essential light chains, myosin heavy chain, and myosin-binding protein-C of the thick filament. Further purification of RLC using reverse-phase HPLC separation and UV detection enriched for RLC PTMs at the intact protein level and provided a stoichiometric and quantitative assessment of endogenous RLC charge variants. Digestion and subsequent LC/MS/MS unequivocally identified that the endogenous charge variants of cardiac RLC focused in unique OFFGEL electrophoresis fractions were unphosphorylated (78.8%), singly phosphorylated (18.1%), and doubly phosphorylated (3.1%) RLC. The novel aspects of this study are that 1) milligram amounts of endogenous cardiac sarcomeric subproteome were focused with resolution comparable with two-dimensional electrophoresis, 2) separation and quantification of post-translationally modified variants were achieved at the intact protein level, 3) separation of intact high molecular weight thick filament proteins was achieved in solution, and 4) endogenous charge variants of RLC were separated; a novel doubly phosphorylated form was identified in mouse, and singly phosphorylated, singly deamidated, and deamidated/phosphorylated forms were identified and quantified in human non-failing and failing heart samples, thus demonstrating the clinical utility of the method.