Contrast recovery coefficients versus iteration number for the TOF-PET data with different timing resolutions.

<p>To avoid misleading impacts introduced by artifacts and distortions on contrast recovery coefficient values, only image results for 100–400 ps full width at half maximum TOF-PET data were analyzed here.</p

Sampled intensity profiles of the reconstructed image shown in Figure 5.

<p>The sample lines in (a) show the locations of the profiles.</p

Phantom images with the dotted rectangles as imaging region-of-interest.

<p>(a) The NEMA-IQ phantom is about cm in size, including four hot lesions (10 mm, 13 mm, 17 mm and 22 mm in diameter) and two cold lesions (28 mm and 37 mm in diameter). The region-of-interest size is cm. (b) The Zubal abdomen phantom is about cm in size. The region-of-interest size is cm.</p

Reconstructed images of NEMA-IQ phantom obtained from TOF-PET data with different timing resolutions.

<p>Note that only the structures inside the ROI are displayed.</p

Sampled intensity profiles for NEMA-IQ phantom obtained from TOF-PET data with different TRs.

<p>The profiles were obtained from the reconstructed images shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0072109#pone-0072109-g007" target="_blank">Figure 7</a>.</p

Reconstructed images of Zubal abdomen phantom obtained from TOF-PET data with different timing resolutions.

<p>The circle shows the low uptake lesion inside the liver. Note that only the structures inside the ROI are displayed.</p

Event discrimination in data acquisition.

<p> indicates the arrival time difference of two photons, is the speed of light, is the distance between the annihilation position and the midpoint of line-of-response.</p

Measurable time differences distribution in conventional (a) and region-of-interest imaging (b).

<p>The distribution was assumed as a Gaussian function with full width at half maximum determined by the system timing resolution.</p

Molecular Cloning and Characterization of Different Expression of <i>MYOZ2</i> and <i>MYOZ3</i> in Tianfu Goat

<div><p>The myozenin family of proteins binds calcineurin, which is involved in myocyte differentiation of skeletal muscle. Moreover, gene expression of myozenin is closely related to meat quality. To further understand the functions and effects of myozenin2 (<i>MYOZ2</i>) and myozenin3 (<i>MYOZ3</i>) genes in goat, we cloned them from Tianfu goat longissimus dorsi muscle. Sequence analyses revealed that full-length coding sequence of <i>MYOZ2</i> consisted of 795 bp and encoded 264 amino acids, and full-length coding sequence of <i>MYOZ3</i> consisted of 735 bp and encoded 244 amino acids. RT-qPCR analyses revealed that mRNA expressions of <i>MYOZ2</i> and <i>MYOZ3</i> were detected in heart, liver, spleen, lung, kidney, leg muscle, abdominal muscle, and longissimus dorsi muscle. Particularly high expression levels of <i>MYOZ2</i> were seen in abdominal muscle and heart (<i>P</i><0.01), low expression levels were seen in leg muscle (<i>P</i><0.01), longissimus dorsi muscle (<i>P</i>>0.05) and very little expression were detected in liver, spleen, lung and kidney (<i>P</i>>0.05). In addition, high expression levels of <i>MYOZ3</i> were seen in abdominal muscle, leg muscle, lungs and kidney (<i>P</i><0.01), low expression levels were found in longissimus dorsi muscle and spleen (<i>P</i><0.01) and very little expression were detected in heart and liver (<i>P</i>>0.05). Temporal mRNA expression results showed that <i>MYOZ2</i> and <i>MYOZ3</i> gene expression varied across four muscle tissues with different ages of the goats. Western blotting further revealed that MYOZ2 and MYOZ3 proteins were only expressed in goat muscle, with notable temporal expression differences in specialized muscle tissues from five development age stages. This work provides the first evidence that <i>MYOZ2</i> and <i>MYOZ3</i> genes are expressed abundantly in Tianfu goat muscle tissues from different development age stages, and lay a foundation for understanding the functions of <i>MYOZ2</i> and <i>MYOZ3</i> genes in muscle fiber differentiation.</p></div

r<i>Bm</i>αTX14 Increases the Life Span and Promotes the Locomotion of <i>Caenorhabditis Elegans</i>

<div><p>The scorpion has been extensively used in various pharmacological profiles or as food supplies. The exploration of scorpion venom has been reported due to the presence of recombinant peptides. r<i>Bm</i>αTX14 is an α-neurotoxin extracted from the venom gland of the East Asian scorpion <i>Buthus martensii</i> Karsch and can affect ion channel conductance. Here, we investigated the functions of r<i>Bmα</i>TX14 using the <i>Caenorhabditis elegans</i> model. Using western blot analysis, r<i>Bm</i>αTX14 was shown to be expressed both in the cytoplasm and inclusion bodies in the <i>E</i>.<i>coli Rosetta</i> (DE3) strain. Circular dichroism spectroscopy analysis demonstrated that purified r<i>Bm</i>αTX14 retained its biological structures. Next, feeding nematodes with <i>E</i>.<i>coli Rosetta</i> (DE3) expressing r<i>Bm</i>αTX14 caused extension of the life span and promoted the locomotion of the nematodes. In addition, we identified several genes that play various roles in the life span and locomotion of <i>C</i>. <i>elegans</i> through microarray analysis and quantitative real-time PCR. Furthermore, if the amino acid site H₁₅ of r<i>Bm</i>αTX14 was mutated, r<i>Bm</i>αTX14 no longer promoted the <i>C</i>. <i>elegans</i> life span. In conclusion, the results not only demonstrated the functions and mechanism of r<i>Bm</i>αTX14 in <i>C</i>. <i>elegans</i>, but also provided the new sight in the utility of recombinant peptides from scorpion venom.</p></div