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      <title>Wiley: genesis: Table of Contents</title>
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      <dc:title>Wiley: genesis: Table of Contents</dc:title>
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         <link>https://onlinelibrary.wiley.com/doi/10.1002/dvg.70055?af=R</link>
         <pubDate>Tue, 12 May 2026 00:00:00 -0700</pubDate>
         <dc:date>2026-05-12T12:00:00-07:00</dc:date>
         <source url="https://onlinelibrary.wiley.com/journal/1526968x?af=R">Wiley: genesis: Table of Contents</source>
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         <title>Issue Information</title>
         <description>genesis, Volume 64, Issue 3, June 2026. </description>
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         <category>ISSUE INFORMATION</category>
         <dc:title>Issue Information</dc:title>
         <dc:identifier>10.1002/dvg.70055</dc:identifier>
         <prism:publicationName>genesis</prism:publicationName>
         <prism:doi>10.1002/dvg.70055</prism:doi>
         <prism:url>https://onlinelibrary.wiley.com/doi/10.1002/dvg.70055?af=R</prism:url>
         <prism:section>ISSUE INFORMATION</prism:section>
         <prism:volume>64</prism:volume>
         <prism:number>3</prism:number>
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         <link>https://onlinelibrary.wiley.com/doi/10.1002/dvg.70054?af=R</link>
         <pubDate>Tue, 12 May 2026 00:00:00 -0700</pubDate>
         <dc:date>2026-05-12T12:00:00-07:00</dc:date>
         <source url="https://onlinelibrary.wiley.com/journal/1526968x?af=R">Wiley: genesis: Table of Contents</source>
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         <title>Phylogenetic Comparison and Splice Site Conservation of the Animal SMNDC1 Gene Family</title>
         <description>genesis, Volume 64, Issue 3, June 2026. </description>
         <dc:description>
ABSTRACT
Alternative splicing is a key post‐transcriptional process that generates multiple mRNAs from a single pre‐mRNA through the coordinated action of the spliceosome and associated splicing factors. SMNDC1 (survival motor neuron domain containing 1) has been identified as an integral component of the spliceosome complex. Previous studies have shown that SMNDC1 is essential for splicing catalysis in vitro and plays a regulatory role in intron retention in cancer. However, the phylogenetic relationships and expression patterns of SMNDC1 across the animal kingdom have not been systematically investigated. In this study, we conducted a comprehensive phylogenetic analysis of SMNDC1 genes in animals. A total of 72 SMNDC1 genes were identified from 66 animal species. Bioinformatic analyses revealed that the gene structure and protein domains of SMNDC1 are highly conserved, with only a few species possessing gene duplications. Notably, the human SMNDC1 gene exhibits elevated expression levels in multiple cancer types, including breast, colon, and rectal cancers, suggesting its potential role in tumor development and its value as a diagnostic or therapeutic target. Overall, our findings provide a systematic overview of the SMNDC1 gene family in animals and establish a foundation for future studies exploring its molecular functions and evolutionary significance.
</dc:description>
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&lt;h2&gt;ABSTRACT&lt;/h2&gt;
&lt;p&gt;Alternative splicing is a key post-transcriptional process that generates multiple mRNAs from a single pre-mRNA through the coordinated action of the spliceosome and associated splicing factors. SMNDC1 (survival motor neuron domain containing 1) has been identified as an integral component of the spliceosome complex. Previous studies have shown that SMNDC1 is essential for splicing catalysis in vitro and plays a regulatory role in intron retention in cancer. However, the phylogenetic relationships and expression patterns of SMNDC1 across the animal kingdom have not been systematically investigated. In this study, we conducted a comprehensive phylogenetic analysis of SMNDC1 genes in animals. A total of 72 SMNDC1 genes were identified from 66 animal species. Bioinformatic analyses revealed that the gene structure and protein domains of SMNDC1 are highly conserved, with only a few species possessing gene duplications. Notably, the human SMNDC1 gene exhibits elevated expression levels in multiple cancer types, including breast, colon, and rectal cancers, suggesting its potential role in tumor development and its value as a diagnostic or therapeutic target. Overall, our findings provide a systematic overview of the SMNDC1 gene family in animals and establish a foundation for future studies exploring its molecular functions and evolutionary significance.&lt;/p&gt;</content:encoded>
         <dc:creator>
Jing‐wan Zhang, 
Hong‐Mei Wang, 
Guojun Ouyang, 
Chao Sun, 
Bao‐Xing Huang
</dc:creator>
         <category>RESEARCH ARTICLE</category>
         <dc:title>Phylogenetic Comparison and Splice Site Conservation of the Animal SMNDC1 Gene Family</dc:title>
         <dc:identifier>10.1002/dvg.70054</dc:identifier>
         <prism:publicationName>genesis</prism:publicationName>
         <prism:doi>10.1002/dvg.70054</prism:doi>
         <prism:url>https://onlinelibrary.wiley.com/doi/10.1002/dvg.70054?af=R</prism:url>
         <prism:section>RESEARCH ARTICLE</prism:section>
         <prism:volume>64</prism:volume>
         <prism:number>3</prism:number>
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         <link>https://onlinelibrary.wiley.com/doi/10.1002/dvg.70053?af=R</link>
         <pubDate>Sat, 09 May 2026 00:00:00 -0700</pubDate>
         <dc:date>2026-05-09T12:00:00-07:00</dc:date>
         <source url="https://onlinelibrary.wiley.com/journal/1526968x?af=R">Wiley: genesis: Table of Contents</source>
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         <title>Pvr and Pvf2 Are Essential for Valve Cell Differentiation in the Larval Drosophila Heart</title>
         <description>genesis, Volume 64, Issue 3, June 2026. </description>
         <dc:description>
ABSTRACT
The directionality of blood flow is regulated by heart valves, among other things. While the heart valves in vertebrates are multicellular and complex, the valve in the Drosophila heart consists of exactly two highly specialized cells. They arise during early larval development from two cardiomyocytes, those that form the boundary between the aorta and the posterior ventricle. Here, we show that the conserved PDGF signaling pathway is involved in the determination of heart valve cells. RNAi‐mediated knockdown of the Pvr receptor and one of its ligands, Pvf2, leads to an inhibition of valve cell differentiation. In contrast, the simultaneous expression of the Pvr and Pvf2 in the entire heart tube leads to the formation of additional heart valve cells in ectopic positions. A single expression of the receptor or the ligand does not lead to heart valve formation.
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&lt;h2&gt;ABSTRACT&lt;/h2&gt;
&lt;p&gt;The directionality of blood flow is regulated by heart valves, among other things. While the heart valves in vertebrates are multicellular and complex, the valve in the &lt;i&gt;Drosophila&lt;/i&gt; heart consists of exactly two highly specialized cells. They arise during early larval development from two cardiomyocytes, those that form the boundary between the aorta and the posterior ventricle. Here, we show that the conserved PDGF signaling pathway is involved in the determination of heart valve cells. RNAi-mediated knockdown of the Pvr receptor and one of its ligands, Pvf2, leads to an inhibition of valve cell differentiation. In contrast, the simultaneous expression of the Pvr and Pvf2 in the entire heart tube leads to the formation of additional heart valve cells in ectopic positions. A single expression of the receptor or the ligand does not lead to heart valve formation.&lt;/p&gt;</content:encoded>
         <dc:creator>
Heiko Meyer, 
Christian Meyer, 
Bettina Priess, 
Achim Paululat
</dc:creator>
         <category>RESEARCH ARTICLE</category>
         <dc:title>Pvr and Pvf2 Are Essential for Valve Cell Differentiation in the Larval Drosophila Heart</dc:title>
         <dc:identifier>10.1002/dvg.70053</dc:identifier>
         <prism:publicationName>genesis</prism:publicationName>
         <prism:doi>10.1002/dvg.70053</prism:doi>
         <prism:url>https://onlinelibrary.wiley.com/doi/10.1002/dvg.70053?af=R</prism:url>
         <prism:section>RESEARCH ARTICLE</prism:section>
         <prism:volume>64</prism:volume>
         <prism:number>3</prism:number>
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      <item>
         <link>https://onlinelibrary.wiley.com/doi/10.1002/dvg.70056?af=R</link>
         <pubDate>Sat, 09 May 2026 00:00:00 -0700</pubDate>
         <dc:date>2026-05-09T12:00:00-07:00</dc:date>
         <source url="https://onlinelibrary.wiley.com/journal/1526968x?af=R">Wiley: genesis: Table of Contents</source>
         <prism:coverDate>Mon, 01 Jun 2026 00:00:00 -0700</prism:coverDate>
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         <title>Efficient Gene Expression System in Medaka Embryos Enables Functional Characterization of nt5c1a Paralogs Involved in Inosine Monophosphate Metabolism</title>
         <description>genesis, Volume 64, Issue 3, June 2026. </description>
         <dc:description>
ABSTRACT
Optimizing transient expression systems in fish embryos is crucial for rapid gene function analysis. Here, we established an efficient system in medaka (Oryzias latipes) embryos by evaluating nucleic acid type and injection site. Our results revealed that injecting the elongation factor 1αA (ef1αA) promoter‐driven plasmid into the yolk yielded the highest expression on day 1 post‐fertilization. Using this optimized system, we investigated cytosolic 5′‐nucleotidase 1a (nt5c1a), which is involved in the metabolism of inosine monophosphate (IMP), an umami flavor compound. In silico analysis revealed that medaka had two nt5c1a paralogs: nt5c1aa and nt5c1ab. While nt5c1ab retains conserved substrate‐recognition sequences and exhibits significant IMP degradation activity, nt5c1aa has lost these functions. Structural analysis using AlphaFold revealed that the Nt5c1aa L305P mutation causes local conformational changes near the substrate‐binding site, potentially altering substrate orientation without disrupting the overall protein fold. Our expression system demonstrated that this single L305P substitution partially restored IMP‐degrading activity in Nt5c1aa, confirming that residue 305 is a key determinant of its functional divergence. Our findings provide a robust foundation for molecular breeding to enhance umami flavor in farmed fish. Specifically, the targeted manipulation of these nt5c1a paralogs could facilitate developing breeds with maximized IMP accumulation in muscle tissues.
</dc:description>
         <content:encoded>
&lt;h2&gt;ABSTRACT&lt;/h2&gt;
&lt;p&gt;Optimizing transient expression systems in fish embryos is crucial for rapid gene function analysis. Here, we established an efficient system in medaka (&lt;i&gt;Oryzias latipes&lt;/i&gt;) embryos by evaluating nucleic acid type and injection site. Our results revealed that injecting the &lt;i&gt;elongation factor 1αA&lt;/i&gt; (&lt;i&gt;ef1αA&lt;/i&gt;) promoter-driven plasmid into the yolk yielded the highest expression on day 1 post-fertilization. Using this optimized system, we investigated &lt;i&gt;cytosolic 5′-nucleotidase 1a&lt;/i&gt; (&lt;i&gt;nt5c1a&lt;/i&gt;), which is involved in the metabolism of inosine monophosphate (IMP), an umami flavor compound. In silico analysis revealed that medaka had two &lt;i&gt;nt5c1a&lt;/i&gt; paralogs: &lt;i&gt;nt5c1aa&lt;/i&gt; and &lt;i&gt;nt5c1ab&lt;/i&gt;. While &lt;i&gt;nt5c1ab&lt;/i&gt; retains conserved substrate-recognition sequences and exhibits significant IMP degradation activity, &lt;i&gt;nt5c1aa&lt;/i&gt; has lost these functions. Structural analysis using AlphaFold revealed that the Nt5c1aa L305P mutation causes local conformational changes near the substrate-binding site, potentially altering substrate orientation without disrupting the overall protein fold. Our expression system demonstrated that this single L305P substitution partially restored IMP-degrading activity in Nt5c1aa, confirming that residue 305 is a key determinant of its functional divergence. Our findings provide a robust foundation for molecular breeding to enhance umami flavor in farmed fish. Specifically, the targeted manipulation of these &lt;i&gt;nt5c1a&lt;/i&gt; paralogs could facilitate developing breeds with maximized IMP accumulation in muscle tissues.&lt;/p&gt;</content:encoded>
         <dc:creator>
Yu Murakami, 
Tomohisa Horibe, 
Masashi Ando, 
Toru Kobayashi
</dc:creator>
         <category>RESEARCH ARTICLE</category>
         <dc:title>Efficient Gene Expression System in Medaka Embryos Enables Functional Characterization of nt5c1a Paralogs Involved in Inosine Monophosphate Metabolism</dc:title>
         <dc:identifier>10.1002/dvg.70056</dc:identifier>
         <prism:publicationName>genesis</prism:publicationName>
         <prism:doi>10.1002/dvg.70056</prism:doi>
         <prism:url>https://onlinelibrary.wiley.com/doi/10.1002/dvg.70056?af=R</prism:url>
         <prism:section>RESEARCH ARTICLE</prism:section>
         <prism:volume>64</prism:volume>
         <prism:number>3</prism:number>
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