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\n \n\n \n \n Agostini, S., Harvey, B. P., Wada, S., Kon, K., Milazzo, M., Inaba, K., & Hall-Spencer, J. M.\n\n\n \n \n \n \n \n Ocean acidification drives community shifts towards simplified non-calcified habitats in a subtropical−temperate transition zone.\n \n \n \n \n\n\n \n\n\n\n Scientific Reports, 8(1): 11354. December 2018.\n \n\n\n\n
\n\n\n\n \n \n \"OceanPaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n  \n \n 32 downloads\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{agostini_ocean_2018,\n\ttitle = {Ocean acidification drives community shifts towards simplified non-calcified habitats in a subtropical−temperate transition zone},\n\tvolume = {8},\n\tissn = {2045-2322},\n\turl = {http://www.nature.com/articles/s41598-018-29251-7},\n\tdoi = {10.1038/s41598-018-29251-7},\n\tlanguage = {en},\n\tnumber = {1},\n\turldate = {2021-07-27},\n\tjournal = {Scientific Reports},\n\tauthor = {Agostini, Sylvain and Harvey, Ben P. and Wada, Shigeki and Kon, Koetsu and Milazzo, Marco and Inaba, Kazuo and Hall-Spencer, Jason M.},\n\tmonth = dec,\n\tyear = {2018},\n\tpages = {11354},\n}\n\n
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\n \n\n \n \n Harvey, B. P., Agostini, S., Wada, S., Inaba, K., & Hall-Spencer, J. M.\n\n\n \n \n \n \n \n Dissolution: The Achilles’ Heel of the Triton Shell in an Acidifying Ocean.\n \n \n \n \n\n\n \n\n\n\n Frontiers in Marine Science, 5: 371. October 2018.\n \n\n\n\n
\n\n\n\n \n \n \"Dissolution:Paper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n  \n \n 31 downloads\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{harvey_dissolution_2018,\n\ttitle = {Dissolution: {The} {Achilles}’ {Heel} of the {Triton} {Shell} in an {Acidifying} {Ocean}},\n\tvolume = {5},\n\tissn = {2296-7745},\n\tshorttitle = {Dissolution},\n\turl = {https://www.frontiersin.org/article/10.3389/fmars.2018.00371/full},\n\tdoi = {10.3389/fmars.2018.00371},\n\turldate = {2021-07-27},\n\tjournal = {Frontiers in Marine Science},\n\tauthor = {Harvey, Ben P. and Agostini, Sylvain and Wada, Shigeki and Inaba, Kazuo and Hall-Spencer, Jason M.},\n\tmonth = oct,\n\tyear = {2018},\n\tpages = {371},\n}\n\n
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\n \n\n \n \n Hill, R. W., Armstrong, E. J., Inaba, K., Morita, M., Tresguerres, M., Stillman, J. H., Roa, J. N., & Kwan, G. T.\n\n\n \n \n \n \n \n Acid secretion by the boring organ of the burrowing giant clam, Tridacna crocea.\n \n \n \n \n\n\n \n\n\n\n Biology Letters, 14(6): 20180047. June 2018.\n \n\n\n\n
\n\n\n\n \n \n \"AcidPaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n  \n \n abstract \n \n\n \n  \n \n 4 downloads\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{hill_acid_2018,\n\ttitle = {Acid secretion by the boring organ of the burrowing giant clam, \\textit{{Tridacna} crocea}},\n\tvolume = {14},\n\tissn = {1744-9561, 1744-957X},\n\turl = {https://royalsocietypublishing.org/doi/10.1098/rsbl.2018.0047},\n\tdoi = {10.1098/rsbl.2018.0047},\n\tabstract = {The giant clam\n              Tridacna crocea\n              , native to Indo-Pacific coral reefs, is noted for its unique ability to bore fully into coral rock and is a major agent of reef bioerosion. However,\n              T. crocea\n              's mechanism of boring has remained a mystery despite decades of research. By exploiting a new, two-dimensional pH-sensing technology and manipulating clams to press their presumptive boring tissue (the pedal mantle) against pH-sensing foils, we show that this tissue lowers the pH of surfaces it contacts by greater than or equal to 2 pH units below seawater pH day and night. Acid secretion is likely mediated by vacuolar-type H\n              +\n              -ATPase, which we demonstrate (by immunofluorescence) is abundant in the pedal mantle outer epithelium. Our discovery of acid secretion solves this decades-old mystery and reveals that, during bioerosion,\n              T. crocea\n              can liberate reef constituents directly to the soluble phase, rather than producing sediment alone as earlier assumed.},\n\tlanguage = {en},\n\tnumber = {6},\n\turldate = {2021-07-27},\n\tjournal = {Biology Letters},\n\tauthor = {Hill, Richard W. and Armstrong, Eric J. and Inaba, Kazuo and Morita, Masaya and Tresguerres, Martin and Stillman, Jonathon H. and Roa, Jinae N. and Kwan, Garfield T.},\n\tmonth = jun,\n\tyear = {2018},\n\tpages = {20180047},\n}\n\n
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\n The giant clam Tridacna crocea , native to Indo-Pacific coral reefs, is noted for its unique ability to bore fully into coral rock and is a major agent of reef bioerosion. However, T. crocea 's mechanism of boring has remained a mystery despite decades of research. By exploiting a new, two-dimensional pH-sensing technology and manipulating clams to press their presumptive boring tissue (the pedal mantle) against pH-sensing foils, we show that this tissue lowers the pH of surfaces it contacts by greater than or equal to 2 pH units below seawater pH day and night. Acid secretion is likely mediated by vacuolar-type H + -ATPase, which we demonstrate (by immunofluorescence) is abundant in the pedal mantle outer epithelium. Our discovery of acid secretion solves this decades-old mystery and reveals that, during bioerosion, T. crocea can liberate reef constituents directly to the soluble phase, rather than producing sediment alone as earlier assumed.\n
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\n \n\n \n \n Inaba, K.\n\n\n \n \n \n \n \n Biochemical purification of axonemal and cytoplasmic dyneins.\n \n \n \n \n\n\n \n\n\n\n In Dyneins, pages 88–111. Elsevier, 2018.\n \n\n\n\n
\n\n\n\n \n \n \"BiochemicalPaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@incollection{inaba_biochemical_2018,\n\ttitle = {Biochemical purification of axonemal and cytoplasmic dyneins},\n\tisbn = {978-0-12-809470-9},\n\turl = {https://linkinghub.elsevier.com/retrieve/pii/B9780128094709000047},\n\tlanguage = {en},\n\turldate = {2021-07-27},\n\tbooktitle = {Dyneins},\n\tpublisher = {Elsevier},\n\tauthor = {Inaba, Kazuo},\n\tyear = {2018},\n\tdoi = {10.1016/B978-0-12-809470-9.00004-7},\n\tpages = {88--111},\n}\n\n
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\n \n\n \n \n Inaba, K., & Shiba, K.\n\n\n \n \n \n \n \n Microscopic analysis of sperm movement: links to mechanisms and protein components.\n \n \n \n \n\n\n \n\n\n\n Microscopy, 67(3): 144–155. June 2018.\n \n\n\n\n
\n\n\n\n \n \n \"MicroscopicPaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{inaba_microscopic_2018,\n\ttitle = {Microscopic analysis of sperm movement: links to mechanisms and protein components},\n\tvolume = {67},\n\tissn = {2050-5698, 2050-5701},\n\tshorttitle = {Microscopic analysis of sperm movement},\n\turl = {https://academic.oup.com/jmicro/article/67/3/144/4993734},\n\tdoi = {10.1093/jmicro/dfy021},\n\tlanguage = {en},\n\tnumber = {3},\n\turldate = {2021-07-27},\n\tjournal = {Microscopy},\n\tauthor = {Inaba, Kazuo and Shiba, Kogiku},\n\tmonth = jun,\n\tyear = {2018},\n\tpages = {144--155},\n}\n\n
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\n \n\n \n \n Kamiya, R., Shiba, K., Inaba, K., & Kato-Minoura, T.\n\n\n \n \n \n \n \n Release of Sticky Glycoproteins from Chlamydomonas Flagella During Microsphere Translocation on the Surface Membrane.\n \n \n \n \n\n\n \n\n\n\n Zoological Science, 35(4): 299. August 2018.\n \n\n\n\n
\n\n\n\n \n \n \"ReleasePaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{kamiya_release_2018,\n\ttitle = {Release of {Sticky} {Glycoproteins} from \\textit{{Chlamydomonas} {Flagella}} {During} {Microsphere} {Translocation} on the {Surface} {Membrane}},\n\tvolume = {35},\n\tissn = {0289-0003},\n\turl = {https://bioone.org/journals/zoological-science/volume-35/issue-4/zs180025/Release-of-Sticky-Glycoproteins-from-Chlamydomonas-Flagella-During-Microsphere-Translocation/10.2108/zs180025.full},\n\tdoi = {10.2108/zs180025},\n\tnumber = {4},\n\turldate = {2021-07-27},\n\tjournal = {Zoological Science},\n\tauthor = {Kamiya, Ritsu and Shiba, Kogiku and Inaba, Kazuo and Kato-Minoura, Takako},\n\tmonth = aug,\n\tyear = {2018},\n\tpages = {299},\n}\n\n
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\n \n\n \n \n Mizotani, Y., Suzuki, M., Hotta, K., Watanabe, H., Shiba, K., Inaba, K., Tashiro, E., Oka, K., & Imoto, M.\n\n\n \n \n \n \n \n 14-3-3εa directs the pulsatile transport of basal factors toward the apical domain for lumen growth in tubulogenesis.\n \n \n \n \n\n\n \n\n\n\n Proceedings of the National Academy of Sciences, 115(38): E8873–E8881. September 2018.\n \n\n\n\n
\n\n\n\n \n \n \"14-3-3εaPaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n  \n \n abstract \n \n\n \n  \n \n 4 downloads\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{mizotani_14-3-3directs_2018,\n\ttitle = {14-3-3εa directs the pulsatile transport of basal factors toward the apical domain for lumen growth in tubulogenesis},\n\tvolume = {115},\n\tissn = {0027-8424, 1091-6490},\n\turl = {http://www.pnas.org/lookup/doi/10.1073/pnas.1808756115},\n\tdoi = {10.1073/pnas.1808756115},\n\tabstract = {The\n              Ciona\n              notochord has emerged as a simple and tractable in vivo model for tubulogenesis. Here, using a chemical genetics approach, we identified UTKO1 as a selective small molecule inhibitor of notochord tubulogenesis. We identified 14-3-3εa protein as a direct binding partner of UTKO1 and showed that 14-3-3εa knockdown leads to failure of notochord tubulogenesis. We found that UTKO1 prevents 14-3-3εa from interacting with ezrin/radixin/moesin (ERM), which is required for notochord tubulogenesis, suggesting that interactions between 14-3-3εa and ERM play a key role in regulating the early steps of tubulogenesis. Using live imaging, we found that, as lumens begin to open between neighboring cells, 14-3-3εa and ERM are highly colocalized at the basal cortex where they undergo cycles of accumulation and disappearance. Interestingly, the disappearance of 14-3-3εa and ERM during each cycle is tightly correlated with a transient flow of 14-3-3εa, ERM, myosin II, and other cytoplasmic elements from the basal surface toward the lumen-facing apical domain, which is often accompanied by visible changes in lumen architecture. Both pulsatile flow and lumen formation are abolished in larvae treated with UTKO1, in larvae depleted of either 14-3-3εa or ERM, or in larvae expressing a truncated form of 14-3-3εa that lacks the ability to interact with ERM. These results suggest that 14-3-3εa and ERM interact at the basal cortex to direct pulsatile basal accumulation and basal–apical transport of factors that are essential for lumen formation. We propose that similar mechanisms may underlie or may contribute to lumen formation in tubulogenesis in other systems.},\n\tlanguage = {en},\n\tnumber = {38},\n\turldate = {2021-07-27},\n\tjournal = {Proceedings of the National Academy of Sciences},\n\tauthor = {Mizotani, Yuji and Suzuki, Mayu and Hotta, Kohji and Watanabe, Hidenori and Shiba, Kogiku and Inaba, Kazuo and Tashiro, Etsu and Oka, Kotaro and Imoto, Masaya},\n\tmonth = sep,\n\tyear = {2018},\n\tpages = {E8873--E8881},\n}\n\n
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\n The Ciona notochord has emerged as a simple and tractable in vivo model for tubulogenesis. Here, using a chemical genetics approach, we identified UTKO1 as a selective small molecule inhibitor of notochord tubulogenesis. We identified 14-3-3εa protein as a direct binding partner of UTKO1 and showed that 14-3-3εa knockdown leads to failure of notochord tubulogenesis. We found that UTKO1 prevents 14-3-3εa from interacting with ezrin/radixin/moesin (ERM), which is required for notochord tubulogenesis, suggesting that interactions between 14-3-3εa and ERM play a key role in regulating the early steps of tubulogenesis. Using live imaging, we found that, as lumens begin to open between neighboring cells, 14-3-3εa and ERM are highly colocalized at the basal cortex where they undergo cycles of accumulation and disappearance. Interestingly, the disappearance of 14-3-3εa and ERM during each cycle is tightly correlated with a transient flow of 14-3-3εa, ERM, myosin II, and other cytoplasmic elements from the basal surface toward the lumen-facing apical domain, which is often accompanied by visible changes in lumen architecture. Both pulsatile flow and lumen formation are abolished in larvae treated with UTKO1, in larvae depleted of either 14-3-3εa or ERM, or in larvae expressing a truncated form of 14-3-3εa that lacks the ability to interact with ERM. These results suggest that 14-3-3εa and ERM interact at the basal cortex to direct pulsatile basal accumulation and basal–apical transport of factors that are essential for lumen formation. We propose that similar mechanisms may underlie or may contribute to lumen formation in tubulogenesis in other systems.\n
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\n \n\n \n \n Momose, T., De Cian, A., Shiba, K., Inaba, K., Giovannangeli, C., & Concordet, J.\n\n\n \n \n \n \n \n High doses of CRISPR/Cas9 ribonucleoprotein efficiently induce gene knockout with low mosaicism in the hydrozoan Clytia hemisphaerica through microhomology-mediated deletion.\n \n \n \n \n\n\n \n\n\n\n Scientific Reports, 8(1): 11734. December 2018.\n \n\n\n\n
\n\n\n\n \n \n \"HighPaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{momose_high_2018,\n\ttitle = {High doses of {CRISPR}/{Cas9} ribonucleoprotein efficiently induce gene knockout with low mosaicism in the hydrozoan \\textit{{Clytia} hemisphaerica} through microhomology-mediated deletion},\n\tvolume = {8},\n\tissn = {2045-2322},\n\turl = {http://www.nature.com/articles/s41598-018-30188-0},\n\tdoi = {10.1038/s41598-018-30188-0},\n\tlanguage = {en},\n\tnumber = {1},\n\turldate = {2021-07-27},\n\tjournal = {Scientific Reports},\n\tauthor = {Momose, Tsuyoshi and De Cian, Anne and Shiba, Kogiku and Inaba, Kazuo and Giovannangeli, Carine and Concordet, Jean-Paul},\n\tmonth = dec,\n\tyear = {2018},\n\tpages = {11734},\n}\n\n
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\n \n\n \n \n Morita, N., Inaba, K., & Saito, Y.\n\n\n \n \n \n \n \n Post-Embryonic Development and Genital-Complex Formation in Three Species of Polyclad Flatworms.\n \n \n \n \n\n\n \n\n\n\n Zoological Science, 35(1): 28. January 2018.\n \n\n\n\n
\n\n\n\n \n \n \"Post-EmbryonicPaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n  \n \n 4 downloads\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{morita_post-embryonic_2018,\n\ttitle = {Post-{Embryonic} {Development} and {Genital}-{Complex} {Formation} in {Three} {Species} of {Polyclad} {Flatworms}},\n\tvolume = {35},\n\tissn = {0289-0003},\n\turl = {https://bioone.org/journals/zoological-science/volume-35/issue-1/zs170114/Post-Embryonic-Development-and-Genital-Complex-Formation-in-Three-Species/10.2108/zs170114.full},\n\tdoi = {10.2108/zs170114},\n\tnumber = {1},\n\turldate = {2021-07-27},\n\tjournal = {Zoological Science},\n\tauthor = {Morita, Nozomi and Inaba, Kazuo and Saito, Yasunori},\n\tmonth = jan,\n\tyear = {2018},\n\tpages = {28},\n}\n\n
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\n \n\n \n \n Shojima, T., Hou, F., Takahashi, Y., Matsumura, Y., Okai, M., Nakamura, A., Mizuno, K., Inaba, K., Kojima, M., Miyakawa, T., & Tanokura, M.\n\n\n \n \n \n \n \n Crystal structure of a Ca2+-dependent regulator of flagellar motility reveals the open-closed structural transition.\n \n \n \n \n\n\n \n\n\n\n Scientific Reports, 8(1): 2014. December 2018.\n \n\n\n\n
\n\n\n\n \n \n \"CrystalPaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n  \n \n 4 downloads\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{shojima_crystal_2018,\n\ttitle = {Crystal structure of a {Ca2}+-dependent regulator of flagellar motility reveals the open-closed structural transition},\n\tvolume = {8},\n\tissn = {2045-2322},\n\turl = {http://www.nature.com/articles/s41598-018-19898-7},\n\tdoi = {10.1038/s41598-018-19898-7},\n\tlanguage = {en},\n\tnumber = {1},\n\turldate = {2021-07-27},\n\tjournal = {Scientific Reports},\n\tauthor = {Shojima, Tomoki and Hou, Feng and Takahashi, Yusuke and Matsumura, Yoshitaka and Okai, Masahiko and Nakamura, Akira and Mizuno, Katsutoshi and Inaba, Kazuo and Kojima, Masaki and Miyakawa, Takuya and Tanokura, Masaru},\n\tmonth = dec,\n\tyear = {2018},\n\tpages = {2014},\n}\n\n
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\n \n\n \n \n Ugwu, S. I., Shiba, K., Inaba, K., & Morita, M.\n\n\n \n \n \n \n \n A Unique Seminal Plasma Protein, Zona Pellucida 3-Like Protein, has Ca2 -Dependent Sperm Agglutination Activity.\n \n \n \n \n\n\n \n\n\n\n Zoological Science, 35(2): 161. April 2018.\n \n\n\n\n
\n\n\n\n \n \n \"APaper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n  \n \n 4 downloads\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{ugwu_unique_2018,\n\ttitle = {A {Unique} {Seminal} {Plasma} {Protein}, {Zona} {Pellucida} 3-{Like} {Protein}, has {Ca2} -{Dependent} {Sperm} {Agglutination} {Activity}},\n\tvolume = {35},\n\tissn = {0289-0003},\n\turl = {https://bioone.org/journals/zoological-science/volume-35/issue-2/zs170150/A-Unique-Seminal-Plasma-Protein-Zona-Pellucida-3-Like-Protein/10.2108/zs170150.full},\n\tdoi = {10.2108/zs170150},\n\tnumber = {2},\n\turldate = {2021-07-27},\n\tjournal = {Zoological Science},\n\tauthor = {Ugwu, Stanley Ifeanyi and Shiba, Kogiku and Inaba, Kazuo and Morita, Masaya},\n\tmonth = apr,\n\tyear = {2018},\n\tpages = {161},\n}\n\n
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\n \n\n \n \n Yoshida, K., Shiba, K., Sakamoto, A., Ikenaga, J., Matsunaga, S., Inaba, K., & Yoshida, M.\n\n\n \n \n \n \n \n Ca2+ efflux via plasma membrane Ca2+-ATPase mediates chemotaxis in ascidian sperm.\n \n \n \n \n\n\n \n\n\n\n Scientific Reports, 8(1): 16622. December 2018.\n \n\n\n\n
\n\n\n\n \n \n \"Ca2+Paper\n  \n \n\n \n \n doi\n  \n \n\n \n link\n  \n \n\n bibtex\n \n\n \n\n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{yoshida_ca2_2018,\n\ttitle = {Ca2+ efflux via plasma membrane {Ca2}+-{ATPase} mediates chemotaxis in ascidian sperm},\n\tvolume = {8},\n\tissn = {2045-2322},\n\turl = {http://www.nature.com/articles/s41598-018-35013-2},\n\tdoi = {10.1038/s41598-018-35013-2},\n\tlanguage = {en},\n\tnumber = {1},\n\turldate = {2021-07-27},\n\tjournal = {Scientific Reports},\n\tauthor = {Yoshida, Kaoru and Shiba, Kogiku and Sakamoto, Ayako and Ikenaga, Jumpei and Matsunaga, Shigeru and Inaba, Kazuo and Yoshida, Manabu},\n\tmonth = dec,\n\tyear = {2018},\n\tpages = {16622},\n}\n\n
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