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\n \n\n \n \n Murata, Y., Iwasaki, H., Sasaki, M., Inaba, K., & Okamura, Y.\n\n\n \n \n \n \n \n Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor.\n \n \n \n \n\n\n \n\n\n\n Nature, 435(7046): 1239–1243. June 2005.\n \n\n\n\n
\n\n\n\n \n \n \"PhosphoinositidePaper\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 1 download\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{murata_phosphoinositide_2005,\n\ttitle = {Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor},\n\tvolume = {435},\n\tissn = {0028-0836, 1476-4687},\n\turl = {http://www.nature.com/articles/nature03650},\n\tdoi = {10.1038/nature03650},\n\tlanguage = {en},\n\tnumber = {7046},\n\turldate = {2021-07-26},\n\tjournal = {Nature},\n\tauthor = {Murata, Yoshimichi and Iwasaki, Hirohide and Sasaki, Mari and Inaba, Kazuo and Okamura, Yasushi},\n\tmonth = jun,\n\tyear = {2005},\n\tpages = {1239--1243},\n}\n\n
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\n \n\n \n \n Satouh, Y., Padma, P., Toda, T., Satoh, N., Ide, H., & Inaba, K.\n\n\n \n \n \n \n \n Molecular Characterization of Radial Spoke Subcomplex Containing Radial Spoke Protein 3 and Heat Shock Protein 40 in Sperm Flagella of the Ascidian Ciona intestinalis.\n \n \n \n \n\n\n \n\n\n\n Molecular Biology of the Cell, 16(2): 626–636. February 2005.\n \n\n\n\n
\n\n\n\n \n \n \"MolecularPaper\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 1 download\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{satouh_molecular_2005,\n\ttitle = {Molecular {Characterization} of {Radial} {Spoke} {Subcomplex} {Containing} {Radial} {Spoke} {Protein} 3 and {Heat} {Shock} {Protein} 40 in {Sperm} {Flagella} of the {Ascidian} \\textit{{Ciona} intestinalis}},\n\tvolume = {16},\n\tissn = {1059-1524, 1939-4586},\n\turl = {https://www.molbiolcell.org/doi/10.1091/mbc.e04-09-0784},\n\tdoi = {10.1091/mbc.e04-09-0784},\n\tabstract = {Members of the heat-shock protein (HSP)40 regulate the protein folding activity of HSP70 proteins and help the functional specialization of this molecular chaperone system in various types of cellular events. We have recently identified Hsp40 as a component of flagellar axoneme in the ascidian Ciona intestinalis, suggesting a correlation between Hsp40 related chaperone system and flagellar function. In this study, we have found that Ciona 37-kDa Hsp40 is extracted from KCl-treated axonemes with 0.5 M KI solution and comigrates with radial spoke protein (RSP)3 along with several proteins as a complex through gel filtration and ion exchange columns. Peptide mass fingerprinting with matrix-assisted laser desorption ionization/time of flight/mass spectrometry revealed that other proteins in the complex include a homolog of sea urchin spokehead protein (homolog of RSP4/6), a membrane occupation and recognition nexus repeat protein with sequence similarity with meichroacidin, and a functionally unknown 33-kDa protein. A spoke head protein, LRR37, is not included in the complex, suggesting that the complex constructs the stalk of radial spoke. Immunoelectron microscopy indicates that Hsp40 is localized in the distal portion of spoke stalk, possibly at the junction between spoke head and the stalk.},\n\tlanguage = {en},\n\tnumber = {2},\n\turldate = {2021-07-26},\n\tjournal = {Molecular Biology of the Cell},\n\tauthor = {Satouh, Yuhkoh and Padma, Potturi and Toda, Toshifusa and Satoh, Nori and Ide, Hiroyuki and Inaba, Kazuo},\n\tmonth = feb,\n\tyear = {2005},\n\tpages = {626--636},\n}\n
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\n Members of the heat-shock protein (HSP)40 regulate the protein folding activity of HSP70 proteins and help the functional specialization of this molecular chaperone system in various types of cellular events. We have recently identified Hsp40 as a component of flagellar axoneme in the ascidian Ciona intestinalis, suggesting a correlation between Hsp40 related chaperone system and flagellar function. In this study, we have found that Ciona 37-kDa Hsp40 is extracted from KCl-treated axonemes with 0.5 M KI solution and comigrates with radial spoke protein (RSP)3 along with several proteins as a complex through gel filtration and ion exchange columns. Peptide mass fingerprinting with matrix-assisted laser desorption ionization/time of flight/mass spectrometry revealed that other proteins in the complex include a homolog of sea urchin spokehead protein (homolog of RSP4/6), a membrane occupation and recognition nexus repeat protein with sequence similarity with meichroacidin, and a functionally unknown 33-kDa protein. A spoke head protein, LRR37, is not included in the complex, suggesting that the complex constructs the stalk of radial spoke. Immunoelectron microscopy indicates that Hsp40 is localized in the distal portion of spoke stalk, possibly at the junction between spoke head and the stalk.\n
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\n \n\n \n \n Shiba, K., Ohmuro, J., Mogami, Y., Nishigaki, T., Wood, C. D., Darszon, A., Tatsu, Y., Yumoto, N., & Baba, S. A.\n\n\n \n \n \n \n \n Sperm-Activating Peptide Induces Asymmetric Flagellar Bending in Sea Urchin Sperm.\n \n \n \n \n\n\n \n\n\n\n Zoological Science, 22(3): 293–299. March 2005.\n \n\n\n\n
\n\n\n\n \n \n \"Sperm-ActivatingPaper\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 3 downloads\n \n \n\n \n \n \n \n \n \n \n\n  \n \n \n\n\n\n
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@article{shiba_sperm-activating_2005,\n\ttitle = {Sperm-{Activating} {Peptide} {Induces} {Asymmetric} {Flagellar} {Bending} in {Sea} {Urchin} {Sperm}},\n\tvolume = {22},\n\tissn = {0289-0003},\n\turl = {http://www.bioone.org/doi/abs/10.2108/zsj.22.293},\n\tdoi = {10.2108/zsj.22.293},\n\tlanguage = {en},\n\tnumber = {3},\n\turldate = {2021-07-26},\n\tjournal = {Zoological Science},\n\tauthor = {Shiba, Kogiku and Ohmuro, Junko and Mogami, Yoshihiro and Nishigaki, Takuya and Wood, Christopher D. and Darszon, Alberto and Tatsu, Yoshiro and Yumoto, Noboru and Baba, Shoji A.},\n\tmonth = mar,\n\tyear = {2005},\n\tpages = {293--299},\n}\n\n
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\n \n\n \n \n 柴小菊, & 吉田\n\n\n \n \n \n \n 卵由来物質によるホヤ精子の運動制御機構.\n \n \n \n\n\n \n\n\n\n 号外海洋, 41: 98–104. 2005.\n \n\n\n\n
\n\n\n\n \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{__2005-2,\n\ttitle = {卵由来物質によるホヤ精子の運動制御機構},\n\tvolume = {41},\n\tjournal = {号外海洋},\n\tauthor = {{柴小菊} and {吉田}},\n\tyear = {2005},\n\tpages = {98--104},\n}\n\n
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\n \n\n \n \n 稲葉一男\n\n\n \n \n \n \n 境界動物の生物学—脊椎動物への進化の研究最前線—、ホヤ精巣における遺伝子発現とそれらの機能解析.\n \n \n \n\n\n \n\n\n\n 月刊海洋, 41: 89–97. 2005.\n \n\n\n\n
\n\n\n\n \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{__2005-4,\n\ttitle = {境界動物の生物学—脊椎動物への進化の研究最前線—、ホヤ精巣における遺伝子発現とそれらの機能解析},\n\tvolume = {41},\n\tjournal = {月刊海洋},\n\tauthor = {{稲葉一男}},\n\tyear = {2005},\n\tpages = {89--97},\n}\n\n
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