A Novel Modification of the Lysine Residue at Position 12 of Histone H4 in Starfish Sperm
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概要
- 論文の詳細を見る
Post-translational modification of core histones is essential in processes requiring chromatin remodeling. We report here a novel modification in histones of the sperm of the starfish, Asterina pectinfera, which involves an ε-(γ-glutamyl)lysine cross-link between the glutamine residue at position 9 of histone H2B and the lysine residue at position 12 of histone H4.
- 社団法人日本農芸化学会の論文
- 1997-12-23
著者
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Shimizu Takahiko
Department of Molecular Gerontology, Tokyo Metropolitan Institute of Gerontology
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Takao T
Osaka Univ. Osaka Jpn
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Shimonishi Yasutsugu
Institute for Protein Research, Osaka University
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Shimizu Takahiko
Department Of Applied Biochemistry Hiroshima University
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IKEGAMI Susumu
Department of Applied Biochemistry, Faculty of Applied Biological Sciences, Hiroshima University
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Takao Toshifumi
Institute for Protein Research, Osaka University
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Takao Toshifumi
Institute For Protein Research Osaka University
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Shimonishi Yasutsugu
Institute For Protein Research Osaka University
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Nunomura Kazuto
Fac. Of Applied Biolo. Sci. Hiroshima Univ.
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NUNOMURA Kazuto
Department of Applied Biochemistry, Hiroshima University
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HOZUMI Keiko
Department of Applied Biochemistry, Hiroshima University
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Hozumi Keiko
Department Of Applied Biochemistry Hiroshima University
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Ikegami Susumu
Department Of Applied Biochemistry Faculty Of Applied Biological Science
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Shimonishi Y
Osaka Univ. Suita Jpn
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Nunomura Kazuto
Department Of Applied Biochemistry Hiroshima University
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Shimizu Takahiko
Department Of Aging Control Medicine Juntendo University Graduate School Of Medicine
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IKEGAMI Susumu
Department of Agricultural Chemistry, University of Tokyo
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