Two SecG Molecules Present in a Single Protein Translocation Machinery Are Functional Even after Crosslinking
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概要
- 論文の詳細を見る
- Japanese Biochemical Societyの論文
- 2000-07-01
著者
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Tokuda H
Univ. Tokyo Tokyo
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Tokuda Hajime
Institute Of Molecular And Cellular Biosciences The University Of Tokyo
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NAGAMORI Shushi
Institute of Molecular and Cellular Biosciences, The University of Tokyo
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NISHIYAMA Ken-ichi
Institute of Molecular and Cellular Biosciences, The University of Tokyo
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Nishiyama Ken-ichi
Institute Of Molecular And Cellular Biosciences The University Of Tokyo
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Nishiyama Ken-ichi
Institute Of Geoscience University Of Tsukuba
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Nishiyama K
Institute Of Molecular And Cellular Biosciences The University Of Tokyo
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Nagamori Shushi
Institute Of Molecular And Cellular Biosciences The University Of Tokyo
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Tokuda Hajime
Institute at Molecular and Cellular Bioscience. The University of Tokyo
関連論文
- Membrane Topology Inversion of SecG Detected by Labeling with a Membrane-Impermeable Sulfhydryl Reagent that Causes a Close Association of SecG with SecA
- Two SecG Molecules Present in a Single Protein Translocation Machinery Are Functional Even after Crosslinking
- Role of the Non-essential Region Encompassing the N-Terminal Two Transmembrane Stretches of Escherichia coli SecE
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- Disruption of rpmJ Encoding Ribosomal Protein L36 Decreases the Expression of secY Upstream of the spc Operon and Inhibits Protein Translocation in Escherichia coli
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- Roles of the Conserved Cytoplasmic Region and No-Conserved Carboxy-Terminal Region of SecE in Escherichia coli Protein Translocase
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- Membrane Topology and Functional Importance of the Periplasmic Region of ABC Transporter LolCDE
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- Biogenesis of Outer Membranes in Gram-Negative Bacteria