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Sökning: WFRF:(Tomii Kentaro)

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1.
  • Imai, Kenichiro, et al. (författare)
  • Localization prediction and structure-based in silico analysis of bacterial proteins : with emphasis on outer membrane proteins.
  • 2013
  • Ingår i: Data Mining for Systems Biology. - New York : Humana Press. - 9781627031066 - 9781627031073 ; , s. 115-140
  • Bokkapitel (refereegranskat)abstract
    • In this chapter, we first discuss protein localization in bacteria and evaluate some localization prediction tools on an independent dataset. Next, we focus on β-barrel outer membrane proteins (BOMPs), describing and evaluating new tools for BOMP detection and topology prediction. Finally, we apply general protein structure prediction methods on these proteins to show that the structure of most BOMPs in E. coli can be modeled reliably.
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2.
  • Shiota, Takuya, et al. (författare)
  • Molecular architecture of the active mitochondrial protein gate
  • 2015
  • Ingår i: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 349:6255, s. 1544-1548
  • Tidskriftsartikel (refereegranskat)abstract
    • Mitochondria fulfill central functions in cellular energetics, metabolism, and signaling. The outer membrane translocator complex (the TOM complex) imports most mitochondrial proteins, but its architecture is unknown. Using a cross-linking approach, we mapped the active translocator down to single amino acid residues, revealing different transport paths for preproteins through the Tom40 channel. An N-terminal segment of Tom40 passes from the cytosol through the channel to recruit chaperones fromthe intermembrane space that guide the transfer of hydrophobic preproteins. The translocator contains three Tom40 beta-barrel channels sandwiched between a central alpha-helical Tom22 receptor cluster and external regulatory Tom proteins. The preprotein-translocating trimeric complex exchanges with a dimeric isoform to assemble new TOM complexes. Dynamic coupling of alpha-helical receptors, beta-barrel channels, and chaperones generates a versatile machinery that transports about 1000 different proteins.
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