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Journal Abstract Search

156 related items for PubMed ID: 19013157

  • 1. Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone.
    Buchanan G, Maillard J, Nabuurs SB, Richardson DJ, Palmer T, Sargent F.
    FEBS Lett; 2008 Dec 10; 582(29):3979-84. PubMed ID: 19013157
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  • 2. Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping.
    Guymer D, Maillard J, Agacan MF, Brearley CA, Sargent F.
    FEBS J; 2010 Jan 10; 277(2):511-25. PubMed ID: 20064164
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  • 6. The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.
    Ulfig A, Fröbel J, Lausberg F, Blümmel AS, Heide AK, Müller M, Freudl R.
    J Biol Chem; 2017 Jun 30; 292(26):10865-10882. PubMed ID: 28515319
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  • 7. A genetic screen for suppressors of Escherichia coli Tat signal peptide mutations establishes a critical role for the second arginine within the twin-arginine motif.
    Buchanan G, Sargent F, Berks BC, Palmer T.
    Arch Microbiol; 2001 Dec 30; 177(1):107-12. PubMed ID: 11797051
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  • 9. Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.
    Bageshwar UK, DattaGupta A, Musser SM.
    PLoS One; 2021 Dec 30; 16(9):e0256715. PubMed ID: 34499687
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  • 10. The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding.
    Ulfig A, Freudl R.
    J Biol Chem; 2018 May 11; 293(19):7281-7299. PubMed ID: 29593092
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  • 12. Coordinating assembly and export of complex bacterial proteins.
    Jack RL, Buchanan G, Dubini A, Hatzixanthis K, Palmer T, Sargent F.
    EMBO J; 2004 Oct 13; 23(20):3962-72. PubMed ID: 15385959
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  • 13. Structural diversity in twin-arginine signal peptide-binding proteins.
    Maillard J, Spronk CA, Buchanan G, Lyall V, Richardson DJ, Palmer T, Vuister GW, Sargent F.
    Proc Natl Acad Sci U S A; 2007 Oct 02; 104(40):15641-6. PubMed ID: 17901208
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  • 14. The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones.
    Shanmugham A, Bakayan A, Völler P, Grosveld J, Lill H, Bollen YJ.
    PLoS One; 2012 Oct 02; 7(3):e34159. PubMed ID: 22479549
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  • 15. Specific inhibition of the translocation of a subset of Escherichia coli TAT substrates by the TorA signal peptide.
    Chanal A, Santini CL, Wu LF.
    J Mol Biol; 2003 Mar 28; 327(3):563-70. PubMed ID: 12634052
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  • 16. An essential role for the DnaK molecular chaperone in stabilizing over-expressed substrate proteins of the bacterial twin-arginine translocation pathway.
    Pérez-Rodríguez R, Fisher AC, Perlmutter JD, Hicks MG, Chanal A, Santini CL, Wu LF, Palmer T, DeLisa MP.
    J Mol Biol; 2007 Mar 30; 367(3):715-30. PubMed ID: 17280684
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  • 17. TorD, a cytoplasmic chaperone that interacts with the unfolded trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli.
    Pommier J, Méjean V, Giordano G, Iobbi-Nivol C.
    J Biol Chem; 1998 Jun 26; 273(26):16615-20. PubMed ID: 9632735
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  • 18. Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains.
    Ize B, Coulthurst SJ, Hatzixanthis K, Caldelari I, Buchanan G, Barclay EC, Richardson DJ, Palmer T, Sargent F.
    Microbiology (Reading); 2009 Dec 26; 155(Pt 12):3992-4004. PubMed ID: 19778964
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  • 19. A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase.
    Hatzixanthis K, Palmer T, Sargent F.
    Mol Microbiol; 2003 Sep 26; 49(5):1377-90. PubMed ID: 12940994
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  • 20. Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase.
    Huang Q, Palmer T.
    mBio; 2017 Aug 01; 8(4):. PubMed ID: 28765221
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