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2. Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy. Walther TH, Grage SL, Roth N, Ulrich AS. J Am Chem Soc; 2010 Nov 17; 132(45):15945-56. PubMed ID: 20977272 [Abstract] [Full Text] [Related]
3. Two minimal Tat translocases in Bacillus. Jongbloed JD, Grieger U, Antelmann H, Hecker M, Nijland R, Bron S, van Dijl JM. Mol Microbiol; 2004 Dec 17; 54(5):1319-25. PubMed ID: 15554971 [Abstract] [Full Text] [Related]
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5. Structure analysis of the protein translocating channel TatA in membranes using a multi-construct approach. Lange C, Müller SD, Walther TH, Bürck J, Ulrich AS. Biochim Biophys Acta; 2007 Oct 21; 1768(10):2627-34. PubMed ID: 17669355 [Abstract] [Full Text] [Related]
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8. Contributions of the transmembrane domain and a key acidic motif to assembly and function of the TatA complex. Warren G, Oates J, Robinson C, Dixon AM. J Mol Biol; 2009 Apr 24; 388(1):122-32. PubMed ID: 19268473 [Abstract] [Full Text] [Related]
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10. Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin-arginine translocase. Barrett CM, Robinson C. FEBS J; 2005 May 26; 272(9):2261-75. PubMed ID: 15853811 [Abstract] [Full Text] [Related]
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