Published in Mol Biol Cell on February 04, 2009
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Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported. EMBO J (2010) 1.05
Structural model for the protein-translocating element of the twin-arginine transport system. Proc Natl Acad Sci U S A (2013) 1.01
Escherichia coli TatA and TatB proteins have N-out, C-in topology in intact cells. J Biol Chem (2012) 0.98
Stoichiometry for binding and transport by the twin arginine translocation system. J Cell Biol (2012) 0.95
Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system. Proc Natl Acad Sci U S A (2013) 0.91
Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site. Mol Microbiol (2012) 0.91
Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells. PLoS One (2013) 0.91
Subunit organization in the TatA complex of the twin arginine protein translocase: a site-directed EPR spin labeling study. J Biol Chem (2009) 0.89
Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat). J Biol Chem (2015) 0.87
Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly. J Cell Biol (2014) 0.86
The chloroplast twin arginine transport (Tat) component, Tha4, undergoes conformational changes leading to Tat protein transport. J Biol Chem (2012) 0.85
Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes. Mol Microbiol (2012) 0.84
The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli. J Biol Chem (2012) 0.82
Salt sensitivity of minimal twin arginine translocases. J Biol Chem (2011) 0.82
The TatC component of the twin-arginine protein translocase functions as an obligate oligomer. Mol Microbiol (2015) 0.79
Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts. Plant Physiol (2012) 0.79
Ultrastructural characterisation of Bacillus subtilis TatA complexes suggests they are too small to form homooligomeric translocation pores. Biochim Biophys Acta (2013) 0.78
A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase. Proc Natl Acad Sci U S A (2017) 0.77
TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency. PLoS One (2015) 0.77
The canonical twin-arginine translocase components are not required for secretion of folded green fluorescent protein from the ancestral strain of Bacillus subtilis. Appl Environ Microbiol (2014) 0.76
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A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase. J Cell Biol (2002) 1.74
Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J Biol Chem (2005) 1.51
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Mapping the signal peptide binding and oligomer contact sites of the core subunit of the pea twin arginine protein translocase. Plant Cell (2013) 1.11
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