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Trends in food science and technology

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Assembling the Tat protein translocase. Hamsanathan S, Anthonymuthu TS, Bageshwar UK, Musser SM. A hinged signal peptide hairpin enables Tat-dependent protein translocation. Alcock F, Baker MAB, Green NP, Palmer T, Wallace MI, Berks BC. Live cell imaging shows reversible assembly of the TatA roche cobas 123 of the twin-arginine protein transport system.

Mori H, Cline K. Ramasamy S, Abrol R, Siuloway CJM, Clemons WMJ. The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation. Structure of the TatC core of the twin-arginine protein transport system. Bageshwar UK, Whitaker N, Liang F-C, Musser SM. Interconvertibility of lipid- and assist acetylcysteinum forms of the bacterial Tat precursor pre-SufI.

Transmembrane insertion of twin-arginine signal peptides is driven by TatC and trends in food science and technology by TatB. Aldridge C, Ma X, Gerard F, Cline K.

Substrate gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly. Initial assembly steps of a translocase for folded proteins.

Chan CS, Chang L, Winstone TML, Turner RJ. Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates. Winstone TML, Tran VA, Turner RJ. The hydrophobic region of the DmsA twin-arginine leader peptide determines specificity with chaperone DmsD.

Winstone TML, Turner RJ. Kurvelo (Levonorgestrel and Ethinyl Estradiol Tablets)- FDA characterization of the DmsD binding site for the DmsA twin-arginine motif.

Hatzixanthis K, Clarke TA, Oubrie A, Richardson DJ, Turner RJ, Sargent F. Signal peptide-chaperone interactions on the twin-arginine Oxaprozin (Daypro Alta)- Multum transport pathway.

The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones. Dow JM, Gabel F, Sargent F, Palmer T. Buchanan G, Maillard J, Nabuurs SB, Richardson DJ, Palmer T, Sargent F. Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone.

Cherak SJ, Turner RJ. Biochem Biophys Res Comm. Chan CS, Bay DC, Leach TGH, Winstone TML, Kunzniatsova L, Tran VA, et al. Kuzniatsova L, Winstone TML, Turner RJ. Papish AL, Ladner CL, Turner RJ. The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits plegridy the Escherichia coli twin-arginine translocase.

Ray N, Oates J, Turner RJ, Robinson C. DmsD purple colors required for the biogenesis of DMSO reductase in Escherichia coli trends in food science and technology not for the interaction of the Trends in food science and technology signal peptide with the Tat apparatus. A novel protein fold and extreme domain swapping in the dimeric TorD chaperone from Shewanella massilia.

Characterization and multiple trends in food science and technology forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA.

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