The Chloroplast Tat Pathway Transports Substrates in the Dark
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference51 articles.
1. Sec-Independent Protein Translocation by the Maize Hcf106 Protein
2. The Maize tha4 Gene Functions in Sec-Independent Protein Transport in Chloroplasts and Is Related to hcf106, tatA, and tatB
3. Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport
4. TatB and TatC Form a Functional and Structural Unit of the Twin-arginine Translocase from Escherichia coli
5. Characterisation of Tat protein transport complexes carrying inactivating mutations
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1. Membrane Chaperoning of a Thylakoid Protease Whose Structural Stability Is Modified by the Protonmotive Force;The Plant Cell;2020-03-13
2. Lipid Chaperoning of a Thylakoid Protease Whose Stability is Modified by the Protonmotive Force;2019-10-02
3. Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway;Photosynthesis Research;2018-08-12
4. The Role of Light–Dark Regulation of the Chloroplast ATP Synthase;Frontiers in Plant Science;2017-07-24
5. The Twin-Arginine Protein Translocation Pathway;Annual Review of Biochemistry;2015-06-02
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