Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Twin-arginine transport"'
Autor:
Isabel Guerrero Montero, Katarzyna Magdalena Dolata, Rabea Schlüter, Gilles Malherbe, Susanne Sievers, Daniela Zühlke, Thomas Sura, Emma Dave, Katharina Riedel, Colin Robinson
Publikováno v:
Microbial Cell Factories, Vol 18, Iss 1, Pp 1-15 (2019)
Abstract Background The Twin-arginine translocation (Tat) pathway of Escherichia coli has great potential for the export of biopharmaceuticals to the periplasm due to its ability to transport folded proteins, and its proofreading mechanism that allow
Externí odkaz:
https://doaj.org/article/399c3e37f4cd4ef5837d604c5b84ca95
Autor:
Maillard, Julien, Spronk, Chris A. E. M., Buchanan, Grant, Lyall, Verity, Richardson, David J., Palmer, Tracy, Vuister, Geerten W., Sargent, Frank
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2007 Oct 01. 104(40), 15641-15646.
Externí odkaz:
https://www.jstor.org/stable/25449192
Autor:
Eudy, Kathryn E.
The Twin-Arginine Transport (TAT) system is used in prokaryotes as well as eukaryotic chloroplasts to transport folded proteins across membranes. Recently, proteins homologous to TAT system component proteins have been discovered in the mitochondria.
Autor:
Susanne Sievers, Daniela Zühlke, Thomas Sura, Katharina Riedel, Colin Robinson, Gilles Malherbe, Emma Dave, Rabea Schlüter, Katarzyna Magdalena Dolata, Isabel Guerrero Montero
Publikováno v:
Microbial Cell Factories, Vol 18, Iss 1, Pp 1-15 (2019)
Microbial Cell Factories
Microbial Cell Factories
Background The Twin-arginine translocation (Tat) pathway of Escherichia coli has great potential for the export of biopharmaceuticals to the periplasm due to its ability to transport folded proteins, and its proofreading mechanism that allows correct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0905b1f3f73a1ac1933d58e44964f850
http://link.springer.com/article/10.1186/s12934-019-1071-7
http://link.springer.com/article/10.1186/s12934-019-1071-7
Autor:
New, Christopher Paul
The chloroplast Twin Arginine Translocase (cpTAT) system transports fully folded proteins across the thylakoid membrane in plant cells using only energy derived from the proton motive force (PMF). Three membrane bound component proteins: cpTatC, Hcf1
Publikováno v:
Plant Direct
The chloroplast twin arginine transport (cpTat) system distinguishes itself as a protein transport pathway by translocating fully folded proteins, using the proton‐motive force (PMF) as the sole source of energy. The cpTat pathway is evolutionarily
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::037435d89313bf181e911e77a11f0364
http://europepmc.org/articles/PMC6508782
http://europepmc.org/articles/PMC6508782
The chloroplast Twin arginine transport (cpTat) system transports folded proteins across the thylakoids in chloroplast using proton motive force as the only source of energy. The cpTat is composed of three components; Tha4, Hcf106, and cpTatC. Hcf106
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1838:413-418
The chloroplast twin arginine translocation (cpTat) system transports highly folded precursor proteins into the thylakoid lumen using the protonmotive force as its only energy source. Hcf106, as one of the core components of the cpTat system, is part
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::076eedfe39c6739042212c9b12dee8d4
https://doi.org/10.1016/j.bbamem.2013.10.007
https://doi.org/10.1016/j.bbamem.2013.10.007
Autor:
Philip N. Rather
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1828:2849-2854
The first member of the rhomboid family of intramembrane serine proteases in bacteria was discovered almost 20 years ago. It is now known that rhomboid proteins are widely distributed in bacteria, with some bacteria containing multiple rhomboids. At
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d186084cab15dc2323501f0774153ef
https://doi.org/10.1016/j.bbamem.2013.03.012
https://doi.org/10.1016/j.bbamem.2013.03.012
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