@article{petersson_prx_2006,
	title = {The {Prx} {Q} protein of {Arabidopsis} thaliana is a member of the luminal chloroplast proteome},
	volume = {580},
	copyright = {FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies},
	issn = {1873-3468},
	url = {https://febs.onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2006.10.001},
	doi = {10.1016/j.febslet.2006.10.001},
	abstract = {Peroxiredoxins have been discovered in many organisms ranging from eubacteria to mammals, and their known biological functions include both oxidant defense and signal transduction. The genome of Arabidopsis thaliana encodes for ten individual peroxiredoxins, of which four are located in the chloroplast. The best-characterized member of the chloroplast peroxiredoxins is 2-Cys Prx that is associated with the stroma side of the thylakoid membrane and is considered to participate in antioxidant defense and protection of photosynthesis. This study addressed the chloroplast peroxiredoxin Prx Q and showed that its subcellular location is the lumen of the thylakoid membrane. To get insight in the biological function of the Prx Q protein of Arabidopsis, the protein levels of the Prx Q protein in thylakoid membranes were studied under different light conditions and oxidative stress. A T-DNA knockout mutant of Prx Q did not show any visible phenotype and had normal photosynthetic performance with a slightly increased oxygen evolving activity.},
	language = {en},
	number = {26},
	urldate = {2021-06-11},
	journal = {FEBS Letters},
	author = {Petersson, Ulrika A. and Kieselbach, Thomas and García-Cerdán, José G. and Schröder, Wolfgang P.},
	year = {2006},
	note = {\_eprint: https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2006.10.001},
	keywords = {PSII, Peroxiredoxin, Photosynthesis},
	pages = {6055--6061},
}

{"_id":"pwv2LE7Fah8uTm4e5","bibbaseid":"petersson-kieselbach-garcacerdn-schrder-theprxqproteinofarabidopsisthalianaisamemberoftheluminalchloroplastproteome-2006","author_short":["Petersson, U. A.","Kieselbach, T.","García-Cerdán, J. G.","Schröder, W. P."],"bibdata":{"bibtype":"article","type":"article","title":"The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome","volume":"580","copyright":"FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies","issn":"1873-3468","url":"https://febs.onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2006.10.001","doi":"10.1016/j.febslet.2006.10.001","abstract":"Peroxiredoxins have been discovered in many organisms ranging from eubacteria to mammals, and their known biological functions include both oxidant defense and signal transduction. The genome of Arabidopsis thaliana encodes for ten individual peroxiredoxins, of which four are located in the chloroplast. The best-characterized member of the chloroplast peroxiredoxins is 2-Cys Prx that is associated with the stroma side of the thylakoid membrane and is considered to participate in antioxidant defense and protection of photosynthesis. This study addressed the chloroplast peroxiredoxin Prx Q and showed that its subcellular location is the lumen of the thylakoid membrane. To get insight in the biological function of the Prx Q protein of Arabidopsis, the protein levels of the Prx Q protein in thylakoid membranes were studied under different light conditions and oxidative stress. A T-DNA knockout mutant of Prx Q did not show any visible phenotype and had normal photosynthetic performance with a slightly increased oxygen evolving activity.","language":"en","number":"26","urldate":"2021-06-11","journal":"FEBS Letters","author":[{"propositions":[],"lastnames":["Petersson"],"firstnames":["Ulrika","A."],"suffixes":[]},{"propositions":[],"lastnames":["Kieselbach"],"firstnames":["Thomas"],"suffixes":[]},{"propositions":[],"lastnames":["García-Cerdán"],"firstnames":["José","G."],"suffixes":[]},{"propositions":[],"lastnames":["Schröder"],"firstnames":["Wolfgang","P."],"suffixes":[]}],"year":"2006","note":"_eprint: https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2006.10.001","keywords":"PSII, Peroxiredoxin, Photosynthesis","pages":"6055–6061","bibtex":"@article{petersson_prx_2006,\n\ttitle = {The {Prx} {Q} protein of {Arabidopsis} thaliana is a member of the luminal chloroplast proteome},\n\tvolume = {580},\n\tcopyright = {FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies},\n\tissn = {1873-3468},\n\turl = {https://febs.onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2006.10.001},\n\tdoi = {10.1016/j.febslet.2006.10.001},\n\tabstract = {Peroxiredoxins have been discovered in many organisms ranging from eubacteria to mammals, and their known biological functions include both oxidant defense and signal transduction. The genome of Arabidopsis thaliana encodes for ten individual peroxiredoxins, of which four are located in the chloroplast. The best-characterized member of the chloroplast peroxiredoxins is 2-Cys Prx that is associated with the stroma side of the thylakoid membrane and is considered to participate in antioxidant defense and protection of photosynthesis. This study addressed the chloroplast peroxiredoxin Prx Q and showed that its subcellular location is the lumen of the thylakoid membrane. To get insight in the biological function of the Prx Q protein of Arabidopsis, the protein levels of the Prx Q protein in thylakoid membranes were studied under different light conditions and oxidative stress. A T-DNA knockout mutant of Prx Q did not show any visible phenotype and had normal photosynthetic performance with a slightly increased oxygen evolving activity.},\n\tlanguage = {en},\n\tnumber = {26},\n\turldate = {2021-06-11},\n\tjournal = {FEBS Letters},\n\tauthor = {Petersson, Ulrika A. and Kieselbach, Thomas and García-Cerdán, José G. and Schröder, Wolfgang P.},\n\tyear = {2006},\n\tnote = {\\_eprint: https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2006.10.001},\n\tkeywords = {PSII, Peroxiredoxin, Photosynthesis},\n\tpages = {6055--6061},\n}\n\n\n\n","author_short":["Petersson, U. A.","Kieselbach, T.","García-Cerdán, J. G.","Schröder, W. P."],"key":"petersson_prx_2006","id":"petersson_prx_2006","bibbaseid":"petersson-kieselbach-garcacerdn-schrder-theprxqproteinofarabidopsisthalianaisamemberoftheluminalchloroplastproteome-2006","role":"author","urls":{"Paper":"https://febs.onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2006.10.001"},"keyword":["PSII","Peroxiredoxin","Photosynthesis"],"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/zotero/upscpub","dataSources":["9cGcv2t8pRzC92kzs","fvfkWcShg3Mybjoog","Tu3jPdZyJF3j547xT","3zTPPmKj8BiTcpc6C"],"keywords":["psii","peroxiredoxin","photosynthesis"],"search_terms":["prx","protein","arabidopsis","thaliana","member","luminal","chloroplast","proteome","petersson","kieselbach","garcía-cerdán","schröder"],"title":"The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome","year":2006}