Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Richard G. Jensen"'
Publikováno v:
Acta Horticulturae. :177-184
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1401cc26cb21ceffb1d789b1edd3d0a3
https://doi.org/10.17660/actahortic.2000.527.21
https://doi.org/10.17660/actahortic.2000.527.21
Publikováno v:
Journal of Experimental Botany. 51:115-122
Transgenic tobacco (Nicotiana tabacum L, cv. SR-1) expressing mannitol 1-phosphate dehydrogenase, MTLD, in chloroplasts and myo-inositol O-methyltransferase, IMT1, in the cytosol after crossing of lines which expressed these foreign genes separately
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68e679d9ca4d0219ff7a64e7730dec23
https://doi.org/10.1093/jxb/51.342.115
https://doi.org/10.1093/jxb/51.342.115
Publikováno v:
Plant Physiology. 121:45-52
For many organisms there is a correlation between increases of metabolites and osmotic stress tolerance, but the mechanisms that cause this protection are not clear. To understand the role of polyols, genes for bacterial mannitol-1-P dehydrogenase an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9cffc8d2a2df5ba28007430cd985b0e5
https://doi.org/10.1104/pp.121.1.45
https://doi.org/10.1104/pp.121.1.45
Autor:
Abreeza Zegeer, Richard G. Jensen, Elena Sheveleva, Sheila Marquez, Wendy Chmara, Hans J. Bohnert
Publikováno v:
Plant Physiology. 117:831-839
We analyzed transgenic tobacco (Nicotiana tabacum L.) expressing Stpd1, a cDNA encoding sorbitol-6-phosphate dehydrogenase from apple, under the control of a cauliflower mosaic virus 35S promoter. In 125 independent transformants variable amounts of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a88096e99a79f9d5e414e424f1f4e6f2
https://doi.org/10.1104/pp.117.3.831
https://doi.org/10.1104/pp.117.3.831
Publikováno v:
Plant Physiology. 116:695-702
A cDNA of pea (Pisum sativum L.) RbcS 3A, encoding a small subunit protein (S) of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), has been expressed in Arabidopsis thalianaunder control of the cauliflower mosaic virus 35S promoter, and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8944a0c7acabe9609ab5557230eac06a
https://doi.org/10.1104/pp.116.2.695
https://doi.org/10.1104/pp.116.2.695
Autor:
Donald E. Nelson, Wendy Chmara, Patricia Adams, Hans J. Bohnert, Howard Griffiths, Richard G. Jensen, Shigehiro Yamada
Publikováno v:
New Phytologist. 138:171-190
This review describes the life cycle of Mesembryantheum crystallinum L. (the common ice plant, Aizoaceae, Caryophyllales), a halophyte with a developmentally programmed switch from C3 photosynthesis to Crassulacean acid metabolism (CAM) which is acce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fb0a72cdb3bdb418d78e26fe45ebbff
https://doi.org/10.1046/j.1469-8137.1998.00111.x
https://doi.org/10.1046/j.1469-8137.1998.00111.x
Publikováno v:
Photosynthesis Research. 57:71-79
Variations in length and charge of the C-terminus of the Rubisco large subunit (L) can be seen in L from different phylogenetic lineages. We examined the catalytic parameters of Rubisco from higher plants and from engineered Synechococcus rbcL in rel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12d185cffd49b8c27186aee78ab2ae50
https://doi.org/10.1023/a:1006020424581
https://doi.org/10.1023/a:1006020424581
Publikováno v:
Photosynthesis Research. 55:67-74
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) (EC 4.1.1.39) not only catalyzes carboxylation and oxygenation of ribulose-1,5-bisphosphate (RuBP), but it can also act either as an epimerase or isomerase converting RuBP into xylulose-1,5-bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef5e4c4c34205a0733d36799bd0c03d9
https://doi.org/10.1023/a:1005989012003
https://doi.org/10.1023/a:1005989012003
Publikováno v:
Plant Physiology. 114:131-136
The small subunit (S) increases the catalytic efficiency of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) by stabilizing the active sites generated by four large subunit (L) dimers. This stabilization appears to be due to an influence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ba608abc24929bff712ff7c3f7445c6
https://doi.org/10.1104/pp.114.1.131
https://doi.org/10.1104/pp.114.1.131
Autor:
Richard G. Jensen, Elena Sheveleva, Hans J. Bohnert, Bo Shen, Dortje Golldack, Manabu Ishitani, Uma R. Kamasani, Gerald Rammesmayer
Publikováno v:
Annals of the New York Academy of Sciences. 792:115-125
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb5e47da3ff3dbf187fb63b6444ae11e
https://doi.org/10.1111/j.1749-6632.1996.tb32498.x
https://doi.org/10.1111/j.1749-6632.1996.tb32498.x