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Autor:
Govindjee, Archie R. Portis
Publikováno v:
Photosynthesis Research. 110:213-220
This News Report is a brief description of the 2010 Lifetime Achievement Award received by William (Bill) L. Ogren from the Rebeiz Foundation for Basic Research, at Champaign, Illinois, on Sep 10, 2011. It focuses mainly on the presentations by two o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87ca3c96dec7ec93bfcdaffff35583a5
https://doi.org/10.1007/s11120-011-9716-3
https://doi.org/10.1007/s11120-011-9716-3
Autor:
William L. Ogren
Publikováno v:
World Soybean Research Conference III: Proceedings ISBN: 9780429267932
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2f21cfe4b21bb89c9d29984c4876650
https://doi.org/10.1201/9780429267932-130
https://doi.org/10.1201/9780429267932-130
Autor:
Michael E. Salvucci, William L. Ogren
Publikováno v:
Photosynthesis Research. 47:1-11
Rubisco, the primary carboxylating enzyme in photosynthesis, must be activated to catalyze CO2 fixation. The concept of an 'activase', a specific protein for activating Rubisco, was first introduced in 1985 based largely on biochemical and genetic st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::599d06dd9b0062e0f030a87ebaa159a6
https://doi.org/10.1007/bf00017748
https://doi.org/10.1007/bf00017748
Autor:
William J. Campbell, William L. Ogren
Publikováno v:
Plant and Cell Physiology. 36:215-220
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d736305f37554a0396f6d64ace9b23df
https://doi.org/10.1093/oxfordjournals.pcp.a078752
https://doi.org/10.1093/oxfordjournals.pcp.a078752
Publikováno v:
Plant Physiology. 107:585-591
Photosynthesis rate, ribulsoe-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activation state, and ribulose bisphosphate concentration were reduced after exposing tomato (Lycopersicon esculentum Mill.) plants to light at 4[deg]C for 6 h. Analysis o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22296458cf8634052941ed6fcb707509
https://doi.org/10.1104/pp.107.2.585
https://doi.org/10.1104/pp.107.2.585
Autor:
William L. Ogren, Beverly M. Orozco
Publikováno v:
Plant Molecular Biology. 23:1129-1138
Deletions in the spinach rubisco activase (Rca) promoter in transgenic tobacco were analyzed to define the regions necessary for conferring light-inducible and tissue-specific expression. Transgenic plants were constructed with Bal 31 deletions of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a20fe0ebdb6bcd8b4573828def1f88b0
https://doi.org/10.1007/bf00042347
https://doi.org/10.1007/bf00042347
Publikováno v:
Plant Physiology. 100:1858-1862
Purified spinach (Spinacea oleracea L.) and barley (Hordeum vulgare L.) ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase supported 50 to 100% activation of substrate-bound Rubisco from spinach, barley, wheat (Triticum aestivum L.),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::255236a8d62bcf51193a6387e2e0bcd0
https://doi.org/10.1104/pp.100.4.1858
https://doi.org/10.1104/pp.100.4.1858
Publikováno v:
Plant Physiology. 98:1285-1289
Phosphoribulokinase (EC 2.7.1.19) was investigated in wild-type Chlamydomonas reinhardtii and in mutant strains deficient in this enzyme activity. Immunoblot analysis revealed substantial amounts of phosphoribulokinase in mutant 12-2B but none in mut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::579bc6ee778b91cb2a0f16b9672f6179
https://doi.org/10.1104/pp.98.4.1285
https://doi.org/10.1104/pp.98.4.1285
Autor:
Keith R. Roesler, William L. Ogren
Publikováno v:
Plant Physiology. 93:188-193
The sequence and kinetic properties of phosphoribulokinase purified from Chlamydomonas reinhardtii were determined and compared with the spinach (Spinacea oleracea) enzyme. Chlamydomonas phosphoribulokinase was purified to apparent homogeneity, with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::62e7f43d9dcfd6f204df25602a970234
https://doi.org/10.1104/pp.93.1.188
https://doi.org/10.1104/pp.93.1.188