Session 02 Hormone metabolism and action

Autor: A. J. Boyd, S. M. Wahrlich, P. R. Poole, P. Brabcová, V. Čapková, J. LuŠtinec, A. Březinová, V. Motyka, C. Auer, J. Holík, M. Kamínek, Z. Burdach, W. Karcz, N. Chauvaux, L. Poduje, R. Child, H. Onckelen, G. N. Cherepneva, J. A. Dieleman, D. Kuiper, S. D. Dimova-Terziivanova, T. D. Tsonev, D. N. Terziivanov, F. A. Gudumak, A. I. Derendovskaya, R. D. Hammerton, B. Nicander, E. Tillberg, J. Holub, G. Ievinsh, O. Kreicbergs, T. Iturriagatoitia-Bueno, P. John, M. Kovač, M. Ravnikar, R. Kurtyka, J. Stolarek, V. V. Kuznetsov, R. Oelmuller, R. G. Herrmann, O. N. Kulaeva, J. Lehmann, R. Atzorn, J. Leopold, C. Wasternack, B. Parthier, L. A. Lutova, I. S. Buzovkina, S. O. Shishkova, O. N. Tikhodeev, A. Yu. Makoveychuk, E. Malkowski, R. Martinez, M. Parra, D. Valero, A. I. M. Gomes, M. A. Moya-Leon, L. I. Musatenko, A. A. Padun, A. R. Mustafina, G. R. Kudoyarova, L. V. Nazarenko, V. E. Semenenko, V. Ördög, Z. Molnár, A. Pastor, L. Alegre, V. -P. Pelkonen, A. Kauppi, O. Junttila, R. Reski, S. Kruse, B. Kasten, K. Reutter, M. Wehe, M. Faust, G. Gorr, W. O. Abel, I. Rukasz, T. Schmülling, M. Faiss, M. Strnad, C. Gatz, Gernot Schneider, O. P. Serdyuk, L. D. Smolygna, T. V. Laurinavichene, A. A. Tsyganskov, F. M. Shakirova, M. V. Bezrukova, L. D. Smolygina, R. Stikic, S. Pekic, W. J. Davies, S. A. Quarrie, L. Tomljanovic, Z. Jovanovic, P. Redig, J. Hanus, V. Dongen, M. Szabó, S. E. Köves, I. Stefanov, J. Molnár, M. D. Titika, V. A. Vasjuk, T. V. Andrianova, C. Vuylsteker, B. Palms, O. Leleu, S. Rambour, Y. Z. Wang, M. D. Cramer, A. Schierholt, S. H. Lips, E. Zažímalová, W. Zhong, W. Hartung, C. Schobert, E. Komor

Publikováno v: Biologia plantarum. 36:S21-S43

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d46506c853d62b6f65286c0d1ef203f3
https://doi.org/10.1007/bf02931114

[Role of hydrogenases 1 and 2 in the hydrogen dependent nitrate respiration by Escherichia coli]

Autor: T V, Laurinavichene, A A, Tsygankov

Publikováno v: Mikrobiologiia. 72(6)

The study of Escherichia coli mutants synthesizing either hydrogenase 1 (HDK203) or hydrogenase 2 (HDK103) showed that the nitrate-dependent uptake of hydrogen by E. coli cells can be accomplished through the action of either of these hydrogenases. T

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c530407c566e2ea80df44bc7570ec48a
https://pubmed.ncbi.nlm.nih.gov/14768538

Regulation of nitrogenase in the photosynthetic bacterium Rhodobacter sphaeroides containing draTG and nifHDK genes from Rhodobacter capsulatus

Autor: A F, Yakunin, A S, Fedorov, T V, Laurinavichene, V M, Glaser, N S, Egorov, A A, Tsygankov, V V, Zinchenko, P C, Hallenbeck

Publikováno v: Canadian journal of microbiology. 47(3)

The photosynthetic bacteria Rhodobacter capsulatus and Rhodospirillum rubrum regulate their nitrogenase activity by the reversible ADP-ribosylation of nitrogenase Fe-protein in response to ammonium addition or darkness. This regulation is mediated by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::efd70d2f45de406804feee3908b4eb80
https://pubmed.ncbi.nlm.nih.gov/11315111

[Role of ferredoxin in the metabolism of hydrogen by Rhodospirillum rubrum]

Autor: I N, Gogotov, T V, Laurinavichene

Publikováno v: Mikrobiologiia. 44(4)

Ferredoxin was purified after isolation from the cells of Rhodospirillum rubrum grown under photoheterotrophic conditions; A385/A280 in the absorption spectrum was not less than 0.53; the molecular weight was ca. 7700; E0' (pH 7.0)--430 mv. Ferredoxi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::641497844d85cd76388bca1f14125055
https://pubmed.ncbi.nlm.nih.gov/241001

[Low potential c-type cytochrome of Thiocapsa roseopersicina]

Autor: O F, Korsunskiĭ, L D, Smolygina, T V, Laurinavichene, I N, Gogotov

Publikováno v: Biokhimiia (Moscow, Russia). 47(3)

The low potential c-type cytochrome from the phototrophic purple sulphur bacterium Thiocapsa roseopersicina, strain BBS was isolated in electrophoretically homogeneous state. The bulk of the cytochrome (approximately 90%) after disruption of the cell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a882a4a7c7d8ba9490b74b0c3094ae6c
https://pubmed.ncbi.nlm.nih.gov/6280782