Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Mikael Zoryan"'
Publikováno v:
Analytical Biochemistry. 383:279-288
Photosystem II is a multimeric protein complex of the thylakoid membrane in chloroplasts. Approximately half of the at least 26 different integral membrane protein subunits have molecular masses lower than 10 kDa. After one-dimensional (1D) or two-di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b815a0d1cf070f8adc55a421d8d14350
https://doi.org/10.1016/j.ab.2008.08.038
https://doi.org/10.1016/j.ab.2008.08.038
Autor:
Lada Mlcòchová, Cristina Dal Bosco, Reinhold G. Herrmann, Jörg Meurer, Mikael Zoryan, Stefanie M. Volz, Lutz A. Eichacker, Serena Schwenkert, Itzhak Ohad, Pavan Umate
Publikováno v:
Journal of Biological Chemistry. 281:34227-34238
Photosystem II (PSII) core complexes consist of CP47, CP43, D1, D2 proteins and of several low molecular weight integral membrane polypeptides, such as the chloroplast-encoded PsbE, PsbF, and PsbI proteins. To elucidate the function of PsbI in the ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b73a7e7cbe70a7fb9ec4280ca71ebff
https://doi.org/10.1074/jbc.m604888200
https://doi.org/10.1074/jbc.m604888200
Publikováno v:
Proteomics. 9(3)
In Photosystem II (PSII), a high number of plastid encoded and membrane integral low molecular weight proteins smaller than 10 kDa, the proteins PsbE, F, H, I, J, K, L, M, N, Tc, Z and the nuclear encoded PsbW, X, Y1, Y2 proteins have been described.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cef38fb953c7f5123e32d01cbd2a401
https://pubmed.ncbi.nlm.nih.gov/19137553
https://pubmed.ncbi.nlm.nih.gov/19137553
Autor:
Uwe G. Maier, Mislav Oreb, Enrico Schleiff, Lutz A. Eichacker, Mikael Zoryan, Aleksandar Vojta
Publikováno v:
FEBS Letters. (30):5945-5951
The precursor protein receptor at the chloroplast outer membrane atToc33 is a GTPase, which can be inactivated by phosphorylation in vitro, being arrested in the GDP loaded state. To assess the physiological function of phosphorylation, attoc33 knock
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f344cac7a48449ca237ab576e7afbef
Publikováno v:
Proteomics; Feb2009, Vol. 9 Issue 3, pn/a-n/a, 4p