Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Shinsuke Sakuma"'
Autor:
Yuka Tomokawa, Shinsuke Sakuma, Noriaki Tamura, Jian Ren Shen, Yasusi Yamamoto, Hitoshi Yamasaki, Takahiro Henmi
Publikováno v:
Plant and Cell Physiology. 44:451-456
During the donor-side photoinhibition of spinach photosystem II, the reaction center D1 protein cross-linked with the antenna chlorophyll binding protein CP43 of photosystem II lacking the oxygen-evolving complex (OEC) subunit proteins. The cross-lin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15e308c61cb55206132e0908c0687da8
https://doi.org/10.1093/pcp/pcg049
https://doi.org/10.1093/pcp/pcg049
Publikováno v:
Simulating Interacting Agents and Social Phenomena ISBN: 9784431997801
WCSS
WCSS
This paper examines effective knowledge-retrieval heuristics in terms of transactive memory in concurrent software development teams. We propose six knowledge-retrieval heuristics and evaluate their effectiveness in four typical situations encountere
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::015787b2cc5ca98cde3ae6f9a34e7dd9
https://doi.org/10.1007/978-4-431-99781-8_11
https://doi.org/10.1007/978-4-431-99781-8_11
Publikováno v:
Methods in Molecular Biology ISBN: 9781607619246
Methods for the isolation of highly active oxygen-evolving photosystem (PS)II membranes from higher plants and the purification of the oxygen-evolving complex (OEC) subunits are described. Membrane samples used as the material for various in vitro st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3061e2c0098ae2c4f1a9908112f1719f
https://doi.org/10.1385/1-59259-799-8:029
https://doi.org/10.1385/1-59259-799-8:029
Autor:
Cui-Yan, Tan, Chun-He, Xu, Jun-Ren, Shen, Shinsuke, Sakuma, Yasushi, Yamamoto, Claude, Balny, Kang-Cheng, Ruan
Publikováno v:
Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica. 35(7)
The unfolding of 23kD (P23k) protein isolated from spinach photosystem II particle was studied by high pressure and fluorescence spectroscopy. The thermal equilibrium study indicated that the protein could be totally unfolded by 180 or 160 MPa at 20
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::017ad70124e92ee78e692a47328e2173
https://pubmed.ncbi.nlm.nih.gov/12883641
https://pubmed.ncbi.nlm.nih.gov/12883641