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810164P

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Direct Evidence for Requirement of Phosphatidylglycerol in Photosystem II of Photosynthesis
Hagio M, et al.
Plant Physiology null
Furong Zhang et al.
Langmuir : the ACS journal of surfaces and colloids, 36(11), 2946-2953 (2020-02-26)
Phospholipase A2 is an important enzyme species which can widely be found in animals, plants, bacteria, and so on. A large number of studies have shown that phospholipase A2 is highly catalytic toward the lipids. Here, sum frequency generation (SFG)...
Miki Hagio et al.
Plant & cell physiology, 43(12), 1456-1464 (2003-01-07)
Phosphatidylglycerol is a ubiquitous phospholipid in the biological membranes of many organisms. In plants, phosphatidylglycerol is mainly present in thylakoid membranes and has been suggested to play specific roles in photosynthesis. Here, we have isolated two T-DNA tagged lines of...
Phosphatidylglycerol is Essential for the Development of Thylakoid Membranes in Arabidopsis thaliana
Hagio M, et al.
Plant & Cell Physiology null
M Hagio et al.
Plant physiology, 124(2), 795-804 (2000-10-12)
Phosphatidylglycerol (PG) is considered to play an important role in the ordered assembly and structural maintenance of the photosynthetic apparatus in thylakoid membranes. However, its function in photosynthesis remains poorly understood. In this study we have identified a pgsA gene...
Separation of phospholipids in microfluidic chip device: application to high-throughput screening assays for lipid-modifying enzymes
Lin S, et al.
Analytical biochemistry null
Sansan Lin et al.
Analytical biochemistry, 314(1), 97-107 (2003-03-14)
Phospholipid molecules such as ceramide and phosphoinositides play crucial roles in signal transduction pathways. Lipid-modifying enzymes including sphingomyelinase and phosphoinositide kinases regulate the generation and degradation of these lipid-signaling molecules and are important therapeutic targets in drug discovery. We now...
Separation of phospholipids in microfluidic chip device: application to high-throughput screening assays for lipid-modifying enzymes
Lin S, et al.
Analytical Biochemistry null
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