M
Maoyin Li
Researcher at Donald Danforth Plant Science Center
Publications - 52
Citations - 5142
Maoyin Li is an academic researcher from Donald Danforth Plant Science Center. The author has contributed to research in topics: Arabidopsis & Phospholipase. The author has an hindex of 30, co-authored 49 publications receiving 4460 citations. Previous affiliations of Maoyin Li include University of North Texas & Kansas State University.
Papers
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Journal ArticleDOI
Profiling Membrane Lipids in Plant Stress Responses ROLE OF PHOSPHOLIPASE Dα IN FREEZING-INDUCED LIPID CHANGES IN ARABIDOPSIS
Ruth Welti,Weiqi Li,Maoyin Li,Yongming Sang,Homigol Biesiada,Han-E Zhou,C.B. Rajashekar,Todd D. Williams,Xuemin Wang +8 more
TL;DR: Data suggest that PC, rather than PE and PG, is the majorin vivo substrate of PLDα, and the greater loss of PC and increase in PA in wild-type plants as compared with PLD α-deficient plants may be responsible for destabilizing membrane bilayer structure.
Journal ArticleDOI
Phospholipase Dα1 and Phosphatidic Acid Regulate NADPH Oxidase Activity and Production of Reactive Oxygen Species in ABA-Mediated Stomatal Closure in Arabidopsis
Yanyan Zhang,Huiying Zhu,Qun Zhang,Maoyin Li,Maoyin Li,Min Yan,Rong Wang,Liling Wang,Ruth Welti,Wenhua Zhang,Xuemin Wang,Xuemin Wang +11 more
TL;DR: PA is as a central lipid signaling molecule that links different components in the ABA signaling network in guard cells that is required for stomatal closure induced by ABA, H2O2, or NO.
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The plasma membrane-bound phospholipase Dδ enhances freezing tolerance in Arabidopsis thaliana
TL;DR: It is shown that freezing tolerance can be manipulated in Arabidopsis thaliana by genetic alteration of the gene encoding phospholipase Dδ (PLDδ), which is involved in membrane lipid hydrolysis and cell signaling, and that the PLD pathway is a unique determinant of the response to freezing.
Journal ArticleDOI
Quantitative profiling of polar glycerolipid species from organs of wild-type Arabidopsis and a PHOSPHOLIPASE Dα1 knockout mutant
Shivakumar P. Devaiah,Mary R. Roth,Ethan Baughman,Maoyin Li,Pamela Tamura,Richard Jeannotte,Ruth Welti,Xuemin Wang +7 more
TL;DR: Comparison between wild-type and a knockout mutant pldalpha1 (locus ID: AT3G15730) provides insight into the metabolic function of phospholipase D (PLD) in different organs, suggesting a role for PLDalpha1 in membrane lipid degradation in seeds.
Journal ArticleDOI
Phospholipase D- and phosphatidic acid-mediated signaling in plants.
TL;DR: Improved knowledge on the mechanism by which specific PLDs and PA mediate given plant responses will facilitate the understanding of the molecular processes that connect the stimulus perception on membranes to intracellular actions and physiological responses.