L
Luyan Ma
Researcher at Wake Forest University
Publications - 8
Citations - 1227
Luyan Ma is an academic researcher from Wake Forest University. The author has contributed to research in topics: Azospirillum brasilense & Biofilm. The author has an hindex of 5, co-authored 8 publications receiving 1100 citations. Previous affiliations of Luyan Ma include China Agricultural University.
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Journal ArticleDOI
Assembly and development of the Pseudomonas aeruginosa biofilm matrix.
TL;DR: Direct visualization reveals that Psl is a key scaffolding matrix component and opens up avenues for therapeutics of biofilm-related complications.
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Analysis of Pseudomonas aeruginosa Conditional Psl Variants Reveals Roles for the Psl Polysaccharide in Adhesion and Maintaining Biofilm Structure Postattachment
TL;DR: Analysis of biofilms formed by the Deltapsl/p(BAD)-psl strain indicated that expression of the psl operon is required to maintain the biofilm structure at steps postattachment, which is critical for initiation and maintenance of theBiofilm structure.
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Pseudomonas aeruginosa Psl Is a Galactose- and Mannose-Rich Exopolysaccharide
TL;DR: Chemical composition analyses and mannose- or galactose-specific lectin staining are used, followed by confocal laser scanning microscopy and electron microscopy, to show that Psl is a galactOSE-rich and manNose-rich exopolysaccharide.
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Control of bacterial biofilms with marine alkaloid derivatives.
Robert W. Huigens,Luyan Ma,Christopher Gambino,Peter D. R. Moeller,Anne Basso,John Cavanagh,Daniel J. Wozniak,Christian Melander +7 more
TL;DR: It is demonstrated that TAGE does not have selective toxicity against cells within the biofilm state, will inhibit biofilm development under flow conditions, indicating that the CV staining protocol correlates with the ability to be active under biomimetic conditions, and will disperse preformed P. aeruginosa biofilms.
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Mapping the MinE Site Involved in Interaction with the MinD Division Site Selection Protein of Escherichia coli
TL;DR: The site within MinE that is required for interaction with MinD was mapped by studying the effects of site-directed minE mutations on MinD-MinE interactions in yeast two-hybrids and three-hybrid experiments, confirming that the MinE N-terminal domain is responsible for the interaction of MinE with Min D.