Author
Raymond A. Deems
Other affiliations:Â University of California
Bio: Raymond A. Deems is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Phospholipase A2 & Phospholipase. The author has an hindex of 28, co-authored 40 publications receiving 3127 citations. Previous affiliations of Raymond A. Deems include University of California.
Papers
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296Â citations
TL;DR: Results suggest that bicelles with low q retain the morphology and bilayer organization typical of their liquid-crystalline counterparts, making them useful membrane mimetics.
270Â citations
TL;DR: This kinetic treatment has made possible the quantitative separation of the association of a lipolytic enzyme with the lipid-water interface (expressed as KsA) and the binding to the substrate in the interface (reflected in the KmB term).
265Â citations
TL;DR: The lipidomic response of the murine macrophage RAW cell line to Kdo2-lipid A, the active component of an inflammatory lipopolysaccharide functioning as a selective TLR4 agonist and compactin, a statin inhibitor of cholesterol biosynthesis is reported.
251Â citations
TL;DR: A large-scale preparation of 3-deoxy-d-manno-octulosonic acid (Kdo)2-Lipid A, a nearly homogeneous Re lipopolysaccharide (LPS) sub-structure with endotoxin activity equal to LPS is reported.
223Â citations
Cited by
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1,952Â citations
1,422Â citations
TL;DR: This review updates the classification of the various PLA(2)'s now described in the literature, and expands or realignment of Groups VI, VII and VIII, as well as the addition of Group XIPLA(2) from plants.
1,308Â citations
TL;DR: This area will be the subject of this review, given that metabolic commitment is influenced not only by substrate availability but also by signaling pathways elicited by metabolites.
1,183Â citations
TL;DR: Diverse covalent modifications of the lipid A moiety may occur during its transit from the outer surface of the inner membrane to the outer membrane of most gram-negative bacteria.
Abstract: The lipid A moiety of lipopolysaccharide forms the outer monolayer of the outer membrane of most gram-negative bacteria. Escherichia coli lipid A is synthesized on the cytoplasmic surface of the inner membrane by a conserved pathway of nine constitutive enzymes. Following attachment of the core oligosaccharide, nascent core-lipid A is flipped to the outer surface of the inner membrane by the ABC transporter MsbA, where the O-antigen polymer is attached. Diverse covalent modifications of the lipid A moiety may occur during its transit from the outer surface of the inner membrane to the outer membrane. Lipid A modification enzymes are reporters for lipopolysaccharide trafficking within the bacterial envelope. Modification systems are variable and often regulated by environmental conditions. Although not required for growth, the modification enzymes modulate virulence of some gram-negative pathogens. Heterologous expression of lipid A modification enzymes may enable the development of new vaccines.
1,148Â citations