Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A
Author:
Funder
Institute for Translational Vaccinology
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference34 articles.
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4. Hydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases;Wyckoff;J. Biol. Chem,1998
5. Structures of Pseudomonas aeruginosa LpxA reveal the basis for its substrate selectivity;Smith;Biochemistry,2015
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1. A comprehensive review of recent developments in the gram-negative bacterial UDP-2,3-diacylglucosamine hydrolase (LpxH) enzyme;International Journal of Biological Macromolecules;2024-05
2. Activation of Canine, Mouse and Human TLR2 and TLR4 by Inactivated Leptospira Vaccine Strains;Frontiers in Immunology;2022-03-21
3. Nanoflow LC–MS Method Allowing In-Depth Characterization of Natural Heterogeneity of Complex Bacterial Lipopolysaccharides;Analytical Chemistry;2021-11-22
4. Variation, Modification and Engineering of Lipid A in Endotoxin of Gram-Negative Bacteria;International Journal of Molecular Sciences;2021-02-25
5. Shortening the Lipid A Acyl Chains of Bordetella pertussis Enables Depletion of Lipopolysaccharide Endotoxic Activity;Vaccines;2020-10-09
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