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The Antibiotic Novobiocin Binds and Activates the ATPase That Powers Lipopolysaccharide Transport

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1016/j.febslet.2009.05.051openalex-snapshot
Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides
inferredcites →https://doi.org/10.1016/j.jmb.2008.04.045openalex-snapshot
Novel Structure of the Conserved Gram-Negative Lipopolysaccharide Transport Protein A and Mutagenesis Analysis
inferredcites →https://doi.org/10.1016/j.resmic.2005.11.014openalex-snapshot
Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG–yhbG locus
inferredcites →https://doi.org/10.1016/j.sbi.2007.07.003openalex-snapshot
Structure and mechanism of ABC transporter proteins
inferredcites →https://doi.org/10.1021/bi100493eopenalex-snapshot
Proteins Required for Lipopolysaccharide Assembly in Escherichia coli Form a Transenvelope Complex
inferredcites →https://doi.org/10.1021/bi300592copenalex-snapshot
Regulated Assembly of the Transenvelope Protein Complex Required for Lipopolysaccharide Export
inferredcites →https://doi.org/10.1021/cb600128vopenalex-snapshot
Probing the Barrier Function of the Outer Membrane with Chemical Conditionality
inferredcites →https://doi.org/10.1021/id500013topenalex-snapshot
A New-Class Antibacterial─Almost. Lessons in Drug Discovery and Development: A Critical Analysis of More than 50 Years of Effort toward ATPase Inhibitors of DNA Gyrase and Topoisomerase IV
inferredcites →https://doi.org/10.1038/nature13464openalex-snapshot
Structural basis for outer membrane lipopolysaccharide insertion
inferredcites →https://doi.org/10.1038/nature13484openalex-snapshot
Structural basis for lipopolysaccharide insertion in the bacterial outer membrane
inferredcites →https://doi.org/10.1038/nrmicro.2016.25openalex-snapshot
Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model
inferredcites →https://doi.org/10.1038/nsmb.3399openalex-snapshot
Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG
inferredcites →https://doi.org/10.1046/j.1365-2958.2002.03091.xopenalex-snapshot
Imp/OstA is required for cell envelope biogenesis in Escherichia coli
inferredcites →https://doi.org/10.1073/pnas.0402340101openalex-snapshot
Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface
inferredcites →https://doi.org/10.1073/pnas.0604744103openalex-snapshot
Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
inferredcites →https://doi.org/10.1073/pnas.0801196105openalex-snapshot
Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli
inferredcites →https://doi.org/10.1073/pnas.0912872107openalex-snapshot
Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane
inferredcites →https://doi.org/10.1073/pnas.1015617108openalex-snapshot
The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel
inferredcites →https://doi.org/10.1073/pnas.1209742109openalex-snapshot
Regulation of cell size in response to nutrient availability by fatty acid biosynthesis in Escherichia coli
inferredcites →https://doi.org/10.1073/pnas.1323516111openalex-snapshot
Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport
inferredcites →https://doi.org/10.1073/pnas.73.12.4474openalex-snapshot
Novobiocin and coumermycin inhibit DNA supercoiling catalyzed by DNA gyrase.
inferredcites →https://doi.org/10.1073/pnas.74.11.4772openalex-snapshot
Nalidixic acid resistance: A second genetic character involved in DNA gyrase activity
inferredcites →https://doi.org/10.1074/jbc.m110.144709openalex-snapshot
Structure and Functional Analysis of LptC, a Conserved Membrane Protein Involved in the Lipopolysaccharide Export Pathway in Escherichia coli*
inferredcites →https://doi.org/10.1074/jbc.m802503200openalex-snapshot
The LptA Protein of Escherichia coli Is a Periplasmic Lipid A-binding Protein Involved in the Lipopolysaccharide Export Pathway
inferredcites →https://doi.org/10.1101/cshperspect.a000414openalex-snapshot
The Bacterial Cell Envelope
inferredcites →https://doi.org/10.1126/science.1228984openalex-snapshot
Cytoplasmic ATP Hydrolysis Powers Transport of Lipopolysaccharide Across the Periplasm in E. coli
inferredcites →https://doi.org/10.1128/jb.00270-08openalex-snapshot
Functional Analysis of the Protein Machinery Required for Transport of Lipopolysaccharide to the Outer Membrane of Escherichia coli
inferredcites →https://doi.org/10.1128/jb.01037-10openalex-snapshot
New Insights into the Lpt Machinery for Lipopolysaccharide Transport to the Cell Surface: LptA-LptC Interaction and LptA Stability as Sensors of a Properly Assembled Transenvelope Complex
inferredcites →https://doi.org/10.1128/jb.01126-06openalex-snapshot
Characterization of lptA and lptB , Two Essential Genes Implicated in Lipopolysaccharide Transport to the Outer Membrane of Escherichia coli
inferredcites →https://doi.org/10.1128/mbio.01729-16openalex-snapshot
Identification of Residues in the Lipopolysaccharide ABC Transporter That Coordinate ATPase Activity with Extractor Function
inferredcites →https://doi.org/10.1128/mmbr.00031-07openalex-snapshot
Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems
inferredcites →https://doi.org/10.1128/mmbr.67.4.593-656.2003openalex-snapshot
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
inferredcites →https://doi.org/10.1146/annurev.biochem.71.110601.135414openalex-snapshot
Lipopolysaccharide Endotoxins
inferredcites →https://doi.org/10.1146/annurev.biochem.78.082907.145923openalex-snapshot
Multidrug Resistance in Bacteria

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Incoming claims: where this work appears in other papers’ reference lists and arguments.

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