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Translocation of Phospholipids Is Facilitated by a Subset of Membrane-spanning Proteins of the Bacterial Cytoplasmic Membrane
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1 of the 41 references listed on this page is in the Retraction Watch database as retracted (export 2026-11-04): 10.1126/science.293.5536.1793 (notice 2006-12-22).
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/j.1460-2075.1989.tb03618.xopenalex-snapshot
Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.
inferredcites →https://doi.org/10.1007/bf02531316openalex-snapshot
Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
inferredcites →https://doi.org/10.1016/0005-2736(95)00272-3openalex-snapshot
Rapid transmembrane movement of C6-NBD-labeled phospholipids across the inner membrane of Escherichia coli
inferredcites →https://doi.org/10.1016/0009-3084(91)90046-eopenalex-snapshot
Transmembrane diffusion of fluorescent phospholipids in human erythrocytes
inferredcites →https://doi.org/10.1016/s0006-3495(00)76807-xopenalex-snapshot
Rapid Flip-Flop of Phospholipids in Endoplasmic Reticulum Membranes Studied by a Stopped-Flow Approach
inferredcites →https://doi.org/10.1016/s0014-5793(02)03061-2openalex-snapshot
Influence of lipids on membrane assembly and stability of the potassium channel KcsA
inferredcites →https://doi.org/10.1016/s0014-5793(98)00733-9openalex-snapshot
Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes
inferredcites →https://doi.org/10.1016/s0021-9258(18)33073-4openalex-snapshot
Reconstitution of rapid and asymmetric assembly of M13 procoat protein into liposomes which have bacterial leader peptidase.
inferredcites →https://doi.org/10.1016/s1084-9521(02)00044-7openalex-snapshot
Phospholipid flip-flop in biogenic membranes: what is needed to connect opposite sides
inferredcites →https://doi.org/10.1016/s1388-1981(99)00110-9openalex-snapshot
Lipid translocation across the plasma membrane of mammalian cells
inferredcites →https://doi.org/10.1021/bi000810nopenalex-snapshot
The Lipopolysaccharide Barrier: Correlation of Antibiotic Susceptibility with Antibiotic Permeability and Fluorescent Probe Binding Kinetics
inferredcites →https://doi.org/10.1021/bi00187a044openalex-snapshot
Pore-Forming Peptides Induce Rapid Phospholipid Flip-Flop in Membranes
inferredcites →https://doi.org/10.1021/bi002903aopenalex-snapshot
Effect of Nonbilayer Lipids on Membrane Binding and Insertion of the Catalytic Domain of Leader Peptidase
inferredcites →https://doi.org/10.1021/bi00320a044openalex-snapshot
Processing of preproteins by liposomes bearing leader peptidase
inferredcites →https://doi.org/10.1021/bi00460a010openalex-snapshot
Protein-mediated phospholipid translocation in the endoplasmic reticulum with a low lipid specificity
inferredcites →https://doi.org/10.1021/bi00783a003openalex-snapshot
Inside-outside transitions of phospholipids in vesicle membranes
inferredcites →https://doi.org/10.1021/bi010627+openalex-snapshot
Membrane-Spanning Peptides Induce Phospholipid Flop: A Model for Phospholipid Translocation across the Inner Membrane of E. coli
inferredcites →https://doi.org/10.1021/bi020385topenalex-snapshot
Transbilayer Movement of Monohexosylsphingolipids in Endoplasmic Reticulum and Golgi Membranes
inferredcites →https://doi.org/10.1021/bi026215yopenalex-snapshot
Lipids in the Structure, Folding, and Function of the KcsA K+ Channel
inferredcites →https://doi.org/10.1021/bi0268403openalex-snapshot
Phospholipid Flop Induced by Transmembrane Peptides in Model Membranes Is Modulated by Lipid Composition
inferredcites →https://doi.org/10.1021/bi9519258openalex-snapshot
Induction of Nonbilayer Structures in Diacylphosphatidylcholine Model Membranes by Transmembrane α-Helical Peptides: Importance of Hydrophobic Mismatch and Proposed Role of Tryptophans
inferredcites →https://doi.org/10.1021/bi962513hopenalex-snapshot
Transbilayer Movement of Fluorescent Phospholipids in Bacillus megaterium Membrane Vesicles
inferredcites →https://doi.org/10.1021/bi971018yopenalex-snapshot
Structural Dynamics of the Streptomyces lividans K+ Channel (SKC1): Oligomeric Stoichiometry and Stability,
inferredcites →https://doi.org/10.1021/bi980233ropenalex-snapshot
Influence of Lipid/Peptide Hydrophobic Mismatch on the Thickness of Diacylphosphatidylcholine Bilayers. A 2H NMR and ESR Study Using Designed Transmembrane α-Helical Peptides and Gramicidin A
inferredcites →https://doi.org/10.1046/j.1432-1327.2002.02820.xopenalex-snapshot
Lipopolysaccharide regions involved in the activation of Escherichia coli outer membrane protease OmpT
inferredcites →https://doi.org/10.1073/pnas.76.12.6245openalex-snapshot
Energetics of rapid transmembrane movement and of compositional asymmetry of phosphatidylethanolamine in membranes of Bacillus megaterium.
inferredcites →https://doi.org/10.1074/jbc.271.12.6651openalex-snapshot
Ultrafast Glycerophospholipid-selective Transbilayer Motion Mediated by a Protein in the Endoplasmic Reticulum Membrane
inferredcites →https://doi.org/10.1074/jbc.273.20.12466openalex-snapshot
Function of Escherichia coli MsbA, an Essential ABC Family Transporter, in Lipid A and Phospholipid Biosynthesis
inferredcites →https://doi.org/10.1074/jbc.273.30.18936openalex-snapshot
Rapid Transmembrane Movement of Newly Synthesized Phosphatidylethanolamine across the Inner Membrane of Escherichia coli
inferredcites →https://doi.org/10.1074/jbc.274.28.19913openalex-snapshot
Δψ Stimulates Membrane Translocation of the C-terminal Part of a Signal Sequence
inferredcites →https://doi.org/10.1074/jbc.c100091200openalex-snapshot
An Escherichia coli Mutant Defective in Lipid Export
inferredcites →https://doi.org/10.1074/jbc.m205857200openalex-snapshot
ATPase Activity of the MsbA Lipid Flippase of Escherichia coli
inferredcites →https://doi.org/10.1093/embo-reports/kvd067openalex-snapshot
Efficient membrane assembly of the KcsA potassium channel in Escherichia coli requires the protonmotive force
inferredcites →https://doi.org/10.1093/emboj/20.18.5033openalex-snapshot
Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
inferredcites →https://doi.org/10.1111/j.1365-2958.1993.tb01098.xopenalex-snapshot
The essential Escherichia coli msbA gene, a multicopy suppressor of null mutations in the htrB gene, is related to the universally conserved family of ATP‐dependent translocators
inferredcites →https://doi.org/10.1126/science.280.5360.69openalex-snapshot
The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
inferredcites →https://doi.org/10.1126/science.293.5536.1793openalex-snapshot
Structure of MsbA from E. coli : A Homolog of the Multidrug Resistance ATP Binding Cassette (ABC) Transporters
inferredcites →https://doi.org/10.1128/jb.154.1.76-83.1983openalex-snapshot
Demonstration by a Novel Genetic Technique That Leader Peptidase Is an Essential Enzyme of Escherichia coli
inferredcites →https://doi.org/10.1128/mmbr.64.4.672-693.2000openalex-snapshot
Molecular Properties of Bacterial Multidrug Transporters
inferredcites →https://doi.org/10.1242/jcs.1989.supplement_11.6openalex-snapshot
Involvement of membrane lipids in protein export in Escherichia coli
inferredcites →https://doi.org/10.3109/09687689509072437openalex-snapshot
A quantitative assay to determine the amount of Signal Peptidase I inE. coliand the orientation of membrane vesicles
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Lipid flippases and their biological functions
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inferred← citeshttps://doi.org/10.1007/s00249-011-0693-4openalex-snapshot
A lipocentric view of peptide-induced pores
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Lipid dynamics in boar sperm studied by advanced fluorescence imaging techniques
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Function of prokaryotic and eukaryotic ABC proteins in lipid transport
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Biogenesis, transport and remodeling of lysophospholipids in Gram-negative bacteria
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Structural biology of membrane-intrinsic β-barrel enzymes: Sentinels of the bacterial outer membrane
inferred← citeshttps://doi.org/10.1016/j.bbamem.2008.01.015openalex-snapshot
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pH-dependent promotion of phospholipid flip-flop by the KcsA potassium channel
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Electrophysiological interrogation of asymmetric droplet interface bilayers reveals surface-bound alamethicin induces lipid flip-flop
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Structural Properties of Model Phosphatidylcholine Flippases
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Modelling of proteins in membranes
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Inner membrane lipids of Escherichia coli form domains
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Biogenesis of the Gram-negative bacterial outer membrane
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Autonomous Synthesis and Scrambling of Phospholipids, Linked to Recycling of Cofactors in Synthetic Cells
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Transbilayer Movement of Phospholipids in Biogenic Membranes
inferred← citeshttps://doi.org/10.1021/bi049063aopenalex-snapshot
Chemical Modification Identifies Two Populations of Glycerophospholipid Flippase in Rat Liver ER
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Molecular Simulations of Lipid Flip-Flop in the Presence of Model Transmembrane Helices
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Flipping Lipids: Why an’ What’s the Reason for?
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Membrane Activity of Biomimetic Facially Amphiphilic Antibiotics
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Ca2+-dependent phospholipid scrambling by a reconstituted TMEM16 ion channel
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Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase
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Translocation of a single Arg$$_9$$ peptide across a DOPC/DOPG(4:1) model membrane using the weighted ensemble method
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Thermodynamics of flip-flop and desorption for a systematic series of phosphatidylcholine lipids
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