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Relevant bibliographies by topics / Gram-negative inner membrane

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Journal articles

Academic literature on the topic 'Gram-negative inner membrane'

Author: Grafiati

Published: 6 September 2023

Last updated: 7 September 2023

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Journal articles on the topic "Gram-negative inner membrane"

1

Powers, Matthew J., and M. Stephen Trent. "Intermembrane transport: Glycerophospholipid homeostasis of the Gram-negative cell envelope." Proceedings of the National Academy of Sciences 116, no. 35 (2019): 17147–55. http://dx.doi.org/10.1073/pnas.1902026116.

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This perspective addresses recent advances in lipid transport across the Gram-negative inner and outer membranes. While we include a summary of previously existing literature regarding this topic, we focus on the maintenance of lipid asymmetry (Mla) pathway. Discovered in 2009 by the Silhavy group [J. C. Malinverni, T. J. Silhavy, Proc. Natl. Acad. Sci. U.S.A. 106, 8009–8014 (2009)], Mla has become increasingly appreciated for its role in bacterial cell envelope physiology. Through the work of many, we have gained an increasingly mechanistic understanding of the function of Mla via genetic, bi

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2

Orlando, Benjamin, Yanyan Li, and Maofu Liao. "Snapshots of Endotoxin Extraction from the Gram-negative Inner Membrane." Microscopy and Microanalysis 26, S2 (2020): 2520. http://dx.doi.org/10.1017/s1431927620021893.

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3

Epand, Raquel F., Jake E. Pollard, Jonathan O. Wright, Paul B. Savage, and Richard M. Epand. "Depolarization, Bacterial Membrane Composition, and the Antimicrobial Action of Ceragenins." Antimicrobial Agents and Chemotherapy 54, no. 9 (2010): 3708–13. http://dx.doi.org/10.1128/aac.00380-10.

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ABSTRACT Ceragenins are cholic acid-derived antimicrobial agents that mimic the activity of endogenous antimicrobial peptides. Ceragenins target bacterial membranes, yet the consequences of these interactions have not been fully elucidated. The role of the outer membrane in allowing access of the ceragenins to the cytoplasmic membrane of Gram-negative bacteria was studied using the ML-35p mutant strain of Escherichia coli that has been engineered to allow independent monitoring of small-molecule flux across the inner and outer membranes. The ceragenins CSA-8, CSA-13, and CSA-54 permeabilize th

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4

Sutterlin, Holly A., Handuo Shi, Kerrie L. May, et al. "Disruption of lipid homeostasis in the Gram-negative cell envelope activates a novel cell death pathway." Proceedings of the National Academy of Sciences 113, no. 11 (2016): E1565—E1574. http://dx.doi.org/10.1073/pnas.1601375113.

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Gram-negative bacteria balance synthesis of the outer membrane (OM), cell wall, and cytoplasmic contents during growth via unknown mechanisms. Here, we show that a dominant mutation (designatedmlaA*, maintenance of lipid asymmetry) that alters MlaA, a lipoprotein that removes phospholipids from the outer leaflet of the OM ofEscherichia coli, increases OM permeability, lipopolysaccharide levels, drug sensitivity, and cell death in stationary phase. Surprisingly, single-cell imaging revealed that death occurs after protracted loss of OM material through vesiculation and blebbing at cell-division

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5

Li, Xiangyuan, Lei Fu, Shan Zhang, Yipeng Wang, and Lianghui Gao. "How Alligator Immune Peptides Kill Gram-Negative Bacteria: A Lipid-Scrambling, Squeezing, and Extracting Mechanism Revealed by Theoretical Simulations." International Journal of Molecular Sciences 24, no. 13 (2023): 10962. http://dx.doi.org/10.3390/ijms241310962.

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Alligator sinensis cathelicidins (As-CATHs) are antimicrobial peptides extracted from alligators that enable alligators to cope with diseases caused by bacterial infections. This study assessed the damaging effects of sequence-truncated and residue-substituted variants of As-CATH4, AS4-1, AS4-5, and AS4-9 (with decreasing charges but increasing hydrophobicity) on the membranes of Gram-negative bacteria at the molecular level by using coarse-grained molecular dynamics simulations. The simulations predicted that all the variants disrupt the structures of the inner membrane of Gram-negative bacte

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6

Pérez-Cruz, Carla, Lidia Delgado, Carmen López-Iglesias, and Elena Mercade. "Outer-Inner Membrane Vesicles Naturally Secreted by Gram-Negative Pathogenic Bacteria." PLOS ONE 10, no. 1 (2015): e0116896. http://dx.doi.org/10.1371/journal.pone.0116896.

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7

Raina, Satish. "Lipopolysaccharides: Regulated Biosynthesis and Structural Diversity." International Journal of Molecular Sciences 24, no. 8 (2023): 7498. http://dx.doi.org/10.3390/ijms24087498.

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The cell envelope of Gram-negative bacteria contains two distinct membranes, an inner (IM) and an outer (OM) membrane, separated by the periplasm, a hydrophilic compartment that includes a thin layer of peptidoglycan [...]

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8

Makowski, Marcin, Mário R. Felício, Isabel C. M. Fensterseifer, Octávio L. Franco, Nuno C. Santos, and Sónia Gonçalves. "EcDBS1R4, an Antimicrobial Peptide Effective against Escherichia coli with In Vitro Fusogenic Ability." International Journal of Molecular Sciences 21, no. 23 (2020): 9104. http://dx.doi.org/10.3390/ijms21239104.

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Discovering antibiotic molecules able to hold the growing spread of antimicrobial resistance is one of the most urgent endeavors that public health must tackle. The case of Gram-negative bacterial pathogens is of special concern, as they are intrinsically resistant to many antibiotics, due to an outer membrane that constitutes an effective permeability barrier. Antimicrobial peptides (AMPs) have been pointed out as potential alternatives to conventional antibiotics, as their main mechanism of action is membrane disruption, arguably less prone to elicit resistance in pathogens. Here, we investi

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9

Banack, Trevor, Peter D. Kim, and William Firshein. "TrfA-Dependent Inner Membrane-Associated Plasmid RK2 DNA Synthesis and Association of TrfA with Membranes of Different Gram-Negative Hosts." Journal of Bacteriology 182, no. 16 (2000): 4380–83. http://dx.doi.org/10.1128/jb.182.16.4380-4383.2000.

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ABSTRACT TrfA, the replication initiator protein of broad-host-range plasmid RK2, was tested for its ability to bind to the membrane of four different gram-negative hosts in addition to Escherichia coli: Pseudomonas aeruginosa, Pseudomonas putida, Salmonella enterica serovar Typhimurium, andRhodobacter sphaeroides. Cells harboring TrfA-encoding plasmids were fractionated into soluble, inner membrane, and outer membrane fractions. The fractions were subjected to Western blotting, and the blots were probed with antibody to the TrfA proteins. TrfA was found to fractionate with the cell membranes

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10

Clausell, Adrià, Maria Garcia-Subirats, Montserrat Pujol, M. Antonia Busquets, Francesc Rabanal, and Yolanda Cajal. "Gram-Negative Outer and Inner Membrane Models: Insertion of Cyclic Cationic Lipopeptides." Journal of Physical Chemistry B 111, no. 3 (2007): 551–63. http://dx.doi.org/10.1021/jp064757+.

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