The cyclic peptide labaditin does not alter the outer membrane integrity of Salmonella enterica serovar Typhimurium
暂无分享,去创建一个
[1] S. Enami,et al. In Situ Nondestructive Analysis of Kalanchoe pinnata Leaf Surface Structure by Polarization-Modulation Infrared Reflection-Absorption Spectroscopy. , 2017, The journal of physical chemistry. B.
[2] Michael R Hamblin,et al. Advances in antimicrobial photodynamic inactivation at the nanoscale , 2017, Nanophotonics.
[3] L. Caseli,et al. Interaction of non-aqueous dispersions of silver nanoparticles with cellular membrane models. , 2017, Journal of colloid and interface science.
[4] C. Verma,et al. Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design , 2017, Front. Neurosci..
[5] G. Maróti,et al. Comparative Analysis of the Bacterial Membrane Disruption Effect of Two Natural Plant Antimicrobial Peptides , 2017, Front. Microbiol..
[6] M. Mahlapuu,et al. Antimicrobial Peptides: An Emerging Category of Therapeutic Agents , 2016, Front. Cell. Infect. Microbiol..
[7] D. Volpati,et al. The importance of cyclic structure for Labaditin on its antimicrobial activity against Staphylococcus aureus. , 2016, Colloids and surfaces. B, Biointerfaces.
[8] M. Kuehn,et al. Outer Membrane Vesicle Production Facilitates LPS Remodeling and Outer Membrane Maintenance in Salmonella during Environmental Transitions , 2016, mBio.
[9] Haohao Dong,et al. Structural insights into cardiolipin transfer from the Inner membrane to the outer membrane by PbgA in Gram-negative bacteria , 2016, Scientific Reports.
[10] I. Autenrieth,et al. Structure and function: Lipid A modifications in commensals and pathogens. , 2016, International journal of medical microbiology : IJMM.
[11] S. Andrews,et al. Crosstalk between the lipopolysaccharide and phospholipid pathways during outer membrane biogenesis in Escherichia coli , 2016, Proceedings of the National Academy of Sciences.
[12] H. Nikaido,et al. Modification of Salmonella Lipopolysaccharides Prevents the Outer Membrane Penetration of Novobiocin. , 2015, Biophysical journal.
[13] Yue Sun,et al. Interactions between chensinin‐1, a natural antimicrobial peptide derived from Rana chensinensis, and lipopolysaccharide , 2015, Biopolymers.
[14] Samuel I. Miller,et al. S. Typhimurium strategies to resist killing by cationic antimicrobial peptides. , 2015, Biochimica et biophysica acta.
[15] S Gnanakaran,et al. Permeability Barrier of Gram-Negative Cell Envelopes and Approaches To Bypass It. , 2015, ACS infectious diseases.
[16] Juneyoung Lee,et al. Antimicrobial Peptides (AMPs) with Dual Mechanisms: Membrane Disruption and Apoptosis. , 2015, Journal of microbiology and biotechnology.
[17] S. Fang,et al. Antibacterial Mechanisms of Polymyxin and Bacterial Resistance , 2015, BioMed research international.
[18] P. Ciancaglini,et al. Interaction of cyclic and linear Labaditin peptides with anionic and zwitterionic micelles. , 2015, Journal of colloid and interface science.
[19] M. Aguilar,et al. Real-time Measurement of Membrane Conformational States Induced by Antimicrobial Peptides: Balance Between Recovery and Lysis , 2014, Scientific Reports.
[20] G. Grassl,et al. Same species, different diseases: how and why typhoidal and non-typhoidal Salmonella enterica serovars differ , 2014, Front. Microbiol..
[21] M. Friedman,et al. Effect of Structure on the Interactions between Five Natural Antimicrobial Compounds and Phospholipids of Bacterial Cell Membrane on Model Monolayers , 2014, Molecules.
[22] D. Alves,et al. Mini-review: Antimicrobial peptides and enzymes as promising candidates to functionalize biomaterial surfaces , 2014, Biofouling.
[23] B. Mattei,et al. Structure-activity relationship of the antimicrobial peptide gomesin: the role of peptide hydrophobicity in its interaction with model membranes. , 2014, Langmuir : the ACS journal of surfaces and colloids.
[24] Ildinete Silva-Pereira,et al. Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance , 2013, Front. Microbiol..
[25] B. Bonev,et al. Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study. , 2013, Biochimica et biophysica acta.
[26] A. Lomize,et al. Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization , 2013, PLoS neglected tropical diseases.
[27] E. Cilli,et al. Dimerization of aurein 1.2: effects in structure, antimicrobial activity and aggregation of Cândida albicans cells , 2013, Amino Acids.
[28] A. Falanga,et al. Microbe-Host Interactions: Structure and Role of Gram-Negative Bacterial Porins , 2012, Current protein & peptide science.
[29] H. Won,et al. Antimicrobial Peptides for Therapeutic Applications: A Review , 2012, Molecules.
[30] T. van der Poll,et al. Host–Pathogen Interaction in Invasive Salmonellosis , 2012, PLoS pathogens.
[31] M. Selsted,et al. θ-Defensins: Cyclic Peptides with Endless Potential* , 2012, The Journal of Biological Chemistry.
[32] E. Breukink,et al. Interaction with Lipid II Induces Conformational Changes in Bovicin HC5 Structure , 2012, Antimicrobial Agents and Chemotherapy.
[33] Nicholas G. Housden,et al. Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF , 2010, Proceedings of the National Academy of Sciences.
[34] C. Toniolo,et al. Fluctuations and the rate-limiting step of peptide-induced membrane leakage. , 2010, Biophysical journal.
[35] T. Silhavy,et al. The bacterial cell envelope. , 2010, Cold Spring Harbor perspectives in biology.
[36] B. Korchowiec,et al. Differentiating oxicam nonsteroidal anti-inflammatory drugs in phosphoglyceride monolayers. , 2010, Langmuir : the ACS journal of surfaces and colloids.
[37] A. Ramamoorthy,et al. Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37. , 2010, Biophysical journal.
[38] A. Delcour,et al. Outer membrane permeability and antibiotic resistance. , 2009, Biochimica et biophysica acta.
[39] M. N. Melo,et al. Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations , 2009, Nature Reviews Microbiology.
[40] J. L. Ding,et al. Interaction of an artificial antimicrobial peptide with lipid membranes. , 2009, Biochimica et biophysica acta.
[41] R. Epand,et al. Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins). , 2007, Biochimica et biophysica acta.
[42] G. Pabst,et al. How lipids influence the mode of action of membrane-active peptides. , 2007, Biochimica et biophysica acta.
[43] P. Janmey,et al. Interaction of the Gelsolin-Derived Antibacterial PBP 10 Peptide with Lipid Bilayers and Cell Membranes , 2006, Antimicrobial Agents and Chemotherapy.
[44] S. Gellman,et al. Role of membrane lipids in the mechanism of bacterial species selective toxicity by two α/β-antimicrobial peptides , 2006 .
[45] M. Niederweis,et al. Mycobacterial porins – new channel proteins in unique outer membranes , 2003, Molecular microbiology.
[46] T. Ganz. Defensins: antimicrobial peptides of innate immunity , 2003, Nature Reviews Immunology.
[47] Dong-Kuk Lee,et al. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. , 2003, Biochemistry.
[48] J. Vanderleyden,et al. O-antigen structural variation: mechanisms and possible roles in animal/plant-microbe interactions. , 2001, FEMS microbiology reviews.
[49] L. Joosten,et al. Lethal Escherichia coli and Salmonella typhimurium endotoxemia is mediated through different pathways , 2001, European journal of immunology.
[50] J. Gunn. Bacterial modification of LPS and resistance to antimicrobial peptides , 2001, Journal of endotoxin research.
[51] M. Pirrung,et al. Antibacterial Agents That Target Lipid A Biosynthesis in Gram-negative Bacteria , 2000, The Journal of Biological Chemistry.
[52] H. Vogel,et al. Diversity of antimicrobial peptides and their mechanisms of action. , 1999, Biochimica et biophysica acta.
[53] G. Schwarz,et al. Polymorphism and interactions of a viral fusion peptide in a compressed lipid monolayer. , 1999, Biophysical journal.
[54] N. A. Nnalue. α-GlcNAc-1→2-α-Glc, the SalmonellaHomologue of a Conserved Lipopolysaccharide Motif in theEnterobacteriaceae, Elicits Broadly Cross-Reactive Antibodies , 1998, Infection and Immunity.
[55] B. Lindner,et al. Molecular Mechanisms of Polymyxin B-Membrane Interactions: Direct Correlation Between Surface Charge Density and Self-Promoted Transport , 1998, The Journal of Membrane Biology.
[56] Y. Kirino,et al. Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog. , 1997, Biochemistry.
[57] J. Schneider-Mergener,et al. High Affinity Endotoxin-binding and Neutralizing Peptides Based on the Crystal Structure of Recombinant Limulus Anti-lipopolysaccharide Factor* , 1996, The Journal of Biological Chemistry.
[58] S. Kosasi,et al. Labaditin, a novel cyclic decapeptide from the latex of Jatropha multifida L. (Euphorbiaceae) , 1989 .
[59] S. Fleischer,et al. Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots , 1970, Lipids.
[60] G. Ames. Lipids of Salmonella typhimurium and Escherichia coli: Structure and Metabolism , 1968, Journal of bacteriology.
[61] R. C. Macridis. A review , 1963 .
[62] S. Castano,et al. Structure and orientation study of Ebola fusion peptide inserted in lipid membrane models. , 2014, Biochimica et biophysica acta.
[63] P. Ciancaglini,et al. Labaditin, a cyclic peptide with rich biotechnological potential: preliminary toxicological studies and structural changes in water and lipid membrane environment , 2010, Amino Acids.
[64] R. Epand,et al. Lipid domains in bacterial membranes and the action of antimicrobial agents. , 2009, Biochimica et biophysica acta.
[65] S. Gellman,et al. Role of membrane lipids in the mechanism of bacterial species selective toxicity by two alpha/beta-antimicrobial peptides. , 2006, Biochimica et biophysica acta.
[66] N. A. Nnalue. alpha-GlcNAc-1-->2-alpha-glc, the Salmonella homologue of a conserved lipopolysaccharide motif in the Enterobacteriaceae, elicits broadly cross-reactive antibodies. , 1998, Infection and immunity.
[67] V. Potter. Structure and metabolism , 1960 .