Transmembrane pores formed by human antimicrobial peptide LL-37. - Wikidata - wikimedia - TriplyDB

Transmembrane pores formed by human antimicrobial peptide LL-37.

Transmembrane pores formed by human antimicrobial peptide LL-37.

http://www.wikidata.org/entity/Q34771808

about

Functional linkage between genes that regulate osmotic stress responses and multidrug resistance transporters: challenges and opportunities for antibiotic discovery High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments.A cactus-derived toxin-like cystine knot Peptide with selective antimicrobial activity Structural and functional characterization of a multifunctional alanine-rich peptide analogue from Pleuronectes americanus Real-time attack of LL-37 on single Bacillus subtilis cells.Localized permeabilization of E. coli membranes by the antimicrobial peptide Cecropin A.NH125 kills methicillin-resistant Staphylococcus aureus persisters by lipid bilayer disruption.Prevention of anti-microbial peptide LL-37-induced apoptosis and ATP release in the urinary bladder by a modified glycosaminoglycan Variations in the interaction of human defensins with Escherichia coli: Possible implications in bacterial killing Human antimicrobial peptides and proteins Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer.The use of MALDI-TOF-MS and in silico studies for determination of antimicrobial peptides' affinity to bacterial cells.Host defense peptides: an alternative as antiinfective and immunomodulatory therapeutics.Activity determinants of helical antimicrobial peptides: a large-scale computational study Density-biased sampling: a robust computational method for studying pore formation in membranes Membrane-Active Small Molecules: Designs Inspired by Antimicrobial Peptides.Determining the mechanism of membrane permeabilizing peptides: identification of potent, equilibrium pore-formers Human β-defensin 3 contains an oncolytic motif that binds PI(4,5)P2 to mediate tumour cell permeabilisation.Membrane permeability of hydrocarbon-cross-linked peptides Mode of Action of Antimicrobial Peptides on E. coli Spheroplasts Neutron Scattering Studies of the Interplay of Amyloid β Peptide(1-40) and An Anionic Lipid 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol.Effect of intracellular expression of antimicrobial peptide LL-37 on growth of escherichia coli strain TOP10 under aerobic and anaerobic conditions Database-Guided Discovery of Potent Peptides to Combat HIV-1 or Superbugs Single-molecule visualization of dynamic transitions of pore-forming peptides among multiple transmembrane positions.Little peptide, big effects: the role of LL-37 in inflammation and autoimmune disease Differential Ability of Bovine Antimicrobial Cathelicidins to Mediate Nucleic Acid Sensing by Epithelial Cells.Mechanistic and structural basis of bioengineered bovine Cathelicidin-5 with optimized therapeutic activity.Antimicrobial peptides and colitis.Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.Antimicrobial peptides (AMPs) as drug candidates: a patent review (2003-2015).The therapeutic applications of antimicrobial peptides (AMPs): a patent review.Effects of Coal Fly Ash Particulate Matter on the Antimicrobial Activity of Airway Surface Liquid.Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation.The Human Antimicrobial Peptides Dermcidin and LL-37 Show Novel Distinct Pathways in Membrane Interactions.Understanding membrane-active antimicrobial peptides.Using electrospun poly(ethylene-oxide) nanofibers for improved retention and efficacy of bacteriolytic antibiotics.Action of Antimicrobial Peptides on Bacterial and Lipid Membranes: A Direct Comparison.Mechanism of action of the tri-hybrid antimicrobial peptide LHP7 from lactoferricin, HP and plectasin on Staphylococcus aureus.Molecular Dynamics Simulations of Human Antimicrobial Peptide LL-37 in Model POPC and POPG Lipid Bilayers.Antimicrobial and Chemotactic Activity of Scorpion-Derived Peptide, ToAP2, against Mycobacterium massiliensis.

P2860

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P2860

Transmembrane pores formed by human antimicrobial peptide LL-37.

http://www.wikidata.org/entity/Q34771808

description

2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Transmembrane pores formed by human antimicrobial peptide LL-37.

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Transmembrane pores formed by human antimicrobial peptide LL-37.

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Transmembrane pores formed by human antimicrobial peptide LL-37.

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type

label

Transmembrane pores formed by human antimicrobial peptide LL-37.

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Transmembrane pores formed by human antimicrobial peptide LL-37.

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Transmembrane pores formed by human antimicrobial peptide LL-37.

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prefLabel

Transmembrane pores formed by human antimicrobial peptide LL-37.

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Transmembrane pores formed by human antimicrobial peptide LL-37.

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Transmembrane pores formed by human antimicrobial peptide LL-37.

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J.BPJ.2011.02.018

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Biophysical Journal

P1476

Transmembrane pores formed by human antimicrobial peptide LL-37.

@en

P2093

Chang-Chun Lee

http://www.w3.org/2001/XMLSchema#string

Huey W Huang

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Yen Sun

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P2860

The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide

LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells

A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution

Antimicrobial peptides of multicellular organisms

Cathelicidins, multifunctional peptides of the innate immunity

Barrel-stave model or toroidal model? A case study on melittin pores.

Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores.

The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities.

NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles.

Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils.

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transmembrane protein

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3072607

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