Melittin: a membrane-active peptide with diverse functions.
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In vitro and in vivo antimicrobial activity of granulysin-derived peptides against Vibrio choleraeAnti-Inflammatory Applications of Melittin, a Major Component of Bee Venom: Detailed Mechanism of Action and Adverse EffectsAnti-parasitic Peptides from Arthropods and their Application in Drug TherapyPerspective of Use of Antiviral Peptides against Influenza VirusPharmacological Alternatives for the Treatment of Neurodegenerative Disorders: Wasp and Bee Venoms and Their Components as New Neuroactive ToolsPeptides and Peptidomimetics for Antimicrobial Drug DesignMechanical properties of lipid bilayers and regulation of mechanosensitive function: from biological to biomimetic channelsNovel lynx spider toxin shares common molecular architecture with defense peptides from frog skinSelective ruthenium labeling of the tryptophan residue in the bee venom Peptide melittinInsights into the Mechanism of Action of Bactericidal Lipophosphonoxinsβ1-Adrenergic receptors activate two distinct signaling pathways in striatal neuronsHoney bee protein atlas at organ-level resolutionEfficacy of Antibacterial Peptides Against Peptide-Resistant MRSA Is Restored by Permeabilization of Bacteria MembranesThe lipid dependence of melittin action investigated by dual-color fluorescence burst analysis.Comprehensive characterization of molecular interactions based on nanomechanicsEngineering biodegradable and multifunctional peptide-based polymers for gene delivery.Suppression of Hepatic Epithelial-to-Mesenchymal Transition by Melittin via Blocking of TGFβ/Smad and MAPK-JNK Signaling Pathways.Acyl transfer from phosphocholine lipids to melittin.Therapeutic Properties of Bioactive Compounds from Different Honeybee Products.Production of human antibody fragments binding to melittin and phospholipase A2 in Africanised bee venom: minimising venom toxicity.Gain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening.Cobra cytotoxins: structural organization and antibacterial activity.Antimicrobial peptides: a new class of antimalarial drugs?Melittin suppresses HIF-1α/VEGF expression through inhibition of ERK and mTOR/p70S6K pathway in human cervical carcinoma cells.Coupled folding and specific binding: fishing for amphiphilicity.Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.Spider venom peptides for gene therapy of Chlamydia infection.Structural basis for the geometry-driven localization of a small protein.Interaction of melittin peptides with perfluorocarbon nanoemulsion particles.The structure of a melittin-stabilized poreHydrogen Exchange Mass Spectrometry of Proteins at Langmuir MonolayersComparative molecular dynamics simulations of the antimicrobial peptide CM15 in model lipid bilayers.Genetically Engineered Yeast Expressing a Lytic Peptide from Bee Venom (Melittin) Kills Symbiotic Protozoa in the Gut of Formosan Subterranean Termites.A role for peptides in overcoming endosomal entrapment in siRNA delivery - A focus on melittinCollagen-like antimicrobial peptides.Structure-activity relationships and action mechanisms of collagen-like antimicrobial peptides.Effects of Melittin Treatment in Cholangitis and Biliary Fibrosis in a Model of Xenobiotic-Induced Cholestasis in MiceLipid interaction of the C terminus and association of the transmembrane segments facilitate atlastin-mediated homotypic endoplasmic reticulum fusion.Spectroscopic and computational study of melittin, cecropin A, and the hybrid peptide CM15.Bee venom phospholipase A2 suppresses allergic airway inflammation in an ovalbumin-induced asthma model through the induction of regulatory T cells.
P2860
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P2860
Melittin: a membrane-active peptide with diverse functions.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Melittin: a membrane-active peptide with diverse functions.
@ast
Melittin: a membrane-active peptide with diverse functions.
@en
type
label
Melittin: a membrane-active peptide with diverse functions.
@ast
Melittin: a membrane-active peptide with diverse functions.
@en
prefLabel
Melittin: a membrane-active peptide with diverse functions.
@ast
Melittin: a membrane-active peptide with diverse functions.
@en
P2860
P1433
P1476
Melittin: a membrane-active peptide with diverse functions
@en
P2093
Amitabha Chattopadhyay
P2860
P2888
P304
P356
10.1007/S10540-006-9030-Z
P50
P577
2007-10-01T00:00:00Z