Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores.
about
Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effectMechanical properties of lipid bilayers and regulation of mechanosensitive function: from biological to biomimetic channelsEvidence for Phenylalanine Zipper-Mediated Dimerization in the X-ray Crystal Structure of a Magainin 2 AnalogueStructure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores.Membrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Simulations of Membrane-Disrupting Peptides II: AMP Piscidin 1 Favors Surface Defects over PoresAssessing the nature of lipid raft membranesThe lipid dependence of melittin action investigated by dual-color fluorescence burst analysis.Connecting peptide physicochemical and antimicrobial properties by a rational prediction model.Antimicrobial peptides in toroidal and cylindrical pores.Antimicrobial peptides bind more strongly to membrane poresMembrane-active peptides: binding, translocation, and flux in lipid vesicles.Perforin rapidly induces plasma membrane phospholipid flip-flopThe nociceptive and anti-nociceptive effects of bee venom injection and therapy: a double-edged swordTransbilayer peptide sorting between raft and nonraft bilayers: comparisons of detergent extraction and confocal microscopy.Many-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formationPerforin oligomers form arcs in cellular membranes: a locus for intracellular delivery of granzymes.The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action.Activity determinants of helical antimicrobial peptides: a large-scale computational studyMembrane Incorporation, Channel Formation, and Disruption of Calcium Homeostasis by Alzheimer's β-Amyloid Protein.Bacterial killing mechanism of sheep myeloid antimicrobial peptide-18 (SMAP-18) and its Trp-substituted analog with improved cell selectivity and reduced mammalian cell toxicity.Interaction of protegrin-1 with lipid bilayers: membrane thinning effect.The role of antimicrobial peptides in preventing multidrug-resistant bacterial infections and biofilm formation.Membrane-proximal external HIV-1 gp41 motif adapted for destabilizing the highly rigid viral envelopeInteraction of melittin peptides with perfluorocarbon nanoemulsion particles.The structure of a melittin-stabilized poreCharge distribution and imperfect amphipathicity affect pore formation by antimicrobial peptides.Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure.The activity of the amphipathic peptide delta-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties.Models of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels.Mode of Action of Antimicrobial Peptides on E. coli SpheroplastsSubstrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter.A novel antimicrobial protein for plant protection consisting of a Xanthomonas oryzae harpin and active domains of cecropin A and melittinMechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.Kinetic Defects Induced by Melittin in Model Lipid Membranes: A Solution Atomic Force Microscopy Study.Antimicrobial properties and membrane-active mechanism of a potential α-helical antimicrobial derived from cathelicidin PMAP-36.Antimicrobial peptides: modes of mechanism, modulation of defense responses.Polyethylenimine and chitosan carriers for the delivery of RNA interference effectors.Preparation and Characterization of Gelonin-Melittin Fusion Biotoxin for Synergistically Enhanced Anti-Tumor Activity.Phospholipase A activity of adenylate cyclase toxin mediates translocation of its adenylate cyclase domain.
P2860
Q21256419-9BF67B55-8A32-4BE9-B437-78041A25F140Q26864371-E6E9CF67-5A4E-402D-A695-E8097E302E66Q27680196-E0DD86E6-BF29-4B42-A850-8477EF544B4EQ30157467-B459D524-1DB1-4B62-A248-3D351E915166Q30378040-F272D445-BAB1-4211-8B76-70F4C7785FB8Q31132190-CC631555-262C-4CA2-9F34-56176F7F710EQ33275288-0BEDD0E4-892D-4EBF-B741-A7CFC4D84995Q33282119-622358CF-4969-4F0A-AADE-806E8BCDC031Q33828728-C3FA8A9A-8AB9-4DFD-B5D0-A8E0A656BC93Q33912437-E3DE217C-9902-4F6A-B242-9CA98874F754Q33912494-770208AF-8C5B-4ED4-93B7-854E0378863FQ33944833-6A3E556D-065A-4F2B-83DE-61AC1EBD36C6Q34023350-BCAEB098-635D-4A7F-8D17-B348C32D5398Q34157706-AC4FCB27-F2BF-437D-B344-F24049FCFF1DQ34350714-95E005A3-0260-48BD-BFBB-9BF93F83501FQ34352457-1E7A1005-9EF3-4DB6-9A21-BE69C1A73F76Q34675229-33C3BF8B-5768-4735-8E0D-A4973FB6D35CQ34757081-48CC2C34-1A8E-437E-8622-266A958BAB8DQ34776684-09ED9D81-3F74-4631-83F8-699C6F564656Q34923956-E2F9CA32-C952-438F-B08D-3640C58F2368Q35039695-0367B0FC-4A9E-489A-9DF2-41F6CCEEE813Q35052050-367DE773-F7A4-465F-A346-40253EA375AEQ35297286-BFF133FA-7F64-423F-B35C-8F3C18C629BFQ35556337-DEFB4CC5-3D4A-481E-A0F5-C3A9AA720054Q35631698-9FCF5FED-0345-4BE3-A992-A5B96952981DQ35687054-30E9973B-6C89-4F11-BA7F-12F57BDEE8C5Q35869840-7731869D-E608-4931-8BD1-4E9DD40C3BD1Q36295920-169C3A0C-4AE7-4CE5-84B0-1E0448F8230BQ36957307-EA2C0245-7881-4A5D-B6A2-170377C3DB90Q36957398-44D3D0BF-9724-4C86-BBA7-6614EAF188C8Q37093925-A4618CE8-D0CD-4EFB-84FF-EC639F7082FFQ37254090-63C4CBC1-174F-476C-A4C9-88D9321F8EF2Q37273564-2B5C1D6B-38FA-4D6B-B789-B211656A1276Q37414152-20328C3E-CBE5-4638-8B05-A4E85EF8D31FQ37441619-7CBE2F21-60CE-425B-A2D0-12E8E851699BQ37500469-21EBCED1-F352-4922-821F-3B6711115536Q37918722-D6570BCE-01E6-4F70-8E1E-14D5C135988FQ38148788-A68A6669-ED37-4B9E-8429-EF4DE842A354Q38413846-5504C423-331C-408A-B512-D3564B06D714Q38650797-5BC89F00-9BC6-469D-9AD2-567DBF2BC8F9
P2860
Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@ast
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@en
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@nl
type
label
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@ast
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@en
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@nl
prefLabel
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@ast
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@en
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@nl
P2093
P2860
P1433
P1476
Melittin-induced bilayer leaka ...... : evidence for toroidal pores.
@en
P2093
Daniel Allende
Thomas J McIntosh
P2860
P304
P356
10.1529/BIOPHYSJ.104.049817
P407
P577
2004-12-13T00:00:00Z