about
Studies on anticancer activities of antimicrobial peptidesAnti-Inflammatory Applications of Melittin, a Major Component of Bee Venom: Detailed Mechanism of Action and Adverse EffectsBarrel-stave model or toroidal model? A case study on melittin pores.Membrane molecule reorientation in an electric field recorded by attenuated total reflection Fourier-transform infrared spectroscopy.Solid-state NMR structure determination of melittin in a lipid environment.PR-39, a syndecan-inducing antimicrobial peptide, binds and affects p130(Cas).Rational design for multifunctional non-liposomal lipid-based nanocarriers for cancer management: theory to practice.Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared studyProcess of inducing pores in membranes by melittinThe alignment of a voltage-sensing peptide in dodecylphosphocholine micelles and in oriented lipid bilayers by nuclear magnetic resonance and molecular modelingConformation and dynamics of melittin bound to magnetically oriented lipid bilayers by solid-state (31)P and (13)C NMR spectroscopy.Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane.Morphological behavior of lipid bilayers induced by melittin near the phase transition temperature.Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes.Voltage-gated channels formed in lipid bilayers by a positively charged segment of the Na-channel polypeptide.Proline-rich peptide from the coral pathogen Vibrio shiloi that inhibits photosynthesis of Zooxanthellae.Lipid membrane editing with peptide cargo linkers in cells and synthetic nanostructures.Production of human antibody fragments binding to melittin and phospholipase A2 in Africanised bee venom: minimising venom toxicity.X-ray scattering with momentum transfer in the plane of membrane. Application to gramicidin organizationConformation of spin-labeled melittin at membrane surfaces investigated by pulse saturation recovery and continuous wave power saturation electron paramagnetic resonance.Primary structure of peptides and ion channels. Role of amino acid side chains in voltage gating of melittin channelsThe nociceptive and anti-nociceptive effects of bee venom injection and therapy: a double-edged swordSupramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: method of analysis.Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR.Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores.Many-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formationAssociation of the wasp venom peptide mastoparan with electrically neutral lipid vesicles. Salt effects on partitioning and conformational state.Activation and inactivation of melittin channels.On the translocation of proteins across membranes.The structure of a melittin-stabilized poreConformational Fine-Tuning of Pore-Forming Peptide Potency and Selectivity.Charge distribution and imperfect amphipathicity affect pore formation by antimicrobial peptides.Template-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein.Role of nanoparticle surface functionality in the disruption of model cell membranesMechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptidesEvidence for neurotoxic activity of tat from human immunodeficiency virus type 1.Protection by chlorpromazine, albumin and bivalent cations against haemolysis induced by melittin, [Ala-14]melittin and whole bee venom.Synthesis and characterization of stable fluorocarbon nanostructures as drug delivery vehicles for cytolytic peptidesFree energies of molecular bound states in lipid bilayers: lethal concentrations of antimicrobial peptidesSingle-molecule visualization of dynamic transitions of pore-forming peptides among multiple transmembrane positions.
P2860
Q24650885-29A2CED4-B66B-4639-A10D-F9125883CCEFQ26749090-7B2380DA-6AD8-487E-848B-7C16311CB550Q28346167-5B9A48CE-A613-40E0-A6AD-30B4183A277CQ28346215-D7ABF0BF-9CF4-45BD-BE16-2F0CC861E33FQ28361996-7B32E134-9A26-4F78-8A22-B42DA081B817Q30176010-0CCCF60C-64A1-4490-B92D-97C4F542C1BFQ30436623-66CDD90B-9E34-4479-B679-11C22C06533DQ30447720-BD6CD5DE-AFEE-432D-916E-0C2BD6C8B113Q30544025-980A16C2-42BD-4B29-8A62-72B9E4D80A92Q30582344-D4675B04-6CF5-4D45-B518-D78667C886A3Q30861151-E8D4B2A7-43EB-4447-9505-A0EE9BAA1859Q32018430-A4612655-026F-43A2-AABB-4FC90C614B10Q33222050-63D8D897-48F6-4A2B-A686-3C9F57AEF86CQ33631782-B3763F5B-8DE5-47D5-B333-B427F868ED32Q33833047-066B1381-03E9-445E-8BFD-93045FB420B7Q33989236-759F5C8F-2847-4F9D-8EF8-5C05DE2B668AQ34017152-0957FF7F-E403-4B29-9E49-59CF6AF8336DQ34053852-F720B0A1-093F-4E9A-9005-2FAB1B4C5D09Q34092000-F001F034-637A-47DE-8D8C-430EDA0CBB2EQ34125315-89A9B4A9-B6F6-4405-986C-11A369BF77B8Q34126752-D1AD3B53-2FE4-49E3-B809-03AE88808DF9Q34157706-B99A3622-4910-45B4-9A74-BC3184F0E26FQ34171738-816D9D72-B7AD-4A9F-9181-71BC1492BBAEQ34187729-684B5B9A-01CE-47B9-A52B-FD63F7F4CA81Q34189385-3BA518B0-CE9B-44E0-9EF9-D54401BA97E6Q34352457-789DD4E5-D4C3-4A84-9259-85F69C9E2F5CQ34360903-DC234B74-E942-4AA8-8AB0-7314AD66BD4BQ34536125-55C4C919-7439-4B56-9DF4-F52A7AD20B2BQ34596724-6DCAB29F-15BB-4C26-BC0A-67A99EE70ADAQ35687054-CD584E8C-0F0F-4A89-B892-2074DC3038B6Q35859779-872444B4-5094-47EA-8B11-71F43A9EFFCFQ35869840-031CCC3B-7711-4B33-8008-F9FCDC608810Q36278341-32FF1440-B039-4F7F-A5DA-3F24EBD5844FQ36428290-121455FA-374B-4C3B-9C65-3C26952D3762Q36516117-EF6D242C-5DB4-4482-A22A-BA90EE550188Q36680591-BE830EA6-26EF-4A3B-8D2D-CBF19772132EQ36814077-0104C2D5-F10E-46D4-BFBB-C47F51F1855DQ37260780-5DCFB3E8-2CD0-403E-A4FB-87A31300DAA9Q37282305-FFF78C9F-9957-479D-8B2C-15E65CFB8613Q37324085-DF400530-8E10-4A7A-BDC4-5D58372C8045
P2860
description
1981 nî lūn-bûn
@nan
1981 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1981 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
name
The sting. Melittin forms channels in lipid bilayers.
@ast
The sting. Melittin forms channels in lipid bilayers.
@en
The sting. Melittin forms channels in lipid bilayers.
@nl
type
label
The sting. Melittin forms channels in lipid bilayers.
@ast
The sting. Melittin forms channels in lipid bilayers.
@en
The sting. Melittin forms channels in lipid bilayers.
@nl
prefLabel
The sting. Melittin forms channels in lipid bilayers.
@ast
The sting. Melittin forms channels in lipid bilayers.
@en
The sting. Melittin forms channels in lipid bilayers.
@nl
P2860
P1433
P1476
The sting. Melittin forms channels in lipid bilayers.
@en
P2093
D C Tosteson
M T Tosteson
P2860
P304
P356
10.1016/S0006-3495(81)84719-4
P407
P577
1981-10-01T00:00:00Z