Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes.
about
From design to screening: a new antimicrobial peptide discovery pipelineSimulating the mechanism of antimicrobial lipopeptides with all-atom molecular dynamics.Bi- or multifunctional opioid peptide drugs.Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide.High-throughput selection of transmembrane sequences that enhance receptor tyrosine kinase activationHigh-throughput discovery of broad-spectrum peptide antibiotics.Broad-spectrum antimicrobial peptides by rational combinatorial design and high-throughput screening: the importance of interfacial activity.Describing the mechanism of antimicrobial peptide action with the interfacial activity modelProgressive structuring of a branched antimicrobial peptide on the path to the inner membrane targetGain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening.Synthetic molecular evolution of pore-forming peptides by iterative combinatorial library screening.pH Dependence of microbe sterilization by cationic antimicrobial peptidesA lipocentric view of peptide-induced pores.Toward the de novo design of antimicrobial peptides: Lack of correlation between peptide permeabilization of lipid vesicles and antimicrobial, cytolytic, or cytotoxic activity in living cells.Iterative antimicrobial candidate selection from informed d-/l-Peptide dimer libraries.Biophysical characterisation of calumenin as a charged F508del-CFTR folding modulatorExamination of bacterial inhibition using a catalytic DNAAntimicrobial activity of synthetic cationic peptides and lipopeptides derived from human lactoferricin against Pseudomonas aeruginosa planktonic cultures and biofilmsConformational Fine-Tuning of Pore-Forming Peptide Potency and Selectivity.PE and PS Lipids Synergistically Enhance Membrane Poration by a Peptide with Anticancer PropertiesReorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations.Determining the mechanism of membrane permeabilizing peptides: identification of potent, equilibrium pore-formersHemolytic activity of membrane-active peptides correlates with the thermodynamics of binding to 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayersMagainin 2 revisited: a test of the quantitative model for the all-or-none permeabilization of phospholipid vesicles.Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.A look at arginine in membranes.Antimicrobial peptides: successes, challenges and unanswered questions.Membrane-active host defense peptides--challenges and perspectives for the development of novel anticancer drugs.New trends in peptide-based anti-biofilm strategies: a review of recent achievements and bioinformatic approaches.Highly efficient macromolecule-sized poration of lipid bilayers by a synthetically evolved peptideSynergistic effects of the membrane actions of cecropin-melittin antimicrobial hybrid peptide BP100All-or-none versus graded: single-vesicle analysis reveals lipid composition effects on membrane permeabilization.Fluctuations and the rate-limiting step of peptide-induced membrane leakage.Rationale-based, de novo design of dehydrophenylalanine-containing antibiotic peptides and systematic modification in sequence for enhanced potency.Correlation between Membrane Partitioning and Functional Activity in a Single Lipid Vesicle Assay Establishes Design Guidelines for Antiviral Peptides.Pores formed by Baxα5 relax to a smaller size and keep at equilibriumSpontaneous membrane-translocating peptides by orthogonal high-throughput screening.Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.A lack of synergy between membrane-permeabilizing cationic antimicrobial peptides and conventional antibiotics.N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins.
P2860
Q28488283-B6F5472B-34C1-4ACC-9760-30F6A48C41CCQ33647074-39B90DCD-6EA4-4C50-8FF4-F3CD6AC17528Q33767037-AD87EB8B-3CB1-48A1-B8FD-B1A1162173BAQ33883192-DF3079E3-6196-49FD-A316-3A15933EDB42Q33964577-9AE844C2-831B-43D0-B80E-7F3F4566BE82Q34072246-BA69366D-B90F-40AA-8382-829BED5877EEQ34112173-1E23C9EB-22E5-419C-B70E-5F2D59C4F8D4Q34204118-AF172C4F-0DB6-4540-B34C-F7AA99B8D5B1Q34304804-F883C1E3-05DF-4637-B7D5-A62A2C2D0747Q34316505-EF61C288-675E-46A8-8326-9B6D02843FEBQ34581262-30A7ED15-5D8D-43D3-A58D-E5718416CF5DQ34708231-D0456133-EC49-4B5A-965A-13A9BAA1154CQ34757093-B1BBB6E1-2EF7-44B1-A75E-94CE86DCF1CDQ34871624-7DD7A5EB-B1FE-4223-93B2-DFECBD75750BQ35024514-50EF7ADB-F510-44CE-A66E-C9F0781C20ECQ35224227-075AA964-FBB4-4C2B-93F6-7BE87CF02C1FQ35532061-32EEF971-BE14-4EC7-8310-224A00AB8EF1Q35684711-E627D76E-B64E-4470-9C32-ADDB6BE8BBA6Q35859779-BC1BF24F-F6AC-43FD-8689-3CB0313D70E9Q36043823-C06BB999-F4AD-4016-A758-5F9DB0E03CCEQ36150814-3AB3ED13-5BCC-4EEB-962A-59401135D1EFQ36191769-576D0C0C-E734-4564-80EF-549A619D05F9Q36645121-0EA0E4F4-AD1A-4FB6-9452-2A0A2B2B8E01Q37260254-6B7DCD1C-5A88-4009-9716-3186F5A89D21Q37414152-17C40D2B-4845-4047-A515-3AD849768819Q37812274-26EFDC25-989B-4334-909A-FE367EE5144BQ37827731-0897F612-316C-4C21-A9CF-CA4094E915C5Q37938364-78B0CD41-626F-4D27-A132-9E514FF2CBA3Q38047034-5C760085-63C5-42EA-8DE7-E31CA1F2FFAEQ38732263-D73E589B-CB5C-4540-9AD4-1C69ED1E04C3Q39878043-EDF0FF9C-15DE-42F6-A02C-4E7FD5ECAD82Q41152752-F0406E13-0D45-41B5-B892-326BF4F5CBC2Q41962682-22C101E3-0BFE-4A85-BCB0-2DFBFA0F91ADQ42067261-EAA638BA-9FF5-4183-9ACC-A5F7404EC589Q42174162-7E5BCD61-BA9B-47F5-9813-D2CF0B66CDE9Q42183300-7F59ADCD-0271-47A9-B9A4-8F00E427F13CQ42254224-2E43005B-9DDA-4C19-819A-C81224D0EDFBQ42425941-414C1FE6-BB86-4E8D-B52F-B0E1AAE2C817Q42535527-CB1C8D62-D75B-44F4-B976-D044EF0F0220Q45516984-02003671-C30C-4EF8-9D76-49B10C6A383F
P2860
Biomolecular engineering by combinatorial design and high-throughput screening: small, soluble peptides that permeabilize membranes.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Biomolecular engineering by co ...... s that permeabilize membranes.
@ast
Biomolecular engineering by co ...... s that permeabilize membranes.
@en
type
label
Biomolecular engineering by co ...... s that permeabilize membranes.
@ast
Biomolecular engineering by co ...... s that permeabilize membranes.
@en
prefLabel
Biomolecular engineering by co ...... s that permeabilize membranes.
@ast
Biomolecular engineering by co ...... s that permeabilize membranes.
@en
P2860
P356
P1476
Biomolecular engineering by co ...... s that permeabilize membranes.
@en
P2093
Ramesh Rathinakumar
William C Wimley
P2860
P304
P356
10.1021/JA8017863
P407
P577
2008-07-09T00:00:00Z