Antimicrobial activity of short arginine- and tryptophan-rich peptides.
about
Human Macrophage Inflammatory Protein 3 : Protein and Peptide Nuclear Magnetic Resonance Solution Structures, Dimerization, Dynamics, and Anti-Infective PropertiesDesign, synthesis and structure-activity relationship study of wollamide B; a new potential anti TB agent.Successful identification of novel agents to control infectious diseases from screening mixture-based peptide combinatorial libraries in complex cell-based bioassays.Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogues in solution and bound to detergent micelles.Surface-active fungicidal D-peptide inhibitors of the plasma membrane proton pump that block azole resistance.Limiting an antimicrobial peptide to the lipid-water interface enhances its bacterial membrane selectivity: a case study of MSI-367Synthesis and Antimicrobial Activities of His(2-aryl)-Arg and Trp-His(2-aryl) Classes of Dipeptidomimetics.A small peptide with therapeutic potential for inflammatory acne vulgarisSynthesis and antimicrobial activity of α-aminoboronic-containing peptidomimetics.Length effects in antimicrobial peptides of the (RW)n seriesMembrane-Active Small Molecules: Designs Inspired by Antimicrobial Peptides.Antifungal activity of (KW)n or (RW)n peptide against Fusarium solani and Fusarium oxysporumEffect of repetitive lysine-tryptophan motifs on the eukaryotic membrane.Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.The potential of antimicrobial peptides as biocides.Activity of a novel-designed antimicrobial peptide and its interaction with lipids.Position-Dependent Influence of the Three Trp Residues on the Membrane Activity of the Antimicrobial Peptide, Tritrpticin.Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity.Tuning the activity of a short arg-trp antimicrobial Peptide by lipidation of a C- or N-terminal lysine side-chain.Conformation of a bactericidal domain of puroindoline a: structure and mechanism of action of a 13-residue antimicrobial peptide.Short Synthetic β-Sheet Antimicrobial Peptides for the Treatment of Multidrug-Resistant Pseudomonas aeruginosa Burn Wound Infections.Variations in amino acid composition of antisense peptide-phosphorodiamidate morpholino oligomer affect potency against Escherichia coli in vitro and in vivo.Serum stabilities of short tryptophan- and arginine-rich antimicrobial peptide analogs.Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures.Development of novel ultrashort antimicrobial peptide nanoparticles with potent antimicrobial and antibiofilm activities against multidrug-resistant bacteria.Cloning and expression of antibacterial goat lactoferricin from Escherichia coli AD494(DE3)pLysS expression system.Novel Miniature Membrane Active Lipopeptidomimetics against Planktonic and Biofilm Embedded Methicillin-Resistant Staphylococcus aureus.Influence of the Multivalency of Ultrashort Arg-Trp-Based Antimicrobial Peptides (AMP) on Their Antibacterial Activity.DNA repair, a novel antibacterial target: Holliday junction-trapping peptides induce DNA damage and chromosome segregation defects.Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity.Exploring Structure-Activity Relationships in Synthetic Antimicrobial Peptides (synAMPs) by a Ferrocene ScanSynthesis and antibacterial activity of trivalent ultrashort Arg-Trp-based antimicrobial peptides (AMPs)
P2860
Q27649353-A54BC59C-8EAE-4D58-9BA9-273539F86DA3Q30313238-96B7B52A-5483-49FF-BCDC-A23F8ACF8311Q30937880-171B5D0F-8DE2-48A3-B0D3-576300331F8EQ30997917-0DB8D098-0861-4480-A86E-C1333021EF22Q31136813-C0723CE0-3E26-40F5-B01A-27B77CAB374CQ33742617-235CEDE9-A932-4A0C-A5FD-5BA0AA3DBE05Q33791478-2F18D917-311B-4390-B2F0-7E11DBBEA290Q34980992-CD394C36-B1CB-43D6-99B9-863100257FA9Q35039936-59254755-9D29-4754-BCDD-1772A27F3807Q35636002-84DB79C4-4C76-487B-9542-753CDDF42665Q35781198-92BB25ED-EF07-4FE0-A4D1-BF2648DA1070Q36432589-EDB4D1F9-4EEE-465C-9037-35B4424141FEQ36590199-4A1406A5-F76A-41F0-890D-9A2EFF43ADE9Q37639825-A451E326-980A-4BF8-BCBB-5013F93DD9B8Q37954604-CEF813EA-AF29-47DD-BA55-9AB945BC7585Q38909503-42EB5DA0-476F-40BC-B6CA-9C9F8044A029Q38977851-F82AB6B8-8022-4E7B-BF9F-FFB4C88CCF8BQ39447406-B1CF9E5A-FBBC-483F-9289-BE4BA210A9F0Q39731315-A926F580-EAD0-43C7-868A-ACD26D9C4C93Q39793865-ED83C1C4-AEC1-465A-98ED-C45CF2A8F645Q40353461-52D799CD-BAB6-45A4-9026-6D0AD42B9310Q41892217-D2D60617-723A-48DC-AF96-22B9FC413841Q41979383-B703B641-92AD-449E-900E-1FBED0FA5CECQ42989557-F918DEF7-77D8-4D6E-915A-F709B3274301Q44484590-225FA826-C356-49AB-A591-99768EE148D9Q46108192-189C04A3-D630-4E06-A317-7CF877854026Q48215377-90D9145E-C744-4405-9A1F-0A1E2AFF9E8CQ50441081-868A4AE0-6351-49AE-A2D6-9FC255FB6FA3Q53639530-DB7F6AA7-36FB-4B55-887D-90BA9CFA6A24Q54263518-902802FD-FCE2-4E19-A716-5D5111F59C45Q58915724-5032C0E1-145C-4AAD-8321-256F6B714D88Q58915855-47D9E25E-FAE7-41DE-BCEB-CE0AAFE850F2
P2860
Antimicrobial activity of short arginine- and tryptophan-rich peptides.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Antimicrobial activity of short arginine- and tryptophan-rich peptides.
@en
Antimicrobial activity of short arginine- and tryptophan-rich peptides.
@nl
type
label
Antimicrobial activity of short arginine- and tryptophan-rich peptides.
@en
Antimicrobial activity of short arginine- and tryptophan-rich peptides.
@nl
prefLabel
Antimicrobial activity of short arginine- and tryptophan-rich peptides.
@en
Antimicrobial activity of short arginine- and tryptophan-rich peptides.
@nl
P2860
P356
P1476
Antimicrobial activity of short arginine- and tryptophan-rich peptides.
@en
P2093
Morten B Strøm
Oystein Rekdal
P2860
P304
P356
10.1002/PSC.398
P577
2002-08-01T00:00:00Z