Ab initio design of potent anti-MRSA peptides based on database filtering technology.
about
Evidence for Phenylalanine Zipper-Mediated Dimerization in the X-ray Crystal Structure of a Magainin 2 AnalogueHigh-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments.Insights into Antimicrobial Peptides from Spiders and ScorpionsDRAMP: a comprehensive data repository of antimicrobial peptides.Ternary nylon-3 copolymers as host-defense peptide mimics: beyond hydrophobic and cationic subunits.Improved methods for classification, prediction, and design of antimicrobial peptides.Host defense antimicrobial peptides as antibiotics: design and application strategies.APD3: the antimicrobial peptide database as a tool for research and education.Natural antimicrobial peptides as promising anti-HIV candidates.Database-Guided Discovery of Potent Peptides to Combat HIV-1 or SuperbugsMembrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Using Diphenylphosphoryl Azide (DPPA) for the Facile Synthesis of Biodegradable Antiseptic Random Copolypeptides.Computational resources and tools for antimicrobial peptides.Next-generation precision antimicrobials: towards personalized treatment of infectious diseases.Resurrecting inactive antimicrobial peptides from the lipopolysaccharide trap.Individual and Combined Effects of Engineered Peptides and Antibiotics on Pseudomonas aeruginosa Biofilms.Design and surface immobilization of short anti-biofilm peptides.Combined Bioinformatic and Rational Design Approach To Develop Antimicrobial Peptides against Mycobacterium tuberculosis.Highly potent antimicrobial peptides from N-terminal membrane-binding region of E. coli MreB.Characterization of Antimicrobial Peptides toward the Development of Novel Antibiotics.Small lipopeptides possess anti-biofilm capability comparable to daptomycin and vancomycinStructural location determines functional roles of the basic amino acids of KR-12, the smallest antimicrobial peptide from human cathelicidin LL-37.Interplay among subunit identity, subunit proportion, chain length, and stereochemistry in the activity profile of sequence-random peptide mixtures.Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds.Arginine-lysine positional swap of the LL-37 peptides reveals evolutional advantages of the native sequence and leads to bacterial probes.Small molecule mimics of DFTamP1, a database designed anti-Staphylococcal peptide.Emerging Nanomedicine Therapies to Counter the Rise of Methicillin-Resistant Staphylococcus aureus.
P2860
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P2860
Ab initio design of potent anti-MRSA peptides based on database filtering technology.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Ab initio design of potent anti-MRSA peptides based on database filtering technology.
@en
Ab initio design of potent anti-MRSA peptides based on database filtering technology.
@nl
type
label
Ab initio design of potent anti-MRSA peptides based on database filtering technology.
@en
Ab initio design of potent anti-MRSA peptides based on database filtering technology.
@nl
prefLabel
Ab initio design of potent anti-MRSA peptides based on database filtering technology.
@en
Ab initio design of potent anti-MRSA peptides based on database filtering technology.
@nl
P2860
P356
P1476
Ab initio design of potent anti-MRSA peptides based on database filtering technology.
@en
P2093
Biswajit Mishra
Guangshun Wang
P2860
P304
12426-12429
P356
10.1021/JA305644E
P407
P577
2012-07-19T00:00:00Z