Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant Gram-negative pathogens
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New Delhi Metallo-β-Lactamase-Mediated Carbapenem Resistance: Origin, Diagnosis, Treatment and Public Health ConcernVersatile roles of the chaperonin GroEL in microorganism-insect interactionsThe proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complexUltrashort cationic lipopeptides and lipopeptoids selectively induce cytokine production in macrophagesDnaK as Antibiotic Target: Hot Spot Residues Analysis for Differential Inhibition of the Bacterial Protein in Comparison with the Human HSP70Imaging the antimicrobial mechanism(s) of cathelicidin-2.Differential stability of therapeutic peptides with different proteolytic cleavage sites in blood, plasma and serumOptimization of oncocin for antibacterial activity using a SPOT synthesis approach: extending the pathogen spectrum to Staphylococcus aureus.Cell-Penetrating Peptides Selectively Cross the Blood-Brain Barrier In Vivo.Novel apidaecin 1b analogs with superior serum stabilities for treatment of infections by gram-negative pathogens.Structure of the mammalian antimicrobial peptide Bac7(1-16) bound within the exit tunnel of a bacterial ribosome.In vivo Efficacy and Pharmacokinetics of Optimized Apidaecin Analogs.Potentiating the Activity of Nisin against Escherichia coli.How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Recent advances on topical antimicrobials for skin and soft tissue infections and their safety concerns.Mechanism of Escherichia coli resistance to Pyrrhocoricin.Insect-derived short proline-rich and murine cathelicidin-related antimicrobial peptides act synergistically on Gram-negative bacteria in vitro.Antibacterial and anti-inflammatory activity of a temporin B peptide analogue on an in vitro model of cystic fibrosis.Immunogenicity and pharmacokinetics of short, proline-rich antimicrobial peptides.Screening and Optimizing Antimicrobial Peptides by Using SPOT-Synthesis.Intracellular toxicity of proline-rich antimicrobial peptides shuttled into mammalian cells by the cell-penetrating peptide penetratin.Ribosomal binding and antibacterial activity of ethylene glycol-bridged apidaecin Api137 and oncocin Onc112 conjugates.An atomistic view of Hsp70 allosteric crosstalk: from the nucleotide to the substrate binding domain and backShort Proline-Rich Antimicrobial Peptides Inhibit Either the Bacterial 70S Ribosome or the Assembly of its Large 50S Subunit.Oncocin Onc72 is efficacious against antibiotic-susceptible Klebsiella pneumoniae ATCC 43816 in a murine thigh infection model.Influence of the yjiL-mdtM Gene Cluster on the Antibacterial Activity of Proline-Rich Antimicrobial Peptides Overcoming Escherichia coli Resistance Induced by the Missing SbmA Transporter System.Insect-derived proline-rich antimicrobial peptides kill bacteria by inhibiting bacterial protein translation at the 70S ribosome.The Effect of Selective D- or Nα-Methyl Arginine Substitution on the Activity of the Proline-Rich Antimicrobial Peptide, Chex1-Arg20.Antibacterial and immunomodulatory activities of insect defensins-DLP2 and DLP4 against multidrug-resistant Staphylococcus aureus.Variation of the net charge, lipophilicity, and side chain flexibility in Dmt(1)-DALDA: Effect on Opioid Activity and Biodistribution.Vesicular disruption of lysosomal targeting organometallic polyarginine bioconjugates.Proline-rich antimicrobial peptides show a long-lasting post-antibiotic effect on Enterobacteriaceae and Pseudomonas aeruginosa.C-Terminal Modification and Multimerization Increase the Efficacy of a Proline-Rich Antimicrobial Peptide.Correlating uptake and activity of proline-rich antimicrobial peptides in Escherichia coli.Controlled systemic release of therapeutic peptides from PEGylated prodrugs by serum proteases.Insect antimicrobial peptides show potentiating functional interactions against Gram-negative bacteria.
P2860
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P2860
Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant Gram-negative pathogens
description
2012 nî lūn-bûn
@nan
2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
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
name
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@ast
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@en
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@nl
type
label
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@ast
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@en
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@nl
prefLabel
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@ast
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@en
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@nl
P2093
P3181
P356
P1433
P1476
Api88 is a novel antibacterial ...... istant Gram-negative pathogens
@en
P2093
Annegret Binas
Bart De Spiegeleer
Daniel Knappe
Gabriele Köhler
Gottfried Alber
Lisandra L Martin
Michael Zahn
Nicole Berthold
Nicole Herth
Oliver Nolte
P304
P3181
P356
10.1021/CB300063V
P577
2012-07-20T00:00:00Z