Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5
about
Peptides and Peptidomimetics for Antimicrobial Drug DesignNovel formulations for antimicrobial peptidesNMR Solution Structure and Condition-Dependent Oligomerization of the Antimicrobial Peptide Human Defensin 5Functional Determinants of Human Enteric -Defensin HD5: CRUCIAL ROLE FOR HYDROPHOBICITY AT DIMER INTERFACEStructural insights into Cn-AMP1, a short disulfide-free multifunctional peptide from green coconut waterHydrophobic determinants of α-defensin bactericidal activity.The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption.Comparative genomics and evolution of the alpha-defensin multigene family in primatesInflammatory bowel disease: an impaired barrier disease.Arginine-specific mono ADP-ribosylation in vitro of antimicrobial peptides by ADP-ribosylating toxinsStructure-activity relationship study of novel peptoids that mimic the structure of antimicrobial peptides.Critical determinants of human α-defensin 5 activity against non-enveloped viruses.Arginine-rich self-assembling peptides as potent antibacterial gelsEnhancement of antiviral activity of human alpha-defensin 5 against herpes simplex virus 2 by arginine mutagenesis at adaptive evolution sites.Neutrophil-derived alpha defensins control inflammation by inhibiting macrophage mRNA translation.Pro-inflammatory and pro-apoptotic properties of Human Defensin 5.The human alpha defensin HD5 neutralizes JC polyomavirus infection by reducing endoplasmic reticulum traffic and stabilizing the viral capsid.Antimicrobial hydrogels for the treatment of infection.Innate antimicrobial immunity in inflammatory bowel diseases.α-Defensins in human innate immunity.Structural and Functional Consequences Induced by Post-Translational Modifications in α-Defensins.α-Defensin HD5 Inhibits Human Papillomavirus 16 Infection via Capsid Stabilization and Redirection to the LysosomeTargeting and inactivation of bacterial toxins by human defensins.Prediction of the impact of coding missense and nonsense single nucleotide polymorphisms on HD5 and HBD1 antibacterial activity against Escherichia coli.Advances in the Fabrication of Antimicrobial Hydrogels for Biomedical ApplicationsVisualizing attack of Escherichia coli by the antimicrobial peptide human defensin 5.Antimicrobial peptides in gastrointestinal inflammationExpression and structure/function relationships of human defensin 5.Paneth's disease.
P2860
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P2860
Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Selective arginines are import ...... tion of human alpha-defensin 5
@ast
Selective arginines are import ...... tion of human alpha-defensin 5
@en
Selective arginines are import ...... tion of human alpha-defensin 5
@nl
type
label
Selective arginines are import ...... tion of human alpha-defensin 5
@ast
Selective arginines are import ...... tion of human alpha-defensin 5
@en
Selective arginines are import ...... tion of human alpha-defensin 5
@nl
prefLabel
Selective arginines are import ...... tion of human alpha-defensin 5
@ast
Selective arginines are import ...... tion of human alpha-defensin 5
@en
Selective arginines are import ...... tion of human alpha-defensin 5
@nl
P2093
P2860
P1433
P1476
Selective arginines are import ...... tion of human alpha-defensin 5
@en
P2093
Erik de Leeuw
Guozhang Zou
Marzena Pazgier
Mohsen Rajabi
P2860
P304
P356
10.1016/J.FEBSLET.2009.06.051
P407
P577
2009-08-06T00:00:00Z