Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
about
A short guided tour through functional and structural features of saposin-like proteinsMacin Family of Antimicrobial Proteins Combines Antimicrobial and Nerve Repair ActivitiesStructure and function of a unique pore-forming protein from a pathogenic acanthamoebaCharacterization and function of the first antibiotic isolated from a vent organism: the extremophile metazoan Alvinella pompejanaGenome-wide identification of pathogenicity factors of the free-living amoeba Naegleria fowleri.Microbial challenge promotes the regenerative process of the injured central nervous system of the medicinal leech by inducing the synthesis of antimicrobial peptides in neurons and microglia.Identification of a Naegleria fowleri membrane protein reactive with anti-human CD59 antibody.Iron-Binding Protein Degradation by Cysteine Proteases of Naegleria fowleri.Introductory remarks: bacterial endosymbionts or pathogens of free-living amebae1.Ancient weapons for attack and defense: the pore-forming polypeptides of pathogenic enteric and free-living amoeboid protozoa.Host-parasite interaction: parasite-derived and -induced proteases that degrade human extracellular matrix.Proteases from Entamoeba spp. and Pathogenic Free-Living Amoebae as Virulence Factors.Pore-forming toxins from pathogenic amoebae.Nf-GH, a glycosidase secreted by Naegleria fowleri, causes mucin degradation: an in vitro and in vivo study.Induction of interleukin-8 by Naegleria fowleri lysates requires activation of extracellular signal-regulated kinase in human astroglial cells.The ameba Balamuthia mandrillaris feeds by entering into mammalian cells in culture.An efficient fluorimetric method to measure the viability of intraerythrocytic Plasmodium falciparum.Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: a comparative functional analysis.The antimicrobial peptide NK-2, the core region of mammalian NK-lysin, kills intraerythrocytic Plasmodium falciparum.Identification of peptidases in highly pathogenic vs. weakly pathogenic Naegleria fowleri amebae.IL-1β and IL-6 activate inflammatory responses of astrocytes against Naegleria fowleri infection via the modulation of MAPKs and AP-1.Antimicrobial and pore-forming peptides of free-living and potentially highly pathogenic Naegleria fowleri are released from the same precursor molecule.Modulation of a "CD59-like" protein in Naegleria fowleri amebae by bacteria.A biochemical comparison of proteases from pathogenic naegleria fowleri and non-pathogenic Naegleria gruberi.The Saposin-Like Protein AplD Displays Pore-Forming Activity and Participates in Defense Against Bacterial Infection During a Multicellular Stage of Dictyostelium discoideum.Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis.Organotypic slice cultures from rat brain tissue: a new approach for Naegleria fowleri CNS infection in vitro
P2860
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P2860
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
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
name
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
@ast
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
@en
type
label
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
@ast
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
@en
prefLabel
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
@ast
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
@en
P2093
P2860
P356
P1476
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
@en
P2093
Claudia Ott
Francine Marciano-Cabral
Rosa Herbst
Thomas Jacobs
Thomas Marti
P2860
P304
22353-22360
P356
10.1074/JBC.M201475200
P407
P577
2002-04-10T00:00:00Z